511:
236:
37:
1084:
Shi, Wei; Vu, Therese; Boucher, Didier; Biernacka, Anna; Nde, Jules; Pandita, Raj K.; Straube, Jasmin; Boyle, Glen M.; Al-Ejeh, Fares; Nag, Purba; Jeffery, Jessie; Harris, Janelle L.; Bain, Amanda L.; Grzelak, Marta; Skrzypczak, Magdalena; Mitra, Abhishek; Dojer, Norbert; Crosetto, Nicola; Cloonan,
638:
The mitochondria of eukaryotic cells contain their own single stranded DNA binding protein. Human mitochondrial SSB (mtSSB) binds to single-stranded mitochondrial DNA as a tetramer and has sequence similarity to bacterial SSB. Human mtSSB is encoded by the
902:"Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution"
1134:
Pandita, R. K.; Chow, T. T.; Udayakumar, D.; Bain, A. L.; Cubeddu, L.; Hunt, C. R.; Shi, W.; Horikoshi, N.; Zhao, Y.; Wright, W. E.; Khanna, K. K.; Shay, J. W.; Pandita, T. K. (14 January 2015).
1085:
Nicole; Becherel, Olivier J.; Finnie, John; Skaar, Jeffrey R.; Walkley, Carl R.; Pandita, Tej K.; Rowicka, Maga; Ginalski, Krzysztof; Lane, Steven W.; Khanna, Kum Kum (4 May 2017).
951:
Tiranti, V; Rocchi, M; DiDonato, S; Zeviani, M (30 April 1993). "Cloning of human and rat cDNAs encoding the mitochondrial single-stranded DNA-binding protein (SSB)".
319:
176:
670:
695:"The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding"
812:"Herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) enhances the ability of the viral DNA helicase-primase to unwind cisplatin-modified DNA"
1035:
Pfeifer, Matthias; Brem, Reto; Lippert, Timothy P.; Boulianne, Bryant; Ho, Howin Ng; Robinson, Mark E.; Stebbing, Justin; Feldhahn, Niklas (15 June 2019).
1237:
651:
Recently, it has been found that it 1. Helps protect the genome, 2. Is vital for stem cells and 3. Is involved with maintaining telomere length.
457:
DNA replication fork. ICP8 may stimulate DNA unwinding and enable bypass of cisplatin damaged DNA by recruiting the helicase-primase to the DNA.
1801:
1764:
392:(HSV-1) SSB, ICP8, is a nuclear protein that, along other replication proteins is required for viral DNA replication during lytic infection.
112:
1884:
1893:
1459:
465:
373:
771:"Photoaffinity labeling of the herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) with oligodeoxyribonucleotides"
1946:
988:"A single-stranded DNA binding protein required for mitochondrial DNA replication in S. cerevisiae is homologous to E. coli SSB"
1999:
1979:
1806:
339:
196:
1616:
1466:
1230:
1607:
1275:
1250:
1136:"Single-Strand DNA-Binding Protein SSB1 Facilitates TERT Recruitment to Telomeres and Maintains Telomere G-Overhangs"
1736:
1712:
1581:
1413:
1360:
1342:
1254:
1087:"Ssb1 and Ssb2 cooperate to regulate mouse hematopoietic stem and progenitor cells by resolving replicative stress"
450:
1984:
1790:
1200:
1989:
1951:
1223:
1204:
413:
630:
is the functional equivalent of SSB in the nucleus of eukaryotic cells, though there is no sequence homology.
327:
184:
1353:
1284:
218:) are a class of proteins that have been identified in both viruses and organisms from bacteria to humans.
1850:
1781:
602:
582:
562:
434:
1776:
1545:
1215:
665:
627:
734:
Anders DG, McCue LA (1996). "The human cytomegalovirus genes and proteins required for DNA synthesis".
