ID A0A0G4EBR5_VITBC Unreviewed; 1074 AA.
AC A0A0G4EBR5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=Vbra_11193 {ECO:0000313|EMBL:CEL92970.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEL92970.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEL92970.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU000442};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR EMBL; CDMY01000123; CEL92970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4EBR5; -.
DR STRING; 1169540.A0A0G4EBR5; -.
DR VEuPathDB; CryptoDB:Vbra_11193; -.
DR InParanoid; A0A0G4EBR5; -.
DR OMA; CNNCRPR; -.
DR OrthoDB; 211439at2759; -.
DR PhylomeDB; A0A0G4EBR5; -.
DR Proteomes; UP000041254; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05777; DNA_polB_delta_exo; 1.
DR CDD; cd05533; POLBc_delta; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 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; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF14260; zf-C4pol; 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 PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000442}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 153..452
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 517..947
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 984..1053
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 122180 MW; 269CB153E0C1AB66 CRC64;
MSKLDGRKAR PRAALDDDDV DMDADNDDGE PMSKRMRSSD WDDEFEPLKR KDLDAPLDPN
NDRIVFMQID IDQYTGKAKR DMWPQGGIPA PDQEVPILRM FGVTEGGQSV LAHIHGFMPY
FYCQCPDKCR DSAKMRAKLE ERLRVNNRGI KQLVLHVEVV QKQSLMWYVP DSTADTSHFF
RITVAQPRLV PPCRDIIERG LELQPGARVP TTPYATFESN IAFPLRYMID NGVTGGCWVE
VPAGSYQVRS HATTVGLCQI EVDLPYTDLV SLPTDGDYMK LAPLRVLSFD IECVKLEGQG
FPQAEEDPVI QIATVVKIHG DEEPLWKAVF VLGTCAPVAG AHVYTFETEY ELLQRWSDFL
TIVDPDVLTG YNVINFDLNY LITRAGILKV DKFAHIGRIQ TAKSKIRDTV FQSRAYGIRE
NKEINTEGRV QFDVLHAIQR DHKLRSYSLN AVSAHFLNEQ KEDVHYSMIG DLHRGNAETR
QRVASYCLKD ATLPLRLMDH LLCMYNYVEM ARVTGTPLSY LLTRGQQIKV VSQLYRTCLK
LGYIFPYAKQ ESSEEKFEGA TVLEPEKDFY GEPIATLDFA SLYPSIMMAY NLCYCTLIPP
QYVSQMNPDE YTKTPIGHCF VKKDNRQGVL PLVLTELLAA RKRAKKDMNA AQDPLTKMVL
NGRQLALKIS ANSVYGFTGA TVGQLACLEI SSSVTAFGRQ MIDQTKEHVE RRYKVAAGYP
HDAKVIYGDT DSVMVNFGEI SVEEAMKYGL EASQEISKTF PPPIRLEFEK VYCPFLLMNK
KRYAGLIWTK PEKYDKMDCK GIETVRRDWC ELVQKTVDDV LNLILVERSV PQAKECVKRV
VADLLQNKVD MSLLVISKSL AKSANAEDYK AKQPHVELAE RMRARDPTSA PAVGDRVAFV
YIKGHKDARA YEKAEDPLYV LEQNLAIDAQ YYLEHQLKQP IIRIFEPLME RPESLFAGNH
TLKVSVPMPA GGAMAKFVQR SLTCLGCRAP IKEGALCKNC KKKEIEIYLK KLDTFRDREL
EFNKLWSECQ RCQGSLHQDV ICTSRDCPIF YRRERVKRDI AQAAEAMQRL KIDW
//