ID I3JZM5_ORENI Unreviewed; 2805 AA.
AC I3JZM5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=DNA polymerase zeta catalytic subunit {ECO:0000256|ARBA:ARBA00021589};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=REV3L {ECO:0000313|Ensembl:ENSONIP00000014320.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000014320.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000014320.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755}.
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DR Ensembl; ENSONIT00000014331.2; ENSONIP00000014320.2; ENSONIG00000011378.2.
DR GeneTree; ENSGT00940000156226; -.
DR HOGENOM; CLU_000203_1_0_1; -.
DR Proteomes; UP000005207; Linkage group LG15.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
DR CDD; cd05778; DNA_polB_zeta_exo; 1.
DR CDD; cd05534; POLBc_zeta; 1.
DR CDD; cd22287; REV3L_RBD; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR032757; DUF4683.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
DR Pfam; PF15735; DUF4683; 2.
DR Pfam; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 98..187
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 655..751
FT /note="DUF4683"
FT /evidence="ECO:0000259|Pfam:PF15735"
FT DOMAIN 760..999
FT /note="DUF4683"
FT /evidence="ECO:0000259|Pfam:PF15735"
FT DOMAIN 1954..2157
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 2224..2674
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 2717..2784
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 258..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1507..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1771..1874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1888..1916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1066
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1898..1912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2805 AA; 314683 MW; ED29213B451CAB74 CRC64;
MFAVRIVTAD YYLTSPIKDL DVCYSEFRES DVKKVPVVRI FGSTPAGQKT CLHLHGVFPY
IYVPYDNYGQ QPERYLRQVA FSIDRALNVA MGNPTSNNQH VFKVVLVSGM PYYGYHAKEK
LFMKIYLYNP QMVKRVCELL QSGAVMNKSY QPHEGHIPYL LQLFIDYNLY GMNLVNLAAV
KFRSSQKKGK GCGQGDTIGG TFVRWEENAI PSSLVLDEVQ RQSTCELEVD AVAVDVLNRL
EIENQIGRNP GLQAIWEDEK QRRREKNQPS QIETPESQDR GFVTSSESEK IFMKRVEEIL
KENEFDNQED FPGELTLHFD PLTPDGLPCT PANAVEVHRG RHPVPEEAVV DEEAILTLLE
NSQSFLPLSQ TSNHSPLLDS SRDQAIIDLL AGLEDDGFCR TPTRQNSQSR SLPGVTNYNC
NSDEEEAGPE LDKEEAELSV IMSQRWDSDP PESASSQSDG QQESSDEDME WSGNNSMFAN
LSIPQLDGAA DESSDSSLTD SGSMTQSSLT ATEKMLGKRN PIPGEMVHLE PPSTAKILLE