323:
180:
1823:
1796:
1747:
389:
384:
and two alpha helices, whereas the back side is a three-stranded beta-sheet The shoulder part of the
369:
125:
473:
441:
residues 368-902 contains the single-strand DNA-binding site of ICP8. The HHHV-1 UL5, UL8, and UL52
1553:
660:
575:
615:
595:
1037:"SSB1/SSB2 Proteins Safeguard B Cell Development by Protecting the Genomes of B Cell Precursors"
1994:
1759:
1576:
1165:
1116:
1066:
1017:
968:
933:
882:
833:
792:
751:
716:
517:
480:, repair and recombination. It has a structure of three beta-strands to a single six-stranded
360:(HHV-5) DNA synthesis appears typical of the herpesviruses, some novel features are emerging.
314:
171:
1716:
1565:
1560:
1452:
1155:
1147:
1106:
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923:
913:
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864:
823:
782:
743:
706:
510:
409:
306:
163:
1929:
1721:
1595:
1313:
1263:
1246:
477:
356:
1569:
1549:
1160:
1135:
1111:
1086:
1061:
1036:
1003:
446:
430:
1012:
987:
877:
852:
1973:
1771:
1698:
1308:
964:
928:
901:
572:
485:
421:
117:
268:
68:
1910:
868:
612:
592:
530:
302:
159:
1151:
81:
1189:
1102:
280:
137:
93:
1855:
527:
377:
1941:
1915:
1703:
1688:
481:
438:
385:
381:
1052:
828:
811:
1879:
1693:
1683:
918:
1169:
1120:
1070:
796:
787:
770:
720:
711:
694:
449:
DNA helicase-primase that is responsible for concomitant DNA unwinding and
17:
1210:
1021:
972:
937:
886:
837:
755:
235:
121:
36:
1956:
1937:
1509:
1500:
1298:
1185:
469:
275:
88:
1520:
1495:
1490:
1322:
405:
105:
100:
747:
521:
334:
191:
41:
Crystal structure of PriB- a primosomal DNA replication protein of
1870:
1865:
1860:
1843:
1838:
1833:
1828:
1816:
1811:
1529:
1524:
1481:
1476:
1471:
640:
454:
418:
353:
1752:
1676:
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1666:
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1656:
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1646:
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1631:
1626:
1621:
1513:
1443:
1438:
1433:
1428:
1423:
1418:
1406:
1399:
1390:
1385:
1380:
1375:
1370:
1365:
1327:
1303:
1291:
1181:
986:
Van Dyck, E; Foury, F; Stillman, B; Brill, SJ (September 1992).
607:
587:
567:
442:
427:
401:
380:. The front side of the neck region consists of a five-stranded
296:
263:
153:
132:
75:
63:
1219:
376:(ssDNA-binding protein (SSB)), the head consists of the eight
853:"The single-stranded DNA-binding protein of Escherichia coli"
900:
Raghunathan S, Ricard CS, Lohman TM, Waksman G (June 1997).
388:
domain contains an alpha-helical and beta-sheet region. The
426:(HHV-1) single-strand DNA-binding protein ICP8 is a 128kDa
412:
fork machinery, including a two-subunit DNA polymerase, a
1180:
This article incorporates text from the public domain
515:
1928:
1902:
1732:
1603:
1594:
1538:
1338:
1271:
1262:
810:Tanguy Le Gac N, Villani G, Boehmer PE (May 1998).
538:
498:
333:
313:
295:
290:
274:
262:
254:
249:
228:
190:
170:
152:
147:
131:
111:
99:
87:
74:
62:
54:
49:
29:
643:gene. In yeast, it is encoded by the RIM1 gene.
542:damaged DNA binding, single-stranded DNA binding
416:and a single-stranded DNA-binding protein. The
240:Single stranded DNA-binding protein(icp8) from
688:
686:
671:Comparison of nucleic acid simulation software
1231:
8:
1600:
1268:
1238:
1224:
1216:
509:
287:
234:
144:
35:
1203:at the U.S. National Library of Medicine
1159:
1110:
1060:
1011:
927:
917:
876:
827:
786:
710:
693:Mapelli M, Panjikar S, Tucker PA (2005).
682:
437:has shown that the region encompassing
495:
225:
26:
769:White EJ, Boehmer PE (October 1999).
7:
1201:Single-Stranded+DNA+Binding+Proteins
851:Meyer RR, Laine PS (December 1990).
