ID I3KAC7_ORENI Unreviewed; 1357 AA.
AC I3KAC7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000018072.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000018072.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 STRING; 8128.ENSONIP00000018073; -.
DR Ensembl; ENSONIT00000018087.2; ENSONIP00000018072.2; ENSONIG00000014373.2.
DR eggNOG; KOG0970; Eukaryota.
DR GeneTree; ENSGT00550000074891; -.
DR TreeFam; TF103001; -.
DR Proteomes; UP000005207; Linkage group LG9.
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: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:UP000005207};
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 34..95
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 364..609
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 674..1124
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1164..1350
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1357 AA; 154032 MW; D4F127C9BB901AD4 CRC64;
IAPDLSNHTH ISCGLAKTRS RREKREKVGR KSALEQLKKA KMGEKIKYEV KEFSSVYEEV
DEDEYSKMVR ERQEDDWIID DDGTGYVEDG REIFDDDLDD DVVEDKRGDS KKNVKKSVVA
KPNSIKSLFM NSNVKRPAEK DVDLSKDDLL GDILQDLHSE KPALLTPPPV VTLKKKKSVG
SPMNPFSIKP QLPKFLAVSL LCSLSRSSRI GSSWGQEEEG GANDAPAEVQ VDSSQLPLVE
GPDGEQVFRF YWLDAFEDPY NQPGVVYLFG KVWIESAKSH VSCCVSVKNI ERTMYLLPRE
YTNPRTGEVS NTPVGMMDVY QEFNELSEKF KIMKFNHVFS LCLISFSCPT ESGEELCAEF
PSLPSDLKGA TFSHIFGTNT SRLEHFLLSR KIKGPCWLDI KSPQLMNQPV SWCKVEALSL
RSDLISVVKD LPPPPLTVMS ISLKTVQNPK THQNEIVSLA ALIHYRFHMD KAPPQPPYQT
HFCVISRPAD CIFPYDFKEA VRKKNGKVEI ASTERTLLGF FLAKMHKIDP DVLVGHDIFG
FDLEVLLQRI NVCKVPHWSK IGRLRRSNMP KLGGRSAFAE KNATCGRLVC DVEISAKELI
RCKSYHLTEL TAQVLKTERI TVPQEDIKNL YSDSPHLLYL LELTWTDAKL ILQIMCELNV
LPLALQITNI AGNVMSRTLM GGRSERNEFL LLHAFHEKDY IVPDKPSFKK AQLETAEGED
DVDAGKGKRK KKAAYAGGLV LDPKVGFYDK FVLLLDFNSL YPSIIQEFNI CFTTVQREAQ
NSQKKKEVED EPEEIPEIPD PNLEMGILPK EIRKLVERRK QVKGLMKQQD INPDLYLQYD
IRQKALKLTA NSMYGCLGFS YSRFYAKPLA ALVTHKGREI LMHTKDMVQK MNLEVIYGDT
DSIMINTNSK CLDEVFKLGN KVKAEVNKLY KLLEIDIDGV FKSLLLLKKK KYAALVVEPN
GEGRFSVKQE LKGLDIVRRD WCDLAKECGN YVIGQILSDQ SRDVIVENIQ KHLVELGEKV
ASGDIPLNQY EIHKALTKDP QDYPDKKSLP HVHVALWINS QGGRRVKAGD TISYLICKDG
SNLPASQRAY ALEQLQKQEN LTLDTQYYLA QQIHPVVSRI CDPIEGIDGV LVASWLGLDP
SQFRAQQQFQ REEEADGLLG VPVQLTDEER YKDCERFTFT CPQCGTDNIY DGVFEGAGAK
VEPSLMRCCH IPCGGSPADY IVNISNKLVL DIRRHIKRYY AGWLMCEDQA CQNRTRRLPI
AFSRHGPICP ACSRATLRPE YSEKALYNQL CFYRFIFDWE YAVTKVLNPE ERSKIIHTQG
QHYVYRKLKE VPDKALASSG YSEINLAKLF QAFSSLK
//
