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Database: UniProt
Entry: A0A2K5E3F0_AOTNA
LinkDB: A0A2K5E3F0_AOTNA
Original site: A0A2K5E3F0_AOTNA 
ID   A0A2K5E3F0_AOTNA        Unreviewed;      1462 AA.
AC   A0A2K5E3F0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   Name=POLA1 {ECO:0000313|Ensembl:ENSANAP00000027731.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000027731.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000027731.1}
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|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   RefSeq; XP_012304282.1; XM_012448859.1.
DR   Ensembl; ENSANAT00000045750.1; ENSANAP00000027731.1; ENSANAG00000031620.1.
DR   GeneID; 105714751; -.
DR   CTD; 5422; -.
DR   GeneTree; ENSGT00550000074891; -.
DR   OMA; MTKMNVG; -.
DR   OrthoDB; 5477697at2759; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProt.
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   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; 1.
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|RuleBase:RU000442};
KW   DNA-binding {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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020};
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          35..96
FT                   /note="DNA polymerase alpha catalytic subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12254"
FT   DOMAIN          410..710
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          775..1227
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1266..1455
FT                   /note="Zinc finger DNA-directed DNA polymerase family B
FT                   alpha"
FT                   /evidence="ECO:0000259|Pfam:PF08996"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..253
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1462 AA;  165971 MW;  38AA62D8156D79EE CRC64;
     MAPVHGDDSV SDSGSFVASR ARREKKSKKA CQEALEKLKR AKAGEKCKYE VEDFTSVYEE
     VDEEQYSKLV QARQDDDWIV DDDGIGYVED GREIFDDDLE DDALDAGEKG KHGKARNKDK
     RNLKKPAVTK PNNIKSMFIA CAGKKTADKA VDLSKDDLLG DILQDLNTET PQITPPPVMI
     LKKRTSIGAS LNPFSVHTPT AVPSGKIAFP VSRKEPPLTP VPLKCAEFAG EPVQAESTEE
     EQESGPMEFE DGDFDEPMEA EEVDLEPVAA KTWDQESEPA EEVKQEVDPG KGTMSYLGSV
     FPDVSCWDVD QEGDSSFSVQ EVQVDSSHLP LVKGADEEQV FHFYWLDAYE DQYNQPGVVF
     MFGKVWIESA ETHVSCCVMV KNIERTLYIL PREMKIDLNT GKETGTPVSM KDVYEEFDEK
     IATKYKIMKF KSKPVEKNYA FEIPDVPEKS EYLEVKYSAE MPQLPQDLKG ETFSHVFGTN
     TSSLELFLMN RKIKGPCWLE VKSPQLLNQP ISWCKVEAMA LKPDLVNVIK DVSPPPLVVM
     AFSMKTMQNA KIHQNEIIAI AALVHHSFAL DKAAPQPPFQ SHFCVVSKPK DCIFPHDFKE
     EIEKKNVKLE VAATERTLLG FFLAKVHKID PDIIVGHNIY GFELEVLLQR INVCKAPHWS
     KIGRLKRSNM PKLGGRSGFG ERSATCGRMI CDVEISAKEL IRCKSYHLSE LVQQILKIER
     AVIPMENIQN MYSESSQLLY LLEHTWKDAK FILQIMCELN VLPLALQITN IAGNIMSRTL
     MGGRSERNEF LLLHAFYENN YIVPDKQIFR KPQQKLGDED EEIDGDTSKY KKGRKKAAYA
     GGLVLDPKVG FYDKFILLLD FNSLYPSIIQ EFNICFTTVQ RVAAEAQKIT EDGEQEQIPE
     LPDTNLEMGI LPREIRKLVE RRKQVKQLMK QQDLNPDLIL QYDIRQKALK LTANSMYGCL
     GFSYSRFYAK PLAALVTYKG REILMHTKEM VQKMNLEVIY GDTDSIMINT NSTNLEEVFK
     LGNKVKSEVN KLYKLLEIDI DGIFKSLLLL KKKKYAALVV EPTSDGNYDT KQELKGLDIV
     RRDWCDLAKD TGSFVIGQIL SDQSRDTIVE NIQKRLIEIG ENVLNGSVPV SQFEINKALT
     KDPQDYPDKK SLPHVHVALW INSQGGRKVK AGDTVSYIIC QDGSNLTASQ RAYAPEQLEK
     QDNLTIDTQY YLAQQIHPVV ARICEPIDGI DAVLIATWLG LDPTQFRVHH YHKDEENDAL
     LGGPAQLTDE EKYRDCERFK CRCPTCGTEN IYDNVFDGSG TDMEPSLYRC SNIDCNASPL
     TFTVQLSNKL IMDIRRFIKK YYDGWLICEE PTCRNRTRHL PLQFSRTGPL CPACMKATLQ
     PEYSDKSLYT QLCFYRYIFD VECALEKLTT DHEKDKLKKQ FFTPKVMQEY RKLKNTAEQF
     LSRSGYSEVN LSKLFAGCAV KS
//
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