ID A0A2K5N6F7_CERAT Unreviewed; 1425 AA.
AC A0A2K5N6F7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:ENSCATP00000032915.1};
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:ENSCATP00000032915.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000032915.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSCATT00000057186.1; ENSCATP00000032915.1; ENSCATG00000039397.1.
DR GeneTree; ENSGT00550000074891; -.
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; 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|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 792..1190
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1229..1418
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 1425 AA; 161159 MW; 308537B9F22DE49C 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 ITNIAGNIMG
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
//
