ID Q013X2_OSTTA Unreviewed; 1530 AA.
AC Q013X2;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=OT_ostta08g00710 {ECO:0000313|EMBL:CAL54807.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CAL54807.1, ECO:0000313|Proteomes:UP000009170};
RN [1] {ECO:0000313|Proteomes:UP000009170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAL54807.1}.
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 EMBL; CAID01000008; CAL54807.1; -; Genomic_DNA.
DR RefSeq; XP_003080639.1; XM_003080591.1.
DR STRING; 70448