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Ribonuclease

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is a type of ribonuclease that cleaves rRNA (16s rRNA and 23s rRNA) from transcribed polycistronic RNA operon in prokaryotes. It also digests double-stranded RNA (dsRNA)-Dicer family of RNAse, cutting pre-miRNA (60–70bp long) at a specific site and transforming it in miRNA (22–30bp), that is actively
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is a ribonuclease of plant origin, which modulates SOS responses in bacteria, for a response to the stress of DNA damage by activation of the SOS mechanism by the RecA/LexA dependent signal transduction pathway that transcriptionally depresses a multiplicity of genes leading
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Some cells also secrete copious quantities of non-specific RNases such as A and T1. RNases are, therefore, extremely common, resulting in very short lifespans for any RNA that is not in a protected environment. It is worth noting that all intracellular RNAs are protected from RNase activity by a
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All organisms studied contain many RNases of two different classes, showing that RNA degradation is a very ancient and important process. As well as clearing of cellular RNA that is no longer required, RNases play key roles in the maturation of all RNA molecules, both messenger RNAs that carry
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The active site looks like a rift valley where all the active site residues create the wall and bottom of the valley. The rift is very thin and the small substrate fits perfectly in the middle of the active site, which allows for perfect interaction with the residues. It actually has a little
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genetic material for making proteins and non-coding RNAs that function in varied cellular processes. In addition, active RNA degradation systems are the first defense against RNA viruses and provide the underlying machinery for more advanced cellular immune strategies such as
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is a ribonuclease that cleaves the RNA in a DNA/RNA duplex to produce ssDNA. RNase H is a non-specific endonuclease and catalyzes the cleavage of RNA via a hydrolytic mechanism, aided by an enzyme-bound divalent metal ion. RNase H leaves a 5'-phosphorylated
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It is involved in processing the 16'-end of the 5s rRNA. It is related to chromosome separation and cell division. It is considered one of the components of cytoplasmic axial filament bundles. It is also thought that it can regulate the formation of this
1248:. It is specific for single-stranded RNAs. It cleaves the 3'-end of unpaired C and U residues, ultimately forming a 3'-phosphorylated product via a 2',3'-cyclic monophosphate intermediate. It does not require any cofactors for its activity 1616:. In addition to the cellular RNases that are released, there are several RNases that are present in the environment. RNases have evolved to have many extracellular functions in various organisms. For example, RNase 7, a member of the 1611:
in molecular biology experiments is greatly complicated by the presence of ubiquitous and hardy ribonucleases that degrade RNA samples. Certain RNases can be extremely hardy and inactivating them is difficult compared to neutralizing
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Wachi M, Umitsuki G, Shimizu M, Takada A, Nagai K. Escherichia coli cafA gene encodes a novel RNase, designated as RNase G, involved in processing of the 5' end of 16S rRNA. Biochem Biophys Res Commun. 1999;259(2):483‐488.
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for the RI-RNase A complex is ~20 fM under physiological conditions. RI is used in most laboratories that study RNA to protect their samples against degradation from environmental RNases.
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Shamsher S. Kanwar*, Puranjan Mishra, Khem Raj Meena, Shruti Gupta and Rakesh Kumar, Ribonucleases and their Applications, 2016, Journal of Advanced Biotechnology and Bioengineering
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Noguchi S (July 2010). "Isomerization mechanism of aspartate to sexxxxxxxx implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate".
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superfamily, is secreted by human skin and serves as a potent antipathogen defence. In these secreted RNases, the enzymatic RNase activity may not even be necessary for its new,
1244:​) is one of the hardiest enzymes in common laboratory usage; one method of isolating it is to boil a crude cellular extract until all enzymes other than RNase A are 2988: 1150:, which comprises a relatively large fraction of cellular protein (~0.1%) in some cell types, and which binds to certain ribonucleases with the highest affinity of any 2934: 2326:
Ahmed TAE, Udenigwe CC, Gomaa A. Editorial: Biotechnology and Bioengineering Applications for Egg-Derived Biomaterials. Front Bioeng Biotechnol. 2021 Sep 20;9:756058
147: 1731:"Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution" 2596: 1111:, and comprise several sub-classes within the EC 2.7 (for the phosphorolytic enzymes) and 3.1 (for the hydrolytic enzymes) classes of enzymes. 2757: 2414: 1595:
curvature to the site which the substrate also has. Although usually most exo- and endoribonucleases are not sequence specific, recently
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is a close homolog of RNase II, but it can, unlike RNase II, degrade RNA with secondary structures without help of accessory factors.
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Tamulaitis G, Kazlauskiene M, Manakova E, Venclovas Č, Nwokeoji AO, Dickman MJ, Horvath P, Siksnys V (November 2014).
3226: 2797: 2586: 1894:"RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme" 1373:
is sequence specific for single-stranded RNAs. It cleaves 3'-end of all 4 residues, but preferentially 3'-end of As.
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Gerdes K, Christensen SK and Lobner-Olesen A (2005). "Prokaryotic toxin-antitoxin stress response loci".
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that recognize and cleave specific sequences of single-stranded RNA have been recently classified.
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is sequence specific for single-stranded RNAs. It cleaves 3'-end of unpaired A and U residues.
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Huang YC, Lin YM, Chang TW, Wu SJ, Lee YS, Chang MD, Chen C, Wu SH, Liao YD (February 2007).
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function. For example, immune RNases act by destabilizing the cell membranes of bacteria.
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is an interferon-induced nuclease that, upon activation, destroys all RNA within the cell
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is sequence specific for single-stranded RNAs. It cleaves 3'-end of unpaired A residues.
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is sequence specific for single-stranded RNAs. It cleaves 3'-end of unpaired G residues.
