ID A0A087XQE0_POEFO Unreviewed; 1109 AA.
AC A0A087XQE0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000007993.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000007993.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU000442};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR EMBL; AYCK01009478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087XQE0; -.
DR STRING; 48698.ENSPFOP00000007993; -.
DR Ensembl; ENSPFOT00000008005.1; ENSPFOP00000007993.1; ENSPFOG00000007750.1.
DR eggNOG; KOG0969; Eukaryota.
DR GeneTree; ENSGT00560000077365; -.
DR OMA; CNNCRPR; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0043625; C:delta DNA polymerase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; 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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05777; DNA_polB_delta_exo; 1.
DR CDD; cd05533; POLBc_delta; 1.
DR Gene3D; 2.40.50.730; -; 2.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
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 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
KW DNA excision {ECO:0000256|ARBA:ARBA00022769};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000442}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 176..484
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 548..981
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1020..1090
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1109 AA; 125318 MW; 52CDE9440B75E5CE CRC64;
MDFKRRNGGP LMGGASQAKR GKATGDWEDS PSQFEEELSM FDDAEMDVED MEGQAGHDVI
PVGDLFSADL NPRWRRPPAP SLDPSSDKLV FQQIDLDYYL GGSVAGMPGQ SQGKVPIIRM
FGVTDSGNSV CCHVHGFAPY FYVPAPNGGF TSNYLEEFKR ELNSVVLKDM RSNKDNISIT
VLAVDICRKE TKGIYGYHGQ RSLDFLRITM AMPRLIAPAK RLLEQGFKFG PFPIQSYQAY
EANIDFEIRF MVDSDVVGCC WIELPKGKYR VREEKSSTDA DSQTLGKVSL CQYEVDVGWT
DFISHPAEGE WQKIAPLRVL SFDIECAGRK GIFPEPDRDP VIQIASMVQR QGETEPFIRT
VFTLQSCASI VGSQILCFTQ EKQLLQSWAE FLRTVDPDII TGYNIQNFDF PYLLNRAAAL
KVNYFPYLGR MRGIKSVLRE LSFQSKQMGR RENKTINMEG RVQFDLLQVL LRDYKLRSYT
LNAVSFHFLQ EQKEDVQHSI ITDLQNGNEQ TRRRLAVYCL KDAYLPLRLL QKLMCVINYM
EMARVTGVPL TYLLSRGQQI KVVSQLLRQA MKQDLVMPVV KTEGGEDYTG ATVIEPEKGY
YSVPIATLDF SSLYPSIMMA HNLCYTTLLQ KGAAEKLGLS PDDFIKTPTG DQFVKSSVRK
GLLPEILENL LSARKRAKTE LKKETDPFKK QVLDGRQLAL KISANSVYGF TGAQVGKLPC
LEISQSVTGF GRQMIEKTKQ LVESKYTISN GYQADARVVY GDTDSVMVKL GVTTVKEAME
IGREAAEWVS SHFTPPIKLE FEKVYYPYLL INKKRYAGLY FSSSPDTHDK MDCKGIETVR
RDNCPLVANL INTCLQKILI ERDPQGAVDH AKEVISDLLC NRIDISQLVI TKELTRTAQE
YAGKQAHVEL AESRMRKRDA GSAPNLGDRV PYVIIKAAKG AAAYMKSEDP IYVLENNIPI
DTQYYLEQQL SKPLLRIFEP ILGETKAESV LLKGDHTRCK TVLTSKVGGL MAFAQKRSTC
IGCKAVLKTD AAVCDFCKKK ESELYQKEIF HLNALEERFS RLWTQCQRCQ GSLHEDVLCT
SRDCPIFYMR KKVQKDLDDQ SKLVSRFGW
//