1063:
449:
29:
389:
487:
C-terminal configuration which includes one dsRBD and two RNase III catalytic domains. Interactions of Dicer occurs with other proteins, which includes TRBP, PACT, and Ago2. RNAs that are produced by Dicer act as guides for a sequence of particular silencing of cognate genes through RNAi and related pathways.
486:
Dicer enzymes process dsRNA substrates into small RNA fragments of individual size ranging from 21-27 nucleotides in length. Dicer has an N-terminal helicase/ATPase domain which is followed by another domain of an unknown function. It also comprises the centrally positioned PAZ domain and a
743:
Soon-Jae Lee, Mengxuan Kong, Paul
Harrison, Mohamed Hijri; Conserved proteins of the RNA interference system in the arbuscular mycorrhizal fungus Rhizoglomus irregulare provide new insight into the evolutionary history of Glomeromycota, Genome Biology and Evolution, evy002,
345:(snoRNA). The basic dsRNA cleavage function of Class 1 RNase III is retained in most of the organisms in which it is present. However, in a number of species the function has changed and taken on different or additional biological roles.
420:- this RNase III is involved in the transcription and processing of rDNA, the 3' end formation of U2 snRNA via cleavage of the terminal loop, cell wall stress response and degradation, and regulation of morphogenesis checkpoint genes.
437:- this RNase III is located on chromosome II of the yeast genome and, when over expressed, is directly involved in the sterility, lack of mating efficiency, abnormal mitotic cell cycle, and mutation suppression of the organism.
483:(RNAi). Class 4 III RNases are S-RNase components. It is a component of the self-incompatibility system in Rosaceae, Solanaceae, and Plantaginaceae. They are recruited to cope with various environmental stress scenarios.
1080:; MacIntosh, Gustavo C.; Goldraij, Ariel (1 July 2015). "NnSR1, a class III non-S-RNase specifically induced in Nicotiana alata under phosphate deficiency, is localized in endoplasmic reticulum compartments".
733:
Liang Y-H, Lavoie M, Comeau M-A, Elela SA, Ji X. Structure of a
Eukaryotic RNase III Post-Cleavage Complex Reveals a Double- Ruler Mechanism for Substrate Selection. Molecular cell. 2014;54(3):431-444.
897:
Wu, Chang-Xian; Xu, Xian-Jin; Zheng, Ke; Liu, Fang; Yang, Xu-Dong; Chen, Chuang-Fu; Chen, Huan-Chun; Liu, Zheng-Fei (1 April 2016). "Characterization of ribonuclease III from
Brucella".
397:
Class II is defined by the presence of an N-terminal domain (NTD), a RIIID, and a dsRBD. Class II is found in some fungi species. They process precursors to rRNA, snRNA, and snoRNA.
274:
that are characterized by their ribonuclease domain, which is labelled the RNase III domain. They are ubiquitous compounds in the cell and play a major role in pathways such as
360:- this RNase III is involved in the processing of viral transcripts and some mRNAs through the cleavage of multiple areas on the dsRNA. This cleavage can be influenced by
682:"CsrA Participates in a PNPase Autoregulatory Mechanism by Selectively Repressing Translation of Transcripts That Have Been Previously Processed by RNase III and PNPase"
140:
645:
Inada, T.; Nakamura, Y. (1995). "Lethal double-stranded RNA processing activity of ribonuclease III in the absence of SuhB protein of
Escherichia coli".
1555:
534:
Filippov, Valery; Solovyev, Victor; Filippova, Maria; Gill, Sarjeet S. (7 March 2000). "A novel type of RNase III family proteins in eukaryotes".
1802:
333:. Typically, class I enzymes possess a single RNase III domain (RIIID) followed by a dsRNA-binding domain (dsRBD). They process precursors to
88:
1716:
1817:
1811:
1612:
1362:
1128:
MacRae, Ian J; Doudna, Jennifer A (February 2007). "Ribonuclease revisited: structural insights into ribonuclease III family enzymes".
1660:
1771:
1560:
840:
Glow, D.; Pianka, D.; Sulej, A. A.; Kozlowski, Lukasz P.; Czarnecka, J.; Chojnowski, G.; Skowronek, K. J.; Bujnicki, J. M. (2015).