3542: 3537: 3269: 3173: 3025: 2506: 2496: 2374: 2307: 2282: 2217: 2182: 2122: 2070: 2045: 2021: 1994: 1869: 1844: 1806: 1782:"Bovine pancreatic ribonuclease: fifty years of the first enzymatic reaction mechanism" 1781: 1757: 1730: 1581: 1193: 1162: 2974: 2919: 2887: 2762: 2481: 2312: 2263: 2222: 2163: 2114: 2075: 2026: 1975: 1915: 1874: 1811: 1762: 1709: 1682: 1657: 1566: 1551: 1236: 1137: 174: 142: 100: 2142:"RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin" 2126: 76: 3315: 3310: 3284: 3212: 3050: 2630: 2535: 2530: 2486: 2302: 2294: 2253: 2212: 2202: 2153: 2106: 2065: 2057: 2016: 2006: 1965: 1905: 1892:
Holzmann J, Frank P, Löffler E, Bennett KL, Gerner C, Rossmanith W (October 2008).
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to transit arrest of cell division as well as initiation of DNA repair.
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Köten B, Simanski M, GlÀser R, Podschun R, Schröder JM, Harder J (July 2009).
2110: 1653: 3521: 3305: 3264: 2866: 2775: 2525: 1136:, formation of an RNA·RNA duplex, and folding within an RNA protein complex ( 49: 3254: 2993: 2647: 2568: 2316: 2267: 2258: 2241: 2226: 2183:"RNase 7 contributes to the cutaneous defense against Enterococcus faecium" 2167: 2158: 2141: 2118: 2079: 2030: 2011: 1979: 1919: 1878: 1860: 1815: 1766: 1661: 1525: 1177: 2095:"The RNase a superfamily: generation of diversity and innate host defense" 104: 3478: 3413: 3249: 3168: 2939: 2833: 2696: 2662: 2600: 1540:
is the major contributor for the 3'-to-5' maturation of many stable RNAs.
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degrades single-stranded RNA from 5'-to-3', exists only in eukaryotes.
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RNases play a critical role in many biological processes, including
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involved in the regulation of transcription and mRNA life-time.
162: 1845:"Retroviral integrase superfamily: the structural perspective" 3439: 3072: 2823: 2819: 2046:"T2 Family ribonucleases: ancient enzymes with diverse roles" 1613: 1602: 1165:, which cleave highly specific sequences of double-stranded 1103:
into smaller components. Ribonucleases can be divided into
2804: 2681: 2674: 2618: 2613: 2283:"RNase A ribonucleases and host defense: an evolving story" 2180: 1891: 1320: 1188:(angiosperms). Many stress-response toxins of prokaryotic 1121: 124: 71: 3204: 1945: 1209: 1312: 1307:
is a type of ribonuclease that is unique in that it is a
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is an RNase that is commonly used in research. RNase A (
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and does not contain RNA has recently been discovered.
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Class of enzyme that catalyzes the degradation of RNA
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Cuchillo CM, Nogués MV, Raines RT (September 2011).
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degrades short oligonucleotides to mononucleotides.
1204: 1722: 1439: 2692:Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase 2396: 1728: 3519: 1729:Ramage HR, Connolly LE, Cox JS (December 2009). 1403:is specific for polyadenine and polyuridine RNA. 2239: 1668: 2139: 1993:Rossier O, Dao J, Cianciotto NP (March 2009). 1524:is involved in the 3'-to-5' processing of pre- 1315:that acts as a catalyst in the same way as an 3220: 2382: 2092: 2043: 1678:Peptide Growth Factors and Their Receptors II 1674: 1695: 1192:have been shown to have RNase activity and 3227: 3213: 2389: 2375: 1836: 1633: 38: 2306: 2280: 2257: 2216: 2206: 2157: 2069: 2020: 2010: 1969: 1909: 1868: 1805: 1756: 1746: 1705:Developmental Biology of Flowering Plants 1603:RNase contamination during RNA extraction 2335:D'Alessio G and Riordan JF, eds. (1997) 1701: 1675:Sporn MB, Roberts AB (6 December 2012). 