ID A0A8C3MUF4_GEOPR Unreviewed; 1402 AA.
AC A0A8C3MUF4; A0A8U8B5Z4;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 2.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS Geospiza parvula (Small tree-finch) (Camarhynchus parvulus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Thraupidae; Camarhynchus.
OX NCBI_TaxID=87175 {ECO:0000313|Ensembl:ENSCPVP00000010423.2, ECO:0000313|Proteomes:UP000694382};
RN [1] {ECO:0000313|Ensembl:ENSCPVP00000010423.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Enbody D E., Pettersson E M.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCPVP00000010423.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCPVP00000010423.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC EC=2.7.7.7; Evidence={ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR Ensembl; ENSCPVT00000010880.2; ENSCPVP00000010423.2; ENSCPVG00000007566.2.
DR Proteomes; UP000694382; Chromosome 1.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IEA:UniProtKB-ARBA.
DR GO; GO:0003682; F:chromatin binding; IEA:TreeGrafter.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:TreeGrafter.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006273; P:lagging strand elongation; IEA:TreeGrafter.
DR GO; GO:0006272; P:leading strand elongation; IEA:TreeGrafter.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR FunFam; 1.10.132.60:FF:000006; DNA polymerase; 1.
DR FunFam; 1.10.287.690:FF:000003; DNA polymerase; 1.
DR FunFam; 1.10.3200.20:FF:000001; DNA polymerase; 1.
DR FunFam; 3.30.420.10:FF:000018; DNA polymerase; 1.
DR FunFam; 3.30.70.2820:FF:000001; DNA polymerase; 1.
DR FunFam; 3.90.1600.10:FF:000022; DNA polymerase; 1.
DR FunFam; 3.90.1600.10:FF:000023; DNA polymerase; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 1.
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; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR NCBIfam; TIGR00592; pol2; 2.
DR PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 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 SUPFAM; SSF90234; Zinc finger domain of DNA polymerase-alpha; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000694382};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 39..100
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 444..655
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 720..1168
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1207..1396
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..33
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1402 AA; 159977 MW; 50FC5CFAC4FDDFB0 CRC64;
FLSCHGDMQN KRTMSESGSF AASRSRRERK NRRGQQEALE RLKKAKAGEK LKYEVEEFTG
VYDEIDEDEY SKMVRDRQDD DWIVDDDGIG YVEDGREIFD EDLDDDALIS NKKGKGGKTS
TIDKKNVKKS VVSKPNTIKS MFMASAGKKN TDKTVDLSKD DLLGDILQDI SAETVQLSPP
PVIVLKRKRS AGVPLNPFSV QSQTPKVKGE KSPLVLPAAL PDDDQGMMDF DEEDFDEPME
AEHVETIPET AESLKRDNEI EKKETESCSL PGLSCWDRID EDEADLVAAE VQLDPNLLPL
VNGESDDQVF RFYWLDAYED QFSQPGVVFL FGKVWIESAN TYVSCCVTVK NIERTVYLLP
RETEIDLSTG KETETPVTIM SVFKEFNDTI SPKYKIMKFK SKKVEKYYAF EIPDVPAKSE
YLEVKYSAEC PRLPQDLKGQ TFSHVFGTNT SSLELLLMNQ KIKGPCWLEI KNPQPSNQPV
SWCKVEAVAM KPGLVNVVKE LSPPPPLVVM SFSMKTIQNP KTHQNEVVAL AALVHQKFPL
DKAPPQPPFQ THFCEIAATE RTLLGFFLAK IHKIDPDVVV GHNIYGFDLE VLLQRINLCK
VPHWSKIGRL RRSNMPKLGG RGGFAERNAA CGRMICDVEI SAKELIRCKS YHLSELVHQI
LKTEKVTILP EEIPNMYSDS PRLLFMLENT WTDARFILQI MCELNVLPLA LQITNISGNV
MSRTMMGGRS ERNEFLLLHA FHEKDYIVPD KQVFKKPPPK PVDEDEDFED QNKSKIGKKK
AAYAGGLVLE PKVGFYDKFI LLLDFNSLYP SIIQEFNICF TTVQRLSSEA QKRVEEEEEI
PELPDPSLEM GILPKEIRKL VERRRQVKQL MKQPDLNPDL YLQYDIRQKA LKLTANSMYG
CLGFSYSRFY AKPLAALVTH KGREILMHTK EMVQKMNLEV IYGDTDSIMI NTNSTSLDEV
FKLGNKIKNE VNKLYKLLEI DIDGIFKSLL LLKKKKYAAL SVEPTGDGKY VTKQELKGLD
IVRRDWCDLA KQTGNYVIGQ ILSDQPRDII VENIQRRLIE IGENVVSGQI PANQFEINKV
SDLIPRIILT KTLPHVHVAM WINSHGGRKV KAGDTVSYII CQDGSDLSAS QRAYAPEQLK
KQENLKIDYQ YYLSQQIHPV VARICMPIEG IDSVLIATWL GLDPSQFRVH HHYHKDENDA
LVGGPAQLTD EEKYRDCERF KFCCLKCGTE NIYDNVFDGS GRFIEPSLQR CSKTECEEPP
FNYVVQMSNK LLLDIRRHLR KYYSGWLICE EPTCQNRTRR LPLSFSRSGP VCQACRKAVL
RPEYSDKALY TQLCFYRYIF DVDYAMDKVV TEEEKEYLKK KQLRGEVSEA YKRLKSTVDK
CLAMSGYSEV NLGKLFTVSI GR
//