259:
1878:
1766:
307:
structure whose function is to cleave dsRNA into multiple subunits. It is a Mg-dependent endonuclease and is largely found in
1687:
1597:
1550:
294:
The RNase III superfamily is divided into four known classes: 1, 2, 3, and 4. Each class is defined by its domain structure.
160:
2198:
2109:
2050:
452:
The crystal structure of the human Drosha ribonuclease enzyme in complex with two C-terminal helices of the DGCR8 protein.
2154:
1721:
1711:
1165:"Mini-III, an unusual member of the RNase III family of enzymes, catalyses 23S ribosomal RNA maturation in B. subtilis"
2114:
2006:
1631:
984:
Filippov V, Solovyev V, Filippova M, Gill SS (Mar 2000). "A novel type of RNase III family proteins in eukaryotes".
1700:
1696:
1692:
1608:
1441:
680:
Park, Hongmarn; Yakhnin, Helen; Connolly, Michael; Romeo, Tony; Babitzke, Paul; Gourse, R. L. (15 December 2015).
1962:
1908:
1868:
1827:
1731:
1570:
1538:
1424:
1388:
2203:
1616:
1465:
1379:
1332:
1326:
320:
270:
and cleaves it at specific targeted locations to transform them into mature RNAs. These enzymes are a group of
148:
1485:
1355:
374:
2188:
2041:
1680:
1062:
757:
Kreuze, Jan F.; Savenkov, Eugene I.; Cuellar, Wilmer; Li, Xiangdong; Valkonen, Jari P. T. (1 June 2005).
1976:
1873:
1665:
1626:
1490:
1412:
144:
2159:
1994:
1989:
1922:
1582:
1407:
101:
2014:
1984:
1788:
1783:
1707:
1643:
1429:
342:
610:
Conrad, Christian; Rauhut, Reinhard (February 2002). "Ribonuclease III: new sense from nuisance".
392:
Class 2 ribonuclease III (Rnt1p) from
Saccharomyces cerevisiae in complex with double-stranded RNA
2147:
1999:
1480:
1470:
1348:
1051:
1948:
1893:
1861:
1736:
1455:
1235:
1186:
1145:
1107:
1043:
1001:
914:
879:
861:
796:
778:
711:
662:
627:
592:
551:
361:
338:
271:
167:
135:
2024:
1604:
1509:
1504:
1460:
1279:
1253:
1225:
1217:
1176:
1137:
1097:
1089:
1035:
993:
906:
869:
853:
786:
770:
701:
693:
654:
619:
582:
543:
480:
127:
2126:
1940:
1856:
1851:
1846:
1759:
1754:
1514:
1392:
1019:
1026:(2001). "Role for a bidentate ribonuclease in the initiation step of RNA interference".
2099:
2094:
2089:
1475:
1450:
1446:
1419:
1402:
1230:
1205:
1023:
874:
841:
791:
758:
706:
681:
997:
623:
587:
570:
547:
2182:
1840:
1749:
1499:
1322:
1181:
1164:
1077:
774:
658:
417:
334:
324:
312:
279:
93:
57:
2193:
1967:
1898:
1621:
1542:
1093:
1055:
958:
263:
123:
1311:
69:
2142:
1913:
1807:
1670:
1636:
1574:
1340:
448:
304:
932:
910:
815:"rnc - Ribonuclease 3 - Escherichia coli (strain K12) - rnc gene & protein"
2119:
1141:
865:
782:
2032:
1831:
1744:
1371:
1239:
1190:
1149:
1111:
1047:
1005:
918:
883:
800:
715:
631:
596:
555:
666:
97:
28:
2077:
2072:
2067:
1888:
1523:
1375:
1307:
857:
814:
571:"Thirty-Three Years Later, a Glimpse at the Ribonuclease III Active Site"
462:
434:
430:
413:
353:
308:
64:
1335:
697:
2084:
2062:
2057:
1675:
1102:
329:
81:
76:
1221:
377:, are homodimeric enzymes and consist solely of the RNase III domains.