1585:is a close homolog of Exoribonuclease I. 1208: 2582:Ubiquitin carboxy-terminal hydrolase L1 2337:Ribonucleases: Structures and Functions 2140:Harder J, Schroder JM (November 2002). 2093:Dyer KD, Rosenberg HF (November 2006). 1842: 1639: 14: 3520: 3208: 3162:either deoxy- or ribo-     2370: 2362:Integrated Enzyme Database for EC 3.1 1457:Polynucleotide Phosphorylase (PNPase) 2743:Protein serine/threonine phosphatase 1589: 1234:, bovine pancreatic ribonuclease A: 2844:Cyclic nucleotide phosphodiesterase 2838:Clostridium perfringens alpha toxin 2639:Tartrate-resistant acid phosphatase 2246:The Journal of Biological Chemistry 2146:The Journal of Biological Chemistry 1143:Another mechanism of protection is 47:Ribonuclease U2 with AMP PDB entry 24: 2687:Pyruvate dehydrogenase phosphatase 25: 3554: 2587:4-hydroxybenzoyl-CoA thioesterase 2350: 1199: 3505: 2357:IUBMB Enzyme Database for EC 3.1 2044:Luhtala N, Parker R (May 2010). 1205:Major types of endoribonucleases 2905:N-acetylglucosamine-6-sulfatase 2793:Sphingomyelin phosphodiesterase 2274: 2233: 2174: 2133: 2086: 2037: 1986: 1935: 1440:Major types of exoribonucleases 1128:number of strategies including 2714:Inositol-phosphate phosphatase 2577:Palmitoyl protein thioesterase 2050:Trends in Biochemical Sciences 1926: 1885: 1822: 1773: 1702:Raghavan V (6 December 2012). 13: 1: 3077:RNA-induced silencing complex 1627: 119:Available protein structures: 3181:Serratia marcescens nuclease 2748:Dual-specificity phosphatase 2738:Protein tyrosine phosphatase 2287:Journal of Leukocyte Biology 2208:10.1371/journal.pone.0006424 1971:10.1016/j.molcel.2014.09.027 1748:10.1371/journal.pgen.1000767 7: 3234: 2658:Fructose 1,6-bisphosphatase 1843:Nowotny M (February 2009). 1152:protein-protein interaction 1114: 10: 3559: 2329: 2062:10.1016/j.tibs.2010.02.002 1942:doi:10.1006/bbrc.1999.0806 1911:10.1016/j.cell.2008.09.013 1830:"Library Preparation Kits" 3391: 3383:Michaelis–Menten kinetics 3355: 3324: 3293: 3242: 3161: 3049: 3001: 2987: 2965: 2947: 2933: 2913: 2895:Galactosamine-6 sulfatase 2852: 2756: 2595: 2563: 2451:6-phosphogluconolactonase 2413: 2281:Rosenberg HF (May 2008). 2111:10.1007/s11030-006-9028-2 1654:10.1107/S0907444910019621 173: 161: 141: 123: 118: 114: 94: 82: 70: 62: 57: 37: 32: 3275:Diffusion-limited enzyme 2643:Purple acid phosphatases 1642:Acta Crystallographica D 1190:toxin-antitoxin systems 3068:Microprocessor complex 2707:Beta-propeller phytase 2259:10.1074/jbc.M607321200 2159:10.1074/jbc.M207587200 2012:10.1099/mic.0.023218-0 1861:10.1038/embor.2008.256 1492:nucleotidyltransferase 1466:nucleotidyltransferase 1214: 1146:ribonuclease inhibitor 1087:(commonly abbreviated 3368:Eadie–Hofstee diagram 3301:Allosteric regulation 3003:Endodeoxyribonuclease 2900:Iduronate-2-sulfatase 2653:Glucose 6-phosphatase 2439:Butyrylcholinesterase 1212: 1156:dissociation constant 3378:Lineweaver–Burk plot 3186:Micrococcal nuclease 3021:Deoxyribonuclease IV 3016:Deoxyribonuclease II 2949:Exodeoxyribonuclease 2609:Alkaline phosphatase 2434:Acetylcholinesterase 2344:Nat. Rev. Microbiol. 1213:Structure of RNase A 1182:self-incompatibility 45:Ustilago sphaerogena 3041:UvrABC endonuclease 3011:Deoxyribonuclease I 2734:Protein phosphatase 2670:Protein phosphatase 2468:Bile salt-dependent 2456:PAF acetylhydrolase 2299:10.1189/jlb.1107725 2199:2009PLoSO...4.6424K 2099:Molecular Diversity 1163:restriction enzymes 1099:the degradation of 3337:Enzyme superfamily 3270:Enzyme promiscuity 3174:Mung bean nuclease 3033:Restriction enzyme 3026:Restriction enzyme 1582:Exoribonuclease II 1215: 1140:particle or RNP). 3493: 3492: 3202: 3201: 3198: 3197: 3194: 3193: 2983: 2982: 2975:Oligonucleotidase 2920:deoxyribonuclease 2888:Steroid sulfatase 2763:Phosphodiesterase 2492:Hormone-sensitive 2339:, Academic Press. 