ID A0A2K5N6E5_CERAT Unreviewed; 1465 AA.
AC A0A2K5N6E5;
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:ENSCATP00000032905.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000032905.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000032905.1}
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_011891001.1; XM_012035611.1.
DR Ensembl; ENSCATT00000057176.1; ENSCATP00000032905.1; ENSCATG00000039397.1.
DR GeneID; 105574605; -.
DR KEGG; caty:105574605; -.
DR CTD; 5422; -.
DR GeneTree; ENSGT00550000074891; -.
DR OMA; MTKMNVG; -.
DR OrthoDB; 5477697at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000039397; Expressed in bone marrow and 12 other cell types or tissues.
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:UP000233060};
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 38..99
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 413..713
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 778..1230
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1269..1458
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1465 AA; 165980 MW; 312A141AED4F9636 CRC64;
MAPVHGDGCE IGASDSGSFV ASRARREKKS KKGRQEALER LKKAKAGEKY KYEVEDFTGV
YEEVDEEQYS KLVQARQDDD WIVDDDGIGY VEDGREIFDD DLEDDALDAG EKGKDGKARN
KDKRNVKKPA VTKPNNIKSM FIACAGKKTA DKAVDLSKDD LLGDILQDLN TETPQITPPP
VTILKKKRSI GASPNPFSVH TSTAVPSGKI ASPVSRKEPP LTPVPLKRAE FAGEPIQVES
TEEEQESGAM EFEDGDFDEP METEEVHLEP MAAKAWDQES EPAEEVKQEA DSGKGTMSDL
GRFLPDVSCW DIDQEGDSSF SVQEVQVDSS QLPLVKGADE EQVFHFYWLD AYEDQYNQPG
VVFLFGKVWI ESAETHVSCC VMVKNIERTL YFLPREMKID LNTGKETGTP VSMKDVYEEF
DEKIATKYKI MKFKSKPVEK NYAFEIPDVP EKSEYLEVKY SAEIPQLPQD LKGETFSHVF
GTNTSSLELF LMNRKIKGPC WLEVKSPQLL NQPISWCKVE AMALKPDLVN VIKDVSPPPL
VVMAFSMKTM QNAKNHQNEI IAVAALVHHS FALDKAAPKP PFQSHFCVVS KPKDCIFPYA
FKEVIEKKNV KVEVAATERT LLGFFLAKVH KIDPDIIVGH NIYGFELEVL LQRINVCKAP
HWSKIGRLKR SNMPKLGGRS GFGERNATCG RMICDVEISA KELIRCKSYH LSELVQQILK
TERVVIPTGD IRNMYSESSQ LLYLLEHTWK DAKFILQIMC ELNVLPLALQ ITNIAGNIMS
RTLMGGRSER NEFLLLHAFY ENNYIVPDKQ IFRKPQQKLG DEDEEIDGDT NKYKKGRKKA
AYAGGLVLDP KVGFYDKFIL LLDFNSLYPS IIQEFNICFT TVQRVASEAQ KVTEDGEQEQ
IPELPDPSLE MGILPREIRK LVERRKQVKQ LMKQQDLNPD LILQYDIRQK ALKLTANSMY
GCLGFSYSRF YAKPLAALVT YKGREILMHT KEMVQKMNLE VIYGDTDSIM INTNSTNLEE
VFKLGNKVKS EVNKLYKLLE IDIDGIFKSL LLLKKKKYAA LVVEPTSDGN YATKQELKGL
DIVRRDWCDL AKDTGNFVIG QILSDQSRDT IVENIQKRLI EIGENVLNGS VPVSQFEINK
ALTKDPQDYP DKKSLPHVHV ALWINSQGGR KVKAGDTVSY VICQDGSNLT ASQRAYAPEQ
LQKQDNLTID TQYYLAQQIH PVVARICEPI DGIDAVLIAT WLGLDPTQFR VHHYHKDEEN
DALLGGPAQL TDEEKYRDCE RFKCPCPTCG TENIYDNVFD GSGTDMEPSL YRCSNIDCKA
SPLTFTVQLS NKLIMDIRRF IKKYYDGWLI CEEPTCGNRT RHLPLQFSRT GPLCPACMKA
TLRPEYSDKS LYTQLCFYRY IFDAECALEK LTTDHEKDKL KKQFFTPRVL QDYRKLKNTA
EQFLSRSGYS EVNLSKLFAG CAVKS
//