2104:
2037:
1930:
1528:
1436:
1039:
745:
502:
497:
458:
357:
316:
155:
241:
235:
229:
222:
216:
210:
204:
198:
192:
185:
179:
173:
461:
family of enzymes known to function in maturation of precursors to
2046:
1797:
1793:
759:"Viral Class 1 RNase III Involved in Suppression of RNA Silencing"
476:
447:
387:
1778:
1655:
1648:
1592:
1587:
1303:
514:
117:
52:
33:
Ribonuclease III structure interacting with double stranded RNA.
1344:
1163:
Redko, Yulia; Bechhofer, David H.; Condon, Ciarán (June 2008).
388:
275:
267:
1206:"Ribonuclease III mechanisms of double-stranded RNA cleavage"
612:
842:"Sequence-specific cleavage of dsRNA by Mini-III RNase"
1302:
This article incorporates text from the public domain
315:. Class 1 RNase III have been found in Glomeromycotan
327:. Among the RNases III in the class are the rnc from
1076:
Rojas, Hernán; Floyd, Brice; Morriss, Stephanie C.;
2135:
2023:
1975:
1961:
1939:
1921:
1907:
1887:
1826:
1730:
1569:
1537:
1387:
166:
154:
134:
116:
111:
87:
75:
63:
51:
43:
38:
21:
1666:Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
403:Yeast nucleases with the Class 2 RNase III domain
729:
727:
725:
1356:
8:
373:The variances of Class 1 RNase III, called
1972:
1918:
1904:
1363:
1349:
1341:
492:Human proteins containing RNase III domain
319:, which was suspected to be the result of
108:
27:
1325:at the U.S. National Library of Medicine
1229:
1180:
1123:
1121:
1101:
873:
790:
705:
586:
1556:Ubiquitin carboxy-terminal hydrolase L1
1280:"Tissue expression of DROSHA - Summary"
1254:"Tissue expression of DICER1 - Summary"
526:
479:family of enzymes known to function in
256:Ribonuclease III (RNase III or RNase C)
18:
2136:either deoxy- or ribo-
1130:Current Opinion in Structural Biology
7:
1717:Protein serine/threonine phosphatase
1210:Wiley Interdisciplinary Reviews: RNA
1204:Nicholson, Allen W. (January 2014).
569:Zamore, Phillip D. (December 2001).
1818:Cyclic nucleotide phosphodiesterase
1812:Clostridium perfringens alpha toxin
1613:Tartrate-resistant acid phosphatase
1661:Pyruvate dehydrogenase phosphatase
746:https://doi.org/10.1093/gbe/evy002
14:
1561:4-hydroxybenzoyl-CoA thioesterase
734:doi:10.1016/j.molcel.2014.03.006.
303:Class 1 RNase III enzymes have a
1182:10.1111/j.1365-2958.2008.06207.x
1061:
775:10.1128/JVI.79.11.7227-7238.2005
1879:N-acetylglucosamine-6-sulfatase
1767:Sphingomyelin phosphodiesterase
475:Class 4 RNases III include the
457:Class 3 RNases III include the
1688:Inositol-phosphate phosphatase
1551:Palmitoyl protein thioesterase
1094:10.1016/j.plantsci.2015.04.012
1:
2051:RNA-induced silencing complex
998:10.1016/S0378-1119(99)00571-5
624:10.1016/S1357-2725(01)00112-1
588:10.1016/S1097-2765(01)00418-X
548:10.1016/S0378-1119(99)00571-5
112:Available protein structures:
2155:Serratia marcescens nuclease
1722:Dual-specificity phosphatase
1712:Protein tyrosine phosphatase
659:10.1016/0300-9084(96)88139-9
1632:Fructose 1,6-bisphosphatase
2220:
1301:
911:10.1016/j.gene.2015.12.068
286:autoregulatory mechanism.