1798:10.1021/bi201075b 1715:978-1-4612-1234-8 1688:978-3-642-74781-6 1609:extraction of RNA 1590:RNase specificity 1567:Exoribonuclease I 1552:Oligoribonuclease 1171:endoribonucleases 1138:ribonucleoprotein 1105:endoribonucleases 1082: 1081: 1078: 1077: 168:structure summary 16:(Redirected from 3550: 3510: 3509: 3501: 3373:Hanes–Woolf plot 3316:Enzyme activator 3311:Enzyme inhibitor 3285:Enzyme catalysis 3229: 3222: 3215: 3206: 3205: 3051:Endoribonuclease 3037: 3031: 2999: 2998: 2945: 2944: 2931: 2930: 2631:Acid phosphatase 2512:Monoacylglycerol 2422:ester hydrolases 2391: 2384: 2377: 2368: 2367: 2321: 2320: 2310: 2278: 2272: 2271: 2261: 2237: 2231: 2230: 2220: 2210: 2178: 2172: 2171: 2161: 2152:(48): 46779–84. 2137: 2131: 2130: 2090: 2084: 2083: 2073: 2041: 2035: 2034: 2024: 2014: 2005:(Pt 3): 882–90. 1990: 1984: 1983: 1973: 1949: 1943: 1939: 1933: 1930: 1924: 1923: 1913: 1889: 1883: 1882: 1872: 1840: 1834: 1833: 1826: 1820: 1819: 1809: 1777: 1771: 1770: 1760: 1750: 1741:(12): e1000767. 1726: 1720: 1719: 1699: 1693: 1692: 1672: 1666: 1665: 1637: 1486:functions as an 1460:functions as an 1313:ribonucleic acid 1243: 1186:flowering plants 1109:exoribonucleases 1073: 1067: 1060: 1054: 1048: 1042: 1036: 1030: 1024: 1018: 1012: 1006: 1000: 994: 988: 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2918: 2909: 2883:Arylsulfatase L 2878:Arylsulfatase B 2873:Arylsulfatase A 2848: 2761: 2752: 2591: 2559: 2421: 2409: 2395: 2353: 2332: 2324: 2279: 2275: 2238: 2234: 2179: 2175: 2138: 2134: 2091: 2087: 2042: 2038: 1991: 1987: 1950: 1946: 1940: 1936: 1931: 1927: 1890: 1886: 1841: 1837: 1828: 1827: 1823: 1792:(37): 7835–41. 1778: 1774: 1727: 1723: 1716: 1700: 1696: 1689: 1673: 1669: 1648:(Pt 7): 843–9. 1638: 1634: 1630: 1605: 1592: 1442: 1235: 1207: 1202: 1169:, a variety of 1134:polyadenylation 1117: 1091:) is a type of 1069: 1063: 1056: 1050: 1044: 1038: 1032: 1026: 1020: 1014: 1008: 1002: 996: 990: 984: 978: 972: 966: 960: 954: 948: 942: 936: 930: 924: 918: 912: 906: 900: 894: 888: 882: 876: 870: 864: 858: 852: 846: 840: 834: 828: 822: 816: 810: 804: 798: 792: 786: 780: 774: 768: 762: 756: 750: 744: 738: 732: 726: 720: 714: 708: 702: 696: 690: 684: 678: 672: 666: 660: 654: 648: 642: 636: 630: 624: 618: 612: 606: 600: 594: 588: 582: 576: 570: 564: 558: 552: 546: 540: 534: 528: 522: 516: 510: 504: 498: 492: 486: 480: 474: 468: 462: 456: 450: 444: 438: 432: 426: 420: 414: 408: 402: 396: 390: 384: 378: 372: 366: 360: 354: 348: 342: 336: 330: 324: 318: 312: 306: 300: 294: 288: 282: 276: 270: 264: 258: 252: 246: 240: 234: 228: 222: 216: 210: 204: 198: 191: 185: 179: 53: 48: 28: 23: 22: 15: 12: 11: 5: 3556: 3546: 3545: 3540: 3535: 3530: 3515: 3514: 3491: 3490: 3488: 3487: 3474: 3461: 3448: 3435: 3422: 3409: 3395: 3393: 3389: 3388: 3386: 3385: 3380: 3375: 3370: 3365: 3359: 3357: 3353: 3352: 3350: 3349: 3344: 3339: 3334: 3328: 3326: 3325:Classification 3322: 3321: 3319: 3318: 3313: 3308: 3303: 3297: 3295: 3291: 3290: 3288: 3287: 3282: 3277: 3272: 3267: 3262: 3257: 3252: 3246: 3244: 3240: 3239: 3232: 3231: 3224: 3217: 3209: 3200: 3199: 3196: 3195: 3192: 3191: 3189: 3188: 3183: 3178: 3177: 3176: 3165: 3163: 3159: 3158: 3156: 3155: 3150: 3149: 3148: 3143: 3138: 3133: 3123: 3118: 3113: 3108: 3107: 3106: 3101: 3096: 3091: 3081: 3080: 3079: 3070: 3055: 3053: 3047: 3046: 3044: 3043: 3038: 3023: 3018: 3013: 3007: 3005: 2996: 2985: 2984: 2981: 2980: 2978: 2977: 2971: 2969: 2963: 2962: 2960: 2959: 2953: 2951: 2942: 2928: 2911: 2910: 2908: 2907: 2902: 2897: 2892: 2891: 2890: 2885: 2880: 2875: 2862: 2860: 2850: 2849: 2847: 2846: 2841: 2831: 2826: 2817: 2812: 2807: 2802: 2801: 2800: 2790: 2789: 2788: 2783: 2773: 2767: 2765: 2754: 2753: 2751: 2750: 2745: 2740: 2731: 2730: 2729: 2711: 2710: 2709: 2699: 2694: 2689: 2684: 2679: 2678: 2677: 2667: 2666: 2665: 2655: 2650: 2645: 2628: 2627: 2626: 2621: 2616: 2605: 2603: 2593: 2592: 2590: 2589: 2584: 2579: 2573: 2571: 2561: 2560: 2558: 2557: 2552: 2546: 2545: 2544: 2543: 2538: 2533: 2522: 2521: 2520: 2519: 2517:Diacylglycerol 2514: 2509: 2504: 2499: 2494: 2489: 2484: 2479: 2470: 2459: 2458: 2453: 2448: 2446:Pectinesterase 2443: 2442: 2441: 2436: 2429:Cholinesterase 2425: 2423: 2411: 2410: 2394: 2393: 2386: 2379: 2371: 2365: 2364: 2359: 2352: 2351:External links 2349: 2348: 2347: 2340: 2331: 2328: 2323: 2322: 2293:(5): 1079–87. 