647:Role in Genome Repair and Anti-aging
1004:10.1002/j.1460-2075.1992.tb05421.x
25:
1894:Control of chromosome duplication
1460:Autonomously replicating sequence
374:single-strand DNA-binding protein
492:Eukaryotic replication protein A
351:Although the overall picture of
212:Single-stranded binding proteins
531:protein A Replication protein A
869:10.1128/MMBR.54.4.342-380.1990
400:Six herpes virus-group-common
1:
1617:DNA polymerase III holoenzyme
1467:Single-strand binding protein
1152:10.1158/0008-5472.CAN-14-2289
775:Biochem. Biophys. Res. Commun
547:
291:Available protein structures:
148:Available protein structures:
1103:10.1182/blood-2016-06-725093
965:10.1016/0378-1119(93)90370-i
906:Proc. Natl. Acad. Sci. U.S.A
634:Eukaryotic mitochondrial SSB
408:that likely constitute the
2016:
1713:Prokaryotic DNA polymerase
1414:Minichromosome maintenance
1361:Origin recognition complex
1179:
472:are important maintaining
1791:Eukaryotic DNA polymerase
1041:The Journal of Immunology
546:
508:
503:
286:
233:
143:
34:
1205:Medical Subject Headings
1053:10.4049/jimmunol.1801618
829:10.1074/jbc.273.22.13801
414:Helicase-primase complex
1354:Pre-replication complex
1285:Pre-replication complex
919:10.1073/pnas.94.13.6652
2000:DNA-binding substances
1980:Protein heteropolymers
788:10.1006/bbrc.1999.1566
712:10.1074/jbc.M406780200
603:Replication protein A3
583:Replication protein A2
563:Replication protein A1
435:Photoaffinity labeling
1777:Replication protein A
1546:Origin of replication
666:Replication protein A
628:Replication protein A
499:Replication protein A
1748:Replication factor C
476:, more specifically
445:encode an essential
390:herpes simplex virus
370:herpes simplex virus
661:DNA-binding protein
466:SSB protein domains
557:Chromosomal locus
1967:
1966:
1924:
1923:
1760:Flap endonuclease
1590:
1589:
1577:Okazaki fragments
1097:(18): 2479–2492.
1047:(12): 3423–3433.
748:10.1159/000150508
625:
624:
621:
620:
453:synthesis at the
349:
348:
345:
344:
340:structure summary
208:Class of proteins
206:
205:
202:
201:
197:structure summary
16:(Redirected from
2007:
1985:Protein families
1717:DNA polymerase I
1601:
1561:Replication fork
1453:Licensing factor
1269:
1240:
1233:
1226:
1217:
1174:
1173:
1163:
1131:
1125:
1124:
1114:
1081:
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1074:
1064:
1032:
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992:The EMBO Journal
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831:
807:
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766:
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759:
731:
725:
724:
714:
690:
548:
524:
513:
496:
288:
238:
226:
145:
43:Escherichia coli
39:
27:
21:
2015:
2014:
2010:
2009:
2008:
2006:
2005:
2004:
1990:DNA replication
1970:
1969:
1968:
1963:
1920:
1898:
1738:
1734:
1728:
1722:Klenow fragment
1605:
1586:
1570:leading strands
1534:
1344:
1340:
1334:
1273:
1258:
1247:DNA replication
1244:
1197:
1192:
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1177:
1140:Cancer Research
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1132:
1128:
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984:
980:
950:
949:
945:
899:
898:
894:
850:
849:
845:
822:(22): 13801–7.
809:
808:
804:
768:
767:
763:
742:(5–6): 378–88.
733:
732:
728:
692:
691:
684:
679:
657:
649:
636:
534:
516:
494:
478:DNA replication
463:
398:
366:
357:cytomegalovirus
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1388:
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1350:
1348:
1343:preparation in
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1195:External links
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1146:(5): 858–869.
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998:(9): 3421–30.
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912:(13): 6652–7.
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857:Microbiol. Rev
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504:(heterotrimer)
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474:DNA metabolism
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447:heterotrimeric
431:metalloprotein
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1772:Topoisomerase
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1699:Topoisomerase
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1234:
1229:
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1222:
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1199:
1198:
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1009:
1005:
1001:
997:
993:
989:
982:
979:
974:
970:
966:
962:
959:(2): 219–25.