1869:Galactosamine-6 sulfatase
1425:6-phosphogluconolactonase
1286:. The Human Protein Atlas
1260:. The Human Protein Atlas
1142:10.1016/j.sbi.2006.12.002
107:
26:
1617:Purple acid phosphatases
1327:Medical Subject Headings
1022:, Caudy AA, Hammond SM,
321:horizontal gene transfer
933:"RNT1/YMR239C Overview"
686:Journal of Bacteriology
22:Ribonuclease III domain
2042:Microprocessor complex
1681:Beta-propeller phytase
1169:Molecular Microbiology
846:Nucleic Acids Research
453:
393:
1977:Endodeoxyribonuclease
1874:Iduronate-2-sulfatase
1627:Glucose 6-phosphatase
1413:Butyrylcholinesterase
939:. Stanford University
451:
391:
278:precursor synthesis,
2199:Protein biosynthesis
2160:Micrococcal nuclease
1995:Deoxyribonuclease IV
1990:Deoxyribonuclease II
1923:Exodeoxyribonuclease
1583:Alkaline phosphatase
1408:Acetylcholinesterase
1284:www.proteinatlas.org
1258:www.proteinatlas.org
959:"pac1 (SPBC119.11c)"
821:. UniProt Consortium
2015:UvrABC endonuclease
1985:Deoxyribonuclease I
1708:Protein phosphatase
1644:Protein phosphatase
1442:Bile salt-dependent
1430:PAF acetylhydrolase
937:www.yeastgenome.org
763:Journal of Virology
698:10.1128/JB.00721-15
343:small nucleolar RNA
2148:Mung bean nuclease
2007:Restriction enzyme
2000:Restriction enzyme
858:10.1093/nar/gkv009
454:
394:
290:Types of RNase III
2176:
2175:
2172:
2171:
2168:
2167:
1957:
1956:
1949:Oligonucleotidase
1894:deoxyribonuclease
1862:Steroid sulfatase
1737:Phosphodiesterase
1466:Hormone-sensitive
1222:10.1002/wrna.1195
769:(11): 7227–7238.
692:(24): 3751–3759.
470:Class 4 RNase III
444:Class 3 RNase III
384:Class 2 RNase III
362:ribosomal protein
339:small nuclear RNA
298:Class 1 RNase III
272:endoribonucleases
253:
252:
249:
248:
161:structure summary
2211:
2025:Endoribonuclease
2011:
2005:
1973:
1919:
1905:
1605:Acid phosphatase
1486:Monoacylglycerol
1396:ester hydrolases
1365:
1358:
1351:
1342:
1296:
1295:
1293:
1291:
1276:
1270:
1269:
1267:
1265:
1250:
1244:
1243:
1233:
1201:
1195:
1194:
1184:
1175:(5): 1096–1106.
1160:
1154:
1153:
1125:
1116:
1115:
1105:
1073:
1067:
1066:
1065:
1059:
1040:10.1038/35053110
1016:
1010:
1009:
981:
975:
974:
972:
970:
955:
949:
948:
946:
944:
929:
923:
922:
894:
888:
887:
877:
852:(5): 2864–2873.
837:
831:
830:
828:
826:
811:
805:
804:
794:
754:
748:
741:
735:
731:
720:
719:
709:
677:
671:
670:
642:
636:
635:
607:
601:
600:
590:
581:(6): 1158–1160.
566:
560:
559:
531:
481:RNA interference
463:microRNA (miRNA)
429:Pac1 (UniProtKB
412:RNT1 (UniProtKB
266:that recognizes
244:
238:
232:
225:
219:
213:
207:
201:
195:
188:
182:
176:
109:
31:
19:
16:Class of enzymes
2219:
2218:
2214:
2213:
2212:
2210:
2209:
2208:
2204:Protein domains
2179:
2178:
2177:
2164:
2131:
2019:
2009:
2003:
1966:
1953:
1941:Exoribonuclease
1935:
1912:
1896:
1892:
1883:
1857:Arylsulfatase L
1852:Arylsulfatase B
1847:Arylsulfatase A
1822:
1735:
1726:
1565:
1533:
1395:
1383:
1369:
1319:
1314:
1300:
1299:
1289:
1287:
1278:
1277:
1273:
1263:
1261:
1252:
1251:
1247:
1203:
1202:
1198:
1162:
1161:
1157:
1127:
1126:
1119:
1075:
1074:
1070:
1060:
1034:(6818): 363–6.