CKHPEHIPVH VLDTEQPLDK HFQLKSSQDS SSESLDKTDI ESFPFGNGKV AKNRKKYGSI
KNVETNCLSI LQNHRTFSLC YSELRNCSAK TDLELNTKDN KSPLLRSIAS APSTLKEDEF
LDPHEDEIGK DGEEGDVGEL KIRYEDYQEN KTERTIVAQQ EAHYKFFPSV ILSNCLSRKK
PGNKKMADTC SKVEQAQPRR SKLKMNKKRL EETIVKNDPL QDLSAKVTCT KPSALPGSKY
TLRTKRKMKY DSEDGEHSGA TRSKNLASVK ERLKDNDVSG GQEVKYQRRR KKEPPIIIKY
IIINRFKGEK NMLVKMSKVN AAEQLVVLTP DKLEHYKKLA PLKDFWPKVP ESTAVKFPVT
EPKAKKHPKR KAKVNSTNKK TINNSSKPLI RQGERVQKPK GRKKAPILPS LPPPRPCYCE
LAHDYDVDYS DVMVELGYLS DRSQSPRDST PPRCWSPSDP LMNTRSSEEL INPHIDPCLS
SAFQKPHRSS TAKGARNKCQ TAKPKRLSDA KRKPSKSAEE PKTEKAKQGN TAVLRQRMKA
GGAVNSSTST TRPRKSRKKK TEEPKRHDLI KESSQLLFPE NELPPSESSS QEVPPFQQQV
GKDSQGTSQT PSTPERNSVT KFIEPKVEDC ETSIMEVNQS ISAPAQTKQQ ACQTTVVKAE
DSQEHCTDLL PPVQEHNKDV QLKEGPPHSG PKNGEMPPLS ETPSGLAVLK KLLQTRQQGQ
PLPIQVVGTA SHSTAIAQAA ALLIPTTKPT KSRRAPTPTS RKPRAPKSNM AKEKRQRNRK
GKMSSTQPNL SVKQEGSMSD ECPLFLSDPG LDSCNFIEDS LSPELPHNYT FDINAIDQTE
FSSPYSGSQF VVTDKNLPVK FLSDISQDSV SAQALDSEKK LDRLLCSGED LQRGSDCNKA
RPNSPDLLDG HTNREPTSSL TSLKSREWDF SLGKAHTLSP FQDFHCERKE LLFSVFDSLP
LSSASFVDHE GSPTGELPEG IDGLTSTTPS SSPRSISSLS QVRASQLQRG AGGGGAHILK
PLMSPPSREE ILSTLLDLEM SEATFQEPFC SDPSDAPGKP MEVGGRKLTV GTRLARELAE
FGGDLSLEGL HFWKTAFSAM THPATTVISS CQGAEASETK GDLSSSSDKK VVLLPCKNPP
NRKRVQVWLK ARKQYESLQK GRRESELLKT ERAGLEVEED GGSERSELPA ADRSLKVELC
SNLSCTRAQR RKKQSLSLIL SPLENTGLRC KSTEASPVSD KGSVCLEQEN KNKEDDDDDK
TTCLESPELP TWQQSHQPSP SGQGQLSENK PGEDSPEPLS SMRCNSPELL RGNHSPSPLA
VSDRDERRTS PQLVHSTPFL RRRWRSKEDL DPVCSTPISQ EDPVSQRLQQ RRRSQADPLR
RVLLTTQMKN QFAALNVPKK DNSQIEGPSI ANSYGFKVSM QNLQDAKALH EVQHLTLMTM
ELHARTRRDL EPDPEFDPIC ALFYCFSSDT PLPDVDNTQL TGAIVVDKDH QGSSQAPLLV
RSGVSGLQVT YAADEKMLFD VLVTIMRRFD PDILVGYEVQ LHSWGYLLQR SSALGVDLCQ
QLSRVPGDSK ENRFAAERDE YGADTMTEIN IIGRITLNLW RVMKTEVTLN NYTFENVAFH
VLHQRFPLYS PRTLSDWFDH NTDLYRWKMV DHYVSRVRGC MQLLQQHDII GRTSELARLF
GIQFFHVLTR GSQYRVESMM LRVAKPLNYV PVTPSIQQRA QQRAPQCIPL VMEPESRFYS
NSVVVLDFQS LYPSIVIAYN YCFSTCLGHV DNLGTPDEFK FGCTSLRVPP ELLYQLRNDI
TVSPGGIAFV KSSVRKGVLP MMLEEILNTR IMVKQSMKTY KQDKALTKLL DARQLGLKLI
ANVTFGYTAA NYSGRMPSVE VGDSIVHKAR ETLERAIRMV NDTKKWGARV VYGDTDSMFV
LLKGATKEQA FKIGKEIAEA VTATNPKPIK LKFEKVYLPC VLQTKKRYVG YMYESLDQKE
PVFDAKGIET VRRDGCPAVS KILERSIKLL FETRDISQVK QFVQRQCVKI LDGRASIQDL
TFAKEYRGSG SYRPGACIPA LELTRRMMAY DRRLEPRVSE RVPYVIVYGT PGVPLIQLVR
RPTEVLQDPT LRLNATYYIT KQILPPLARM FQLIGVDVFS WYQELPRIQK ASCSSVVGGE
EAGRKGTISQ YFTTLHCPVC DELTQLGVCS RCRAEPQRVT VTLYQDMRQW ESQQEQLLKI
CRNCSGCAER QVPCVSLNCP VLYKLSRVNR QLSKAPYLRQ LLEQF
//