2273: 2252:(7): 4626–33. 2232: 2173: 2132: 2085: 2036: 1985: 1958:Molecular Cell 1944: 1934: 1925: 1884: 1835: 1821: 1772: 1721: 1714: 1694: 1687: 1667: 1631: 1629: 1626: 1604: 1601: 1591: 1588: 1587: 1586: 1571: 1556: 1541: 1529: 1507: 1495: 1469: 1441: 1438: 1437: 1436: 1420: 1404: 1389: 1374: 1359: 1344: 1332: 1293: 1281: 1265: 1249: 1206: 1203: 1201: 1200:Classification 1198: 1130:5' end capping 1116: 1113: 1080: 1079: 1076: 1075: 177: 171: 170: 165: 159: 158: 145: 139: 138: 128: 121: 120: 112: 111: 98: 92: 91: 86: 80: 79: 74: 68: 67: 64: 60: 59: 55: 54: 43: 35: 34: 26: 9: 6: 4: 3: 2: 3555: 3544: 3541: 3539: 3536: 3534: 3531: 3529: 3528:Ribonucleases 3526: 3525: 3523: 3513: 3508: 3503: 3502: 3499: 3485: 3481: 3480: 3475: 3472: 3468: 3467: 3462: 3459: 3455: 3454: 3449: 3446: 3442: 3441: 3436: 3433: 3429: 3428: 3423: 3420: 3416: 3415: 3410: 3407: 3403: 3402: 3397: 3396: 3394: 3390: 3384: 3381: 3379: 3376: 3374: 3371: 3369: 3366: 3364: 3361: 3360: 3358: 3354: 3348: 3345: 3343: 3342:Enzyme family 3340: 3338: 3335: 3333: 3330: 3329: 3327: 3323: 3317: 3314: 3312: 3309: 3307: 3306:Cooperativity 3304: 3302: 3299: 3298: 3296: 3292: 3286: 3283: 3281: 3278: 3276: 3273: 3271: 3268: 3266: 3265:Oxyanion hole 3263: 3261: 3258: 3256: 3253: 3251: 3248: 3247: 3245: 3241: 3237: 3230: 3225: 3223: 3218: 3216: 3211: 3210: 3207: 3187: 3184: 3182: 3179: 3175: 3172: 3171: 3170: 3167: 3166: 3164: 3160: 3154: 3151: 3147: 3144: 3142: 3139: 3137: 3134: 3132: 3129: 3128: 3127: 3124: 3122: 3119: 3117: 3114: 3112: 3109: 3105: 3102: 3100: 3097: 3095: 3092: 3090: 3087: 3086: 3085: 3082: 3078: 3074: 3071: 3069: 3065: 3062: 3061: 3060: 3057: 3056: 3054: 3052: 3048: 3042: 3039: 3034: 3027: 3024: 3022: 3019: 3017: 3014: 3012: 3009: 3008: 3006: 3004: 3000: 2997: 2995: 2990: 2986: 2976: 2973: 2972: 2970: 2968: 2964: 2958: 2955: 2954: 2952: 2950: 2946: 2943: 2941: 2936: 2932: 2929: 2926: 2921: 2916: 2912: 2906: 2903: 2901: 2898: 2896: 2893: 2889: 2886: 2884: 2881: 2879: 2876: 2874: 2871: 2870: 2869: 2868: 2867:arylsulfatase 2864: 2863: 2861: 2859: 2855: 2851: 2845: 2842: 2839: 2835: 2832: 2830: 2827: 2825: 2821: 2818: 2816: 2813: 2811: 2808: 2806: 2803: 2799: 2796: 2795: 2794: 2791: 2787: 2784: 2782: 2779: 2778: 2777: 2776:Phospholipase 2774: 2772: 2769: 2768: 2766: 2764: 2759: 2755: 2749: 2746: 2744: 2741: 2739: 2735: 2732: 2728: 2724: 2720: 2717: 2716: 2715: 2712: 2708: 2705: 2704: 2703: 2700: 2698: 2695: 2693: 2690: 2688: 2685: 2683: 2680: 2676: 2673: 2672: 2671: 2668: 2664: 2661: 2660: 2659: 2656: 2654: 2651: 2649: 2646: 2644: 2640: 2636: 2632: 2629: 2625: 2622: 2620: 2617: 2615: 2612: 2611: 2610: 2607: 2606: 2604: 2602: 2598: 2594: 2588: 2585: 2583: 2580: 2578: 2575: 2574: 2572: 2570: 2566: 2562: 2556: 2553: 2551: 2548: 2547: 2542: 2539: 2537: 2534: 2532: 2529: 2528: 2527: 2526:Phospholipase 2524: 2523: 2518: 2515: 2513: 2510: 2508: 2505: 2503: 2500: 2498: 2495: 2493: 2490: 2488: 2485: 2483: 2480: 2478: 2474: 2471: 2469: 2466: 2465: 2464: 2461: 2460: 2457: 2454: 2452: 2449: 2447: 2444: 2440: 2437: 2435: 2432: 2431: 2430: 2427: 2426: 2424: 2420: 2416: 2412: 2407: 2403: 2399: 2392: 2387: 2385: 2380: 2378: 2373: 2372: 2369: 2363: 2360: 2358: 2355: 2354: 2346:(3) 371–382. 2345: 2341: 2338: 2334: 2333: 2327: 2318: 2314: 2309: 2304: 2300: 2296: 2292: 2288: 2284: 2277: 2269: 2265: 2260: 2255: 2251: 2247: 2243: 2236: 2228: 2224: 2219: 2214: 2209: 2204: 2200: 2196: 2192: 2188: 2184: 2177: 2169: 2165: 2160: 2155: 2151: 2147: 2143: 2136: 2128: 2124: 2120: 2116: 2112: 2108: 2105:(4): 585–97. 