1018:
1017:
1013:
983:
982:
978:
968:
966:
963:www.pombase.org
957:
956:
952:
942:
940:
931:
930:
926:
896:
895:
891:
839:
838:
834:
824:
822:
819:www.uniprot.org
813:
812:
808:
756:
755:
751:
742:
738:
732:
723:
679:
678:
674:
644:
643:
639:
609:
608:
604:
568:
567:
563:
533:
532:
528:
523:
511:
494:
352:Rnc (UniProtKB
292:
262:) is a type of
240:
234:
228:
221:
215:
209:
203:
197:
191:
184:
178:
172:
34:
17:
12:
11:
5:
2217:
2215:
2207:
2206:
2201:
2196:
2191:
2181:
2180:
2174:
2173:
2170:
2169:
2166:
2165:
2163:
2162:
2157:
2152:
2151:
2150:
2139:
2137:
2133:
2132:
2130:
2129:
2124:
2123:
2122:
2117:
2112:
2107:
2097:
2092:
2087:
2082:
2081:
2080:
2075:
2070:
2065:
2055:
2054:
2053:
2044:
2029:
2027:
2021:
2020:
2018:
2017:
2012:
1997:
1992:
1987:
1981:
1979:
1970:
1959:
1958:
1955:
1954:
1952:
1951:
1945:
1943:
1937:
1936:
1934:
1933:
1927:
1925:
1916:
1902:
1885:
1884:
1882:
1881:
1876:
1871:
1866:
1865:
1864:
1859:
1854:
1849:
1836:
1834:
1824:
1823:
1821:
1820:
1815:
1805:
1800:
1791:
1786:
1781:
1776:
1775:
1774:
1764:
1763:
1762:
1757:
1747:
1741:
1739:
1728:
1727:
1725:
1724:
1719:
1714:
1705:
1704:
1703:
1685:
1684:
1683:
1673:
1668:
1663:
1658:
1653:
1652:
1651:
1641:
1640:
1639:
1629:
1624:
1619:
1602:
1601:
1600:
1595:
1590:
1579:
1577:
1567:
1566:
1564:
1563:
1558:
1553:
1547:
1545:
1535:
1534:
1532:
1531:
1526:
1520:
1519:
1518:
1517:
1512:
1507:
1496:
1495:
1494:
1493:
1491:Diacylglycerol
1488:
1483:
1478:
1473:
1468:
1463:
1458:
1453:
1444:
1433:
1432:
1427:
1422:
1420:Pectinesterase
1417:
1416:
1415:
1410:
1403:Cholinesterase
1399:
1397:
1385:
1384:
1370:
1368:
1367:
1360:
1353:
1345:
1339:
1338:
1330:
1318:
1317:External links
1315:
1298:
1297:
1271:
1245:
1196:
1155:
1136:(1): 138–145.
1117:
1078:Bassham, Diane
1068:
1011:
992:(1): 213–221.
976:
950:
924:
905:(2): 183–192.
889:
832:
806:
749:
736:
721:
672:
653:(4): 294–302.
637:
618:(2): 116–129.
602:
575:Molecular Cell
561:
542:(1): 213–221.
525:
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2:
2216:
2205:
2202:
2200:
2197:
2195:
2192:
2190:
2189:Ribonucleases
2187:
2186:
2184:
2161:
2158:
2156:
2153:
2149:
2146:
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2144:
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1906:
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1900:
1895:
1890:
1886:
1880:
1877:
1875:
1872:
1870:
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1841:arylsulfatase
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1750:Phospholipase
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418:S. cerevisiae
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335:ribosomal RNA
332:
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325:cyanobacteria
322:
318:
314:
313:bacteriophage
310:
306:
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287:
285:
281:
280:RNA Silencing
277:
273:
269:
265:
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257:
243:
237:
231:
227:
226:B:37-121
224:
218:
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208:A:37-121
206:
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189:A:37-121
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20:
2010:}}
2004:{{
1968:Endonuclease
1899:ribonuclease
1839:
1622:Nucleotidase
1543:Thioesterase
1288:. Retrieved
1283:
1274:
1262:. Retrieved
1257:
1248:
1216:(1): 31–48.
1213:
1209:
1199:
1172:
1168:
1158:
1133:
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1085:
1081:
1071:
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1027:
1014:
989:
985:
979:
967:. Retrieved
962:
953:
941:. Retrieved
936:
927:
902:
898:
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835:
823:. Retrieved
818:
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766:
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469:
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443:
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402:
383:
382:
341:(snRNA) and
328:
297:
296:
293:
283:
264:ribonuclease
255:
254:
239:A:333-418
233:A:37-121
220:A:37-121
214:B:37-121
202:A:37-121
196:A:37-121
190:
183:A:41-134
177:B:51-141
2143:Nuclease S1
1914:Exonuclease
1808:Lecithinase
1637:Calcineurin
1575:Phosphatase
1481:Lipoprotein
1471:Endothelial
1103:11336/42800
1088:: 250–259.