958:
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944:
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935:
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920:
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911:
907:
903:
896:
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863:(4): 342–80.
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821:
817:
816:J. Biol. Chem
813:
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798:
794:
789:
784:
780:
776:
772:
765:
762:
757:
753:
749:
745:
741:
737:
736:Intervirology
730:
727:
722:
718:
713:
708:
705:(4): 2990–7.
704:
700:
696:
689:
687:
683:
676:
672:
669:
667:
664:
662:
659:
658:
654:
652:
646:
644:
642:
633:
631:
629:
617:
614:
611:
609:
606:
604:
601:
600:
597:
594:
591:
589:
586:
584:
581:
580:
577:
574:
571:
569:
566:
564:
561:
560:
556:
553:
550:
549:
545:
541:
537:
533:
532:
529:
523:
519:
512:
507:
502:
497:
491:
489:
487:
483:
479:
475:
471:
467:
461:Bacterial SSB
460:
458:
456:
452:
448:
444:
440:
436:
432:
429:
425:
423:
420:
415:
411:
407:
403:
395:
393:
391:
387:
383:
379:
378:alpha helices
375:
371:
368:In ICP8, the
363:
361:
359:
358:
355:
341:
338:
336:
332:
329:
325:
321:
318:
316:
312:
308:
304:
301:
298:
294:
289:
285:
282:
279:
277:
273:
270:
267:
265:
261:
257:
253:
248:
243:
237:
232:
227:
221:
219:
217:
213:
198:
195:
193:
189:
186:
182:
178:
175:
173:
169:
165:
161:
158:
155:
151:
146:
142:
139:
136:
134:
130:
127:
123:
119:
116:
114:
110:
107:
104:
102:
98:
95:
92:
90:
86:
83:
80:
77:
73:
70:
67:
65:
61:
57:
53:
48:
44:
38:
33:
28:
19:
1911:Processivity
1737:synthesis in
1143:
1139:
1129:
1094:
1090:
1079:
1044:
1040:
1030:
995:
991:
981:
956:
952:
946:
909:
905:
895:
860:
856:
846:
819:
815:
805:
781:(2): 493–7.
778:
774:
764:
739:
735:
729:
702:
698:
650:
637:
626:
551:Subunit name
526:
464:
417:
399:
367:
352:
350:
258:Viral_DNA_bp
241:
229:Viral_DNA_bp
215:
211:
210:
42:
1930:Termination
1604:Prokaryotic
1596:Replication
1272:Prokaryotic
1251:prokaryotic
1249:(comparing
1211:SSB in PFAM
699:J Biol Chem
528:Proteopedia
422:herpesvirus
410:replication
250:Identifiers
50:Identifiers
18:SSB protein
1974:Categories
1942:Telomerase
1916:DNA ligase
1909:Movement:
1733:Eukaryotic
1704:DNA gyrase
1689:DNA ligase
1608:elongation
1339:Eukaryotic
1276:initiation
1264:Initiation
1255:eukaryotic
677:References
484:to form a
482:beta-sheet
439:amino acid
386:N-terminal
382:beta-sheet
303:structures
160:structures
1880:DNA clamp
1694:DNA clamp
1684:Replisome
1190:IPR000635
396:Mechanism
364:Structure
281:IPR000635
222:Viral SSB
106:PDOC00602
94:IPR000424
1995:Proteins
1938:Telomere
1554:Replicon
1510:Helicase
1501:RNASEH2A
1345:G1 phase
1299:Helicase
1186:InterPro
1170:25589350
1121:28270450
