ID A0A3B4TBZ6_SERDU Unreviewed; 1474 AA.
AC A0A3B4TBZ6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000003623.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000003623.1}
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 STRING; 41447.ENSSDUP00000003623; -.
DR Ensembl; ENSSDUT00000003704.1; ENSSDUP00000003623.1; ENSSDUG00000002748.1.
DR GeneTree; ENSGT00550000074891; -.
DR OMA; MTKMNVG; -.
DR OrthoDB; 5477697at2759; -.
DR Proteomes; UP000261420; 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: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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 44..105
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 432..727
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 792..1241
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1281..1467
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1474 AA; 166402 MW; A06D7EB088C6C9C1 CRC64;
MAPVSNPDKD MDGPDGDDGG DACGLARSRS RREKREKVGR KSALEQLKKA KMGEKVKYEV
EEFTSVYEEV DEEQYSKMVR ERQEDDWIID DDGTGYVEDG REIFDDDLDD DVVENNKGKP
SARGADSKKT AKKSVVAKPN TIKSLFMNSN VKRPAEKDVD LSKDDLLGDI LQDLHSEKPS
PLAPPPVVTL KKKKSLGSPM NPFSIKPPKE SPSATGLKAK VIRPPPPDLT PKPSARPPPS
KPALPMERQR AKVEELDEEE VNEALAFDGV DFDEPMEVGL EEEKPAVTEN TEPESKVAAV
TAVKVEPKAE PEDPALLPSR IGSSWGQEEE GEASEAPVEV QVDSSQLPLL EGADGEQVFR
FYWLDAFEDP YTQPGVVYLF GKVWIESAKS HVSCCVTVKN IERTMYFLPR EYKVNPKTGE
VSETPVGMMD VYQEFNEISE KFRIMKFKSK KVEKNYSFEI PDVPSQCEYL EVRYSAEFPG
LPSDLKGATF SHIFGTNISS LEHFLLSRKI KGPCWLDIKT PQLIGQPVSW CKVEALALRS
DLVTVVKDLS PPPITVMSIS LKTIQNPKTH HNEIVSLAAL VHCQFYMDKA PPQPPYQAHF
CVVSKPVDCI FPYDFKEAVR KKNGKVEIAA TERTLLGFFL AKMHKIDPDV LVGHDIFGFD
LEVLLQRINA CKVPHWSKIG RLRRANMPKL GGRGSFAEKS ATCGRLVCDV EISAKELIRC
KSYHLTELAV QVLKTERVTV PQEEIKNLYS DSPHLLYLLE LTWTDAKLIL QIMCELNVLP
LALQITNIAG NVMSRTLMGG RSERNEFLLL HAFHEKNYIV PDKPSFKKAQ LDTAEGDEDV
DAGKGKRKKK AAYAGGLVLD PKVGFYDKFV LLLDFNSLYP SIIQEFNICF TTVQREAHNK
QKKNEEDEPE EIPEIPDSDL EMGILPKEIR KLVERRKQVK QLMKQQDINT DLYMQYDIRQ
KALKLTANSM YGCLGFSYSR FYAKPLAALV THKGREILMH TKDMVQKMNL EVIYGDTDSI
MINTNSRSLE EVYKLGNKVK AEVNKLYKLL EIDIDGVFKS LLLLKKKKYA ALVVENHGDG
QYSVKQELKG LDIVRRDWCD LAKECGNYVI GQILSDQSRD VIVENIQKHL VEVGEKVASG
AIPLNQYEIN KALTKDPQDY PDKKSLPHVH VALWINSQGG RRVKAGDTVS YIICKDGSTL
AASQRAYALE QLQKQEGLSL DTQYYLAQQI HPVVSRICDP IEGIDTVLIA TWLGLDPSQF
RSQQQYQREE EADGMLGAPV QLTDEERYKD CERFTFTCPQ CGTNNIYDSV FEGAGSKLEP
SLMRCCHIPC GSRPLDYAVN ISNKLLLEIR RHIKKYYSGW LVCEDQACQN RTRRLPIAFS
RHGPICPSCT RATLRPEYSE KALYNQLCFY RFIFDWDYAI AKVLQGDEKS YVNGLSKTRE
VYQKLKEVPD KALATSGYSE INLAKLFQAF SSLK
//