2104: 2100: 2096: 2089: 2081: 2077: 2072: 2067: 2063: 2059: 2055: 2051: 2047: 2040: 2032: 2028: 2023: 2018: 2013: 2008: 2004: 2000: 1996: 1989: 1981: 1977: 1972: 1967: 1964:(4): 506–17. 1963: 1959: 1955: 1948: 1938: 1929: 1921: 1917: 1912: 1907: 1904:(3): 462–74. 1903: 1899: 1895: 1888: 1880: 1876: 1871: 1866: 1862: 1858: 1855:(2): 144–51. 1854: 1850: 1846: 1839: 1831: 1825: 1817: 1813: 1808: 1803: 1799: 1795: 1791: 1787: 1783: 1776: 1768: 1764: 1759: 1754: 1749: 1744: 1740: 1736: 1735:PLOS Genetics 1732: 1725: 1717: 1711: 1707: 1706: 1698: 1690: 1684: 1680: 1679: 1671: 1663: 1659: 1655: 1651: 1647: 1643: 1636: 1632: 1625: 1623: 1619: 1615: 1610: 1600: 1598: 1584: 1583: 1578: 1575: 1572: 1569: 1568: 1563: 1560: 1557: 1554: 1553: 1548: 1545: 1542: 1539: 1538: 1533: 1530: 1527: 1523: 1522: 1517: 1514: 1511: 1508: 1505: 1504: 1499: 1496: 1493: 1490:as well as a 1489: 1485: 1484: 1479: 1476: 1473: 1470: 1467: 1464:as well as a 1463: 1459: 1458: 1453: 1450: 1447: 1444: 1443: 1433: 1432: 1427: 1424: 1421: 1417: 1416: 1411: 1408: 1405: 1402: 1401: 1396: 1393: 1390: 1387: 1386: 1381: 1378: 1375: 1372: 1371: 1366: 1363: 1360: 1357: 1356: 1351: 1348: 1345: 1342: 1341: 1336: 1333: 1330: 1326: 1322: 1318: 1314: 1310: 1306: 1305: 1300: 1297: 1294: 1291: 1290: 1286:3.1.26.-??: 1285: 1282: 1278: 1277: 1272: 1269: 1266: 1262: 1261: 1256: 1253: 1250: 1247: 1242: 1238: 1233: 1229: 1228: 1223: 1220: 1217: 1216: 1211: 1197: 1195: 1191: 1187: 1183: 1179: 1174: 1172: 1168: 1164: 1159: 1157: 1153: 1149: 1147: 1141: 1139: 1135: 1131: 1125: 1123: 1112: 1110: 1106: 1102: 1098: 1094: 1090: 1086: 1072: 1066: 1062: 1059: 1053: 1047: 1041: 1035: 1029: 1023: 1017: 1011: 1005: 999: 993: 987: 981: 975: 969: 963: 957: 951: 945: 939: 933: 927: 921: 915: 909: 903: 897: 891: 885: 879: 873: 867: 861: 855: 849: 843: 837: 831: 825: 819: 813: 807: 801: 795: 789: 783: 777: 771: 765: 759: 753: 747: 741: 735: 729: 723: 717: 711: 705: 699: 693: 687: 681: 675: 669: 663: 657: 651: 645: 639: 633: 627: 621: 615: 609: 603: 597: 591: 585: 579: 573: 567: 561: 555: 549: 543: 537: 531: 525: 519: 513: 507: 501: 495: 489: 483: 477: 471: 465: 459: 453: 447: 441: 435: 429: 423: 417: 411: 405: 399: 393: 387: 381: 375: 369: 363: 357: 351: 345: 339: 333: 327: 321: 315: 309: 303: 297: 291: 285: 279: 273: 267: 261: 255: 249: 243: 237: 231: 225: 219: 213: 207: 201: 194: 188: 182: 178: 176: 172: 169: 166: 164: 160: 157: 153: 149: 146: 144: 140: 136: 132: 129: 126: 122: 117: 113: 110: 106: 102: 99: 97: 93: 90: 87: 85: 81: 78: 75: 73: 69: 65: 61: 56: 51: 46: 41: 36: 31: 19: 3479:Translocases 3476: 3463: 3450: 3437: 3424: 3414:Transferases 3411: 3398: 3255:Binding site 3036:}} 3030:{{ 2994:Endonuclease 2925:ribonuclease 2924: 2865: 2648:Nucleotidase 2569:Thioesterase 2343: 2336: 2325: 2290: 2286: 2276: 2249: 2245: 2235: 2193:(7): e6424. 2190: 2186: 2176: 2149: 2145: 2135: 2102: 2098: 2088: 2056:(5): 253–9. 2053: 2049: 2039: 2002: 1999:Microbiology 1998: 1988: 1961: 1957: 1947: 1937: 1928: 1901: 1897: 1887: 1852: 1849:EMBO Reports 1848: 1838: 1824: 1789: 1786:Biochemistry 1785: 1775: 1738: 1734: 1724: 1704: 1697: 1677: 1670: 1645: 1641: 1635: 1606: 1593: 1580: 1565: 1550: 1535: 1519: 1501: 1481: 1455: 1429: 1413: 1398: 1383: 1368: 1353: 1338: 1302: 1287: 1274: 1258: 1231: 1225: 1178:angiogenesis 1175: 1160: 1144: 1142: 1126: 1118: 1088: 1085:Ribonuclease 1084: 1083: 1068:A:83-175 1061:A:82-174 1055:A:82-174 1049:B:82-174 1043:A:82-174 983:A:46-129 953:A:46-129 941:A:46-129 929:A:46-129 923:A:46-129 911:B:46-129 905:A:46-129 899:A:46-129 893:A:46-129 887:A:46-129 881:A:46-129 875:A:46-129 869:C:46-129 845:A:46-129 839:A:46-129 821:D:46-129 803:B:46-129 797:B:46-129 767:A:46-129 761:A:46-129 755:A:46-129 749:A:46-129 743:A:46-129 737:A:46-129 731:A:46-129 719:D:46-129 707:A:46-129 701:A:46-129 695:A:46-129 