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Database: UniProt
Entry: A0A087XQE0_POEFO
LinkDB: A0A087XQE0_POEFO
Original site: A0A087XQE0_POEFO 
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
//
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