ID A0A3B4AGT0_9GOBI Unreviewed; 1380 AA.
AC A0A3B4AGT0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000015885.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000015885.1}
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; 409849.ENSPMGP00000015885; -.
DR Ensembl; ENSPMGT00000016951.1; ENSPMGP00000015885.1; ENSPMGG00000013016.1.
DR Proteomes; UP000261520; 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 37..97
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 354..648
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 713..1157
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1196..1373
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..148
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 13..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 157512 MW; DF25F07A11571CC4 CRC64;
MAPVSNPDKD MDVPDCGLAK SRSRREKREK FGRKSALEQL KKAKKGEKIK YEVEEFTSVY
EEVDEEEYSK MVRDRQEDDW IIDDGTGYVE DGREIFDDDL EEDVVETKKK AGAKGAESKK
NTKKTSVSKP NTIKSLFMNS NVKRPAEKDV DLSKDDLLGD ILQDLHSEKS SALTPPPVVT
LKKKKALGSP MNPFSIKSPK NNAMALDEVD FDEPMDVADE AEKPVMKEEL EPEVKTAPAQ
TTVKVQPKEE PQDPVLEETA PAEVQVDPSQ LPLVEGPEGE MVFRFYWLDA FEDPYTQPVV
YLFGKVWIES AQSHVSCCVS VKNIERTMYL LPREFKVNPK TGEASDTPVR IMDIYHEFNE
LSEKFKIMKF KSKKVEKNYA FEIPDVPTQC EYLEVRYSAE LPPLPSDLKG ETFSHVFGTN
TSSLEHFLLS RKIKGPCWLD IKTPLMSQPV SWCKVEALAL RTDLISVVRD LPPPPVTVMS
ISLKTVQNPK THQNEIVSLA ALIHCRFHMD KAPPQPPFQT HFCVSKPTDC IFPYDFSDAV
KKKNGKVEIA GTERTLLGFF LAKMHKIDPD VLVGHDIFGF DLEVLLQRIN VCKVPHWSKI
GRLRRTNMPK LGGRSSFAEK NATCGRLVCD VEISAKELIR CKSYHLTELV AHVLKMERPT
VPQENIRNLY DSPHLLYLLE LTWTDAKLIL QLMCELNVLP LALQITNIAG NVLSRTLMGG
RAERNEYLLL HAFNEKNYIV PDKPSFRKVQ QEQVEGEEDV GKRKKKAAYS GGLVLDPKVF
YDKFILLLDF NSLYPSIIQE FNICFTTVER EVYNSQKKKK EGIEEIPEIP DSSLEMGILP
KEIRKLVERR KQVKQLMKQQ QDLNPDLYLQ YDIRQKALKL TANSMYGCLG FSYSRFYAKP
LAALVTHKGR EILMHTKDMV QKMNLEVIYG DTDSIMINTN SKSLEEVFKL GNKVKAEVNK
LYKLLEIDID GVFKSLLLLK KKKYAALVVE QHGEGRYTLK QELKGLDIVR RDWCDLAKEC
GYVIGQILSD QSRDVIVENI QKHLVEMGEK VAAGAIPLTL FEIHKFQALT KDPQDYPDKK
SLPHVHVALW INSQGGRRVK AGDTISYVIC KDGSTLPASQ RAYALEQLQK QESLSLDTQY
YLAHQVHPVV SRICDPIEGI DNVLIATWLL DPGQFRAQQQ HQREEEADGT LGAPVQLTDE
ERYRDCERFT FTCPQCGTDN IYDNVFEGAG LKLEPSLMRC CHIPCGSRPI DYTVNISNKL
LLDIRRHIKK YYSGWLVCED LACQNRTRRI PIAFSRHGPI CPACTRATLR PEYSEKALYN
QLCFYRFIFD WEHAVNKVLP PDDKKDVYRR LKEVPDKALA ISGYSEINLS KLFQAFSFLK
//