683:A:46-129 677:B:46-129 671:A:46-129 665:A:46-129 641:D:46-129 635:A:46-129 629:B:46-129 623:A:46-129 611:A:46-129 605:A:46-129 599:M:67-156 593:B:67-156 587:C:67-156 581:A:67-156 575:A:67-156 569:B:67-156 563:A:67-156 557:C:67-156 551:A:67-156 545:C:67-156 539:C:67-156 527:C:67-156 515:B:67-156 509:C:67-156 503:C:67-156 497:C:67-156 491:B:67-156 485:B:67-156 479:C:67-156 473:A:67-156 467:B:67-156 461:B:67-156 455:B:67-156 449:B:67-156 443:C:67-156 437:B:67-156 431:B:67-156 425:B:67-156 419:B:67-156 413:A:67-156 407:C:67-156 401:C:67-156 395:A:67-156 389:B:67-156 383:A:67-156 377:B:67-156 371:A:72-161 365:A:72-161 359:B:72-161 353:A:72-161 347:B:72-161 341:A:79-159 335:B:79-159 329:X:11-92 323:B:11-92 317:B:11-92 311:B:11-92 305:B:11-92 299:A:11-92 293:A:11-92 287:B:11-92 281:A:11-92 275:A:11-92 269:B:11-92 263:A:11-92 257:A:11-92 251:B:11-92 245:A:11-92 239:A:11-92 233:B:11-92 227:A:11-92 221:B:11-92 215:B:11-92 209:A:11-92 203:A:11-92 197: 196:B:11-92 190:A:56-137 184:A:56-137 66:Ribonuclease 44: 33:ribonuclease 3250:Active site 3169:Nuclease S1 2940:Exonuclease 2834:Lecithinase 2663:Calcineurin 2601:Phosphatase 2507:Lipoprotein 2497:Endothelial 1488:exonuclease 1462:exonuclease 1161:Similar to 1037::23-113 1031::45-127 1025::45-127 1019::45-127 1013::45-127 1007::21-102 1001::21-102 995::46-129 989::46-129 977::46-129 971::46-129 965::46-129 959::46-129 947::46-129 935::46-129 917::46-129 863::46-129 857::46-129 851::46-129 833::46-129 827::46-129 815::46-129 809::46-129 791::46-129 785::46-129 779::46-129 773::46-129 725::46-129 713::46-129 689::46-129 659::46-129 653::46-129 647::46-129 617::46-129 533::67-156 521::67-156 58:Identifiers 3522:Categories 3453:Isomerases 3427:Hydrolases 3294:Regulation 2482:Pancreatic 2419:Carboxylic 1628:References 1435:structure. 1340:RNase PhyM 131:structures 3543:EC 3.1.27 3538:EC 3.1.26 3332:EC number 3059:RNase III 2917:(includes 2858:Sulfatase 2771:Autotaxin 2635:Prostatic 2487:Lysosomal 2402:esterases 2398:Hydrolase 1532:EC number 1510:EC number 1498:EC number 1472:EC number 1446:EC number 1410:3.1.26.12 1337:3.1.??: 1335:EC number 1284:EC number 1276:RNase III 1246:denatured 1132:, 3' end 1097:catalyzes 89:IPR000026 3356:Kinetics 3280:Cofactor 3243:Activity 3153:RNase T1 2915:Nuclease 2550:Cutinase 2317:18211964 2268:17150966 2227:19641608 2187:PLOS ONE 2168:12244054 2127:20922592 2119:16969722 2080:20189811 2031:19246759 1980:25458845 1920:18984158 1879:19165139 1816:21838247 1767:20011113 1662:20606265 1577:3.1.13.1 1562:3.1.11.1 1547:3.1.13.3 1534:3.1.??: 1516:3.1.13.5 1500:3.1.??: 1483:RNase PH 1478:2.7.7.56 1431:RNase G 1426:3.1.26.- 1415:RNase E 1395:3.1.27.8 1385:RNase U2 1380:3.1.27.4 1370:RNase T2 1365:3.1.27.1 1355:RNase T1 1350:3.1.27.3 1325:ribosome 1309:ribozyme 1299:3.1.26.5 1271:3.1.26.3 1264:product. 1255:3.1.26.4 1222:3.1.27.5 1194:homology 1115:Function 1093:nuclease 1074:A:83-175 148:RCSB PDB 84:InterPro 3512:Biology 3466:Ligases 3236:Enzymes 3126:RNase E 3121:RNase Z 3116:RNase A 3111:RNase P 3084:RNase H 2702:Phytase 2502:Hepatic 2477:Lingual 2473:Gastric 2330:Sources 2308:2692241 2218:2712763 2195:Bibcode 2071:2888479 2022:2662391 1870:2637324 1807:3172371 1758:2781298 1622:exapted 1618:RNase A 1537:RNase T 1521:RNase D 1503:RNase R 1452:2.7.7.8 1400:RNase V 1329:protein 1304:RNase P 1289:RNase L 1260:RNase H 1227:RNase A 77:PF00545 3533:EC 3.1 3498:Portal 3440:Lyases 3064:Drosha 2989:3.1.21 2957:RecBCD 2935:3.1.11 2555:PETase 2463:Lipase 2315:  2305:  2266:  2225:  2215:  2166:  2125:  2117:  2078:  2068:  2029:  2019:  1978:  1918:  1877:  1867:  1814:  1804:  1765:  1755:  1712:  1685:  1660:  1614:DNases 1597:CRISPR 1317:enzyme 1154:; the 163:PDBsum 137:  127:  109:SUPFAM 63:Symbol 3392:Types 3073:Dicer 3028:;see 2854:3.1.6 2824:PDE4B 2820:PDE4A 2758:3.1.4 2727:IMPA3 2723:IMPA2 2719:IMPA1 2597:3.1.3 2565:3.1.2 