1071:31085591
797:10529391
721:15507432
655:See also
539:Function
525:
470:bacteria
406:proteins
372:(HSV-1)
320:RCSB PDB
276:InterPro
177:RCSB PDB
89:InterPro
1851:epsilon
1739:S phase
1566:Lagging
1521:Primase
1496:RNASEH1
1491:RNase H
1323:Primase
1161:4351820
1112:5418634
1062:6545462
1022:1324172
973:8482537
938:9192620
887:2087220
838:9593724
756:9130047
573:Chr. 17
404:encode
269:PF00747
244:virus-1
101:PROSITE
69:PF00436
1582:Primer
1207:(MeSH)
1168:
1158:
1119:
1109:
1069:
1059:
1020:
1013:556877
1010:
971:
936:
926:
885:
878:372786
875:
836:
795:
754:
719:
613:Chr. 7
593:Chr. 1
451:primer
335:PDBsum
309:
299:
255:Symbol
192:PDBsum
166:
156:
126:SUPFAM
82:CL0021
55:Symbol
1871:POLE4
1866:POLE3
1861:POLE2
1844:POLD4
1839:POLD3
1834:POLD2
1829:POLD1
1824:delta
1817:PRIM2
1812:PRIM1
1807:POLA2
1802:POLA1
1797:alpha
1530:PRIM2
1525:PRIM1
1482:SSBP4
1477:SSBP3
1472:SSBP2
1091:Blood
929:21213
641:SSBP1
616:p21.3
596:p35.3
576:p13.3
486:dimer
455:viral
443:genes
419:human
402:genes
354:human
138:3.A.7
122:SCOPe
113:SCOP2
1957:DKC1
1952:TERC
1947:TERT
1903:Both
1885:PCNA
1856:POLE
1782:RPA1
1765:FEN1
1753:RFC1
1677:holE
1672:holD
1667:holC
1662:holB
1657:holA
1652:dnaX
1647:dnaT
1642:dnaQ
1637:dnaN
1632:dnaH
1627:dnaE
1622:dnaC
1568:and
1539:Both
1514:HFM1
1444:MCM7
1439:MCM6
1434:MCM5
1429:MCM4
1424:MCM3
1419:MCM2
1407:Cdt1
1400:Cdc6
1391:ORC6
1386:ORC5
1381:ORC4
1376:ORC3
1371:ORC2
1366:ORC1
1328:dnaG
1309:dnaB
1304:dnaA
1292:dnaC
1184:and
1182:Pfam
1166:PMID
1117:PMID
1067:PMID
1018:PMID
969:PMID
953:Gene
934:PMID
883:PMID
834:PMID
793:PMID
752:PMID
717:PMID
608:RPA3
588:RPA2
568:RPA1
554:Gene
522:1L1O
428:zinc
328:PDBj
324:PDBe
307:ECOD
297:Pfam
264:Pfam
216:SSBs
185:PDBj
181:PDBe
164:ECOD
154:Pfam
133:TCDB
118:1kaw
78:clan
76:Pfam
64:Pfam
1550:Ori
1253:to
1156:PMC
1148:doi
1107:PMC
1099:doi
1095:129
1057:PMC
1049:doi
1045:202
1008:PMC
1000:doi
961:doi
957:126
924:PMC
914:doi
873:PMC
865:doi
824:doi
820:273
783:doi
779:264
744:doi
707:doi
703:280
518:PDB
468:in
315:PDB
172:PDB
58:SSB
30:SSB
1976::
1940::
1715::
1523::
1512::
1314:T7
1188::
1164:.
1154:.
1144:75
1142:.
1138:.
1115:.
1105:.
1093:.
1089:.
1065:.
1055:.
1043:.
1039:.
1016:.
1006:.
996:11
994:.
990:.
967:.
955:.
932:.
922:.
910:94
908:.
904:.
881:.
871:.
861:54
859:.
855:.
832:.
818:.
814:.
791:.
777:.
773:.
750:.
740:39
738:.
715:.
701:.
697:.
685:^
520::
488:.
433:.
326:;
322:;
305:/
183:;
179:;
162:/
124:/
120:/
1793::
1741:)
1735:(
1610:)
1606:(
1552:/
1548:/
1347:)
1341:(
1278:)
1274:(
1257:)
1239:e
1232:t
1225:v
1172:.
1150::
1123:.
1101::
1073:.
1051::
1024:.
1002::
975:.
963::
940:.
916::
889:.
867::
840:.
826::
799:.
785::
758:.
746::
723:.
709::
424:1
214:(
20:)
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