1020:Bernstein E
305:homodimeric
39:Identifiers
2183:Categories
1456:Pancreatic
1393:Carboxylic
1290:5 November
1264:5 November
969:5 November
965:. EMBL-EBI
943:5 November
825:5 November
521:References
282:, and the
124:structures
2033:RNase III
1891:(includes
1832:Sulfatase
1745:Autotaxin
1609:Prostatic
1461:Lysosomal
1376:esterases
1372:Hydrolase
1323:RNase+III
1312:IPR000999
1024:Hannon GJ
866:0305-1048
783:0022-538X
647:Biochimie
364:presence.
82:PDOC00448
70:IPR000999
47:RNase_III
2127:RNase T1
1889:Nuclease
1524:Cutinase
1336:3.1.26.3
1308:InterPro
1240:24124076
1191:18363798
1150:17194582
1112:26025538
1048:11201747
1006:10713462
919:26778206
884:25634891
801:15890961
716:26438818
632:11809414
597:11885596
556:10713462
509:See also
435:S. pombe
375:Mini-III
337:(rRNA),
309:bacteria
260:3.1.26.3
258:(BRENDA
245:A:10-111
141:RCSB PDB
65:InterPro
2100:RNase E
2095:RNase Z
2090:RNase A
2085:RNase P
2058:RNase H
1676:Phytase
1476:Hepatic
1451:Lingual
1447:Gastric
1231:3867540
1056:4371481
875:4357697
792:1112141
707:4652041
667:8589060
330:E. coli
77:PROSITE
58:PF00636
2038:Drosha
1963:3.1.21
1931:RecBCD
1909:3.1.11
1529:PETase
1437:Lipase
1329:(MeSH)
1238:
1228:
1189:
1148:
1110:
1054:
1046:
1028:Nature
1004:
917:
882:
872:
864:
799:
789:
781:
714:
704:
665:
630:
595:
554:
503:DROSHA
498:DICER1
459:Drosha
431:P22192
414:Q02555
358:E.Coli
354:P0A7Y0
156:PDBsum
130:
120:
102:SUPFAM
44:Symbol
2047:Dicer
2002:;see
1828:3.1.6
1798:PDE4B
1794:PDE4A
1732:3.1.4
1701:IMPA3
1697:IMPA2
1693:IMPA1
1571:3.1.3
1539:3.1.2
1389:3.1.1
1052:S2CID
477:Dicer
323:from
317:fungi
268:dsRNA
98:SCOPe
89:SCOP2
1965:-31:
1911:-16:
1897:and
1803:PDE5
1789:PDE3
1784:PDE2
1779:PDE1
1671:PTEN
1656:OCRL
1649:PP2A
1598:ALPP
1593:ALPL
1588:ALPI
1382:3.1)
1306:and
1304:Pfam
1292:2016
1266:2016
1236:PMID
1187:PMID
1146:PMID
1108:PMID
1044:PMID
1002:PMID
986:Gene
971:2016
945:2016
915:PMID
899:Gene
880:PMID
862:ISSN
827:2016
797:PMID
779:ISSN
712:PMID
663:PMID
628:PMID
593:PMID
552:PMID
536:Gene
515:RncO
433:) -
416:) -
356:) -
311:and
242:1u61
236:2ffl
230:1yz9
223:1yyk
217:1yyo
211:1rc5
205:1i4s
199:1yyw
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186:1jfz
180:2a11
174:1o0w
149:PDBj
145:PDBe
128:ECOD
118:Pfam
94:1jfz
53:Pfam
2194:RNA
2120:4/5
1226:PMC
1218:doi
1177:doi
1138:doi
1098:hdl
1090:doi
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1036:doi
1032:409
994:doi
990:245
907:doi
903:579
870:PMC
854:doi
787:PMC
771:doi
702:PMC
694:doi
690:197
655:doi
620:doi
583:doi
544:doi
540:245
284:pnp
276:RNA
168:PDB
136:PDB
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