2415:3.1.1 2123:S2CID 1526:tRNAs 1095:that 1089:RNase 105:SCOPe 96:SCOP2 18:RNase 3484:list 3477:EC7 3471:list 3464:EC6 3458:list 3451:EC5 3445:list 3438:EC4 3432:list 3425:EC3 3419:list 3412:EC2 3406:list 3399:EC1 2991:-31: 2937:-16: 2923:and 2829:PDE5 2815:PDE3 2810:PDE2 2805:PDE1 2697:PTEN 2682:OCRL 2675:PP2A 2624:ALPP 2619:ALPL 2614:ALPI 2408:3.1) 2313:PMID 2264:PMID 2223:PMID 2164:PMID 2115:PMID 2076:PMID 2027:PMID 1976:PMID 1916:PMID 1898:Cell 1875:PMID 1812:PMID 1763:PMID 1710:ISBN 1683:ISBN 1658:PMID 1607:The 1321:tRNA 1311:– a 1241:2AAS 1232:e.g. 1180:and 1148:(RI) 1122:RNAi 1107:and 1071:1r4y 1065:1de3 1058:1jbs 1052:1jbt 1046:1jbr 1040:1aqz 1034:1rtu 1028:1rck 1022:1fus 1016:1rcl 1010:1fut 1004:1rds 998:1rms 992:1rgk 986:4rnt 980:1i2f 974:5rnt 968:8rnt 962:2aae 956:7rnt 950:1iyy 944:3gsp 938:1hyf 932:2gsp 926:2bu4 920:1i3i 914:1lra 908:2aad 902:1tto 896:2bir 890:1loy 884:1g02 878:5bir 872:1i3f 866:1q9e 860:3bir 854:9rnt 848:5gsp 842:1lov 836:1fzu 830:1rn4 824:1rgl 818:3hoh 812:2rnt 806:4bir 800:1rgc 794:1ch0 788:6rnt 782:1bu4 776:1gsp 770:1ygw 764:7gsp 758:5hoh 752:1trp 746:1hz1 740:5bu4 734:1rhl 728:4bu4 722:1rga 716:4hoh 710:1rnt 704:1rn1 698:3bu4 692:1i2g 686:1det 680:1trq 674:1bir 668:1i0x 662:1low 656:4gsp 650:6gsp 644:3rnt 638:2hoh 632:1i2e 626:1bvi 620:1fys 614:1rls 608:1i0v 602:1b2m 596:1brn 590:1x1x 584:1b21 578:1rnb 572:1fw7 566:1x1u 560:1a2p 554:1bng 548:1bne 542:1brj 536:1brs 530:1yvs 524:1b2s 518:1bnr 512:1b20 506:1b27 500:1b2u 494:1bri 488:1x1y 482:1bse 476:1bsc 470:1b2z 464:1b2x 458:1bni 452:1x1w 446:1b3s 440:1bsb 434:1bsa 428:1bnj 422:1bgs 416:1bnf 410:1bns 404:1brk 398:1brg 392:1brh 386:1ban 380:1bsd 374:1bao 368:1buj 362:1gov 356:1gou 350:1goy 344:2rbi 338:1pyl 332:1py3 326:1ynv 320:1gmr 314:1i8v 308:1rgh 302:1rgg 296:1rgf 290:1gmp 284:1sar 278:1uci 272:1gmq 266:1rsn 260:1c54 254:1t2i 248:1rge 242:1ucl 236:1box 230:1t2h 224:1ay7 218:1lni 212:1ucj 206:2sar 200:1i70 193:1uck 187:1mgr 181:1mgw 156:PDBj 152:PDBe 135:ECOD 125:Pfam 101:1brn 72:Pfam 50:3agn 3146:4/5 2303:PMC 2295:doi 2254:doi 2250:282 2213:PMC 2203:doi 2154:doi 2150:277 2107:doi 2066:PMC 2058:doi 2017:PMC 2007:doi 2003:155 1966:doi 1906:doi 1902:135 1865:PMC 1857:doi 1802:PMC 1794:doi 1753:PMC 1743:doi 1650:doi 1454:: 1237:PDB 1184:in 1167:DNA 1101:RNA 175:PDB 143:PDB 3524:: 3104:2C 3099:2B 3094:2A 3075:: 3066:: 2856:: 2736:: 2725:, 2721:, 2637:)/ 2599:: 2567:: 2536:A2 2531:A1 2417:: 2406:EC 2400:: 2311:. 2301:. 2291:83 2289:. 2285:. 2262:. 2248:. 2244:. 2221:. 2211:. 2201:. 2189:. 2185:. 2162:. 2148:. 2144:. 2121:. 2113:. 2103:10 2101:. 2097:. 2074:. 2064:. 2054:35 2052:. 2048:. 2025:. 2015:. 2001:. 1997:. 1974:. 1962:56 1960:. 1956:. 1914:. 1900:. 1896:. 1873:. 1863:. 1853:10 1851:. 1847:. 1810:. 1800:. 1790:50 1788:. 1784:. 1761:. 1751:. 1737:. 1733:. 1656:. 1646:66 1644:. 1579:: 1574:EC 1564:: 1559:EC 1549:: 1544:EC 1518:: 1513:EC 1480:: 1475:EC 1449:EC 1428:: 1423:EC 1412:: 1407:EC 1397:: 1392:EC 1382:: 1377:EC 1367:: 1362:EC 1352:: 1347:EC 1301:: 1296:EC 1273:: 1268:EC 1257:: 1252:EC 1239:: 1224:: 1219:EC 1196:. 1124:. 154:; 150:; 133:/ 107:/ 103:/ 3500:: 3486:) 3482:( 3473:) 3469:( 3460:) 3456:( 3447:) 3443:( 3434:) 3430:( 3421:) 3417:( 3408:) 3404:( 3228:e 3221:t 3214:v 3141:3 3136:2 3131:1 3089:1 2927:) 2840:) 2836:( 2822:/ 2798:1 2786:D 2781:C 2760:: 2641:/ 2633:( 2541:B 2475:/ 2404:( 2390:e 2383:t 2376:v 2319:. 2297:: 2270:. 2256:: 2229:. 2205:: 2197:: 2191:4 2170:. 2156:: 2129:. 2109:: 2082:. 2060:: 2033:. 2009:: 1982:. 1968:: 1922:. 1908:: 1881:. 1859:: 1832:. 1818:. 1796:: 1769:. 1745:: 1739:5 1718:. 1691:. 1664:. 1652:: 1528:. 1494:. 1468:. 20:)

Index

RNase

3agn
Pfam
PF00545
InterPro
IPR000026
SCOP2
1brn
SCOPe
SUPFAM
Pfam
structures
ECOD
PDB
RCSB PDB
PDBe
PDBj
PDBsum
structure summary
PDB
1mgw
1mgr
1uck
1i70
2sar
1ucj
1lni
1ay7
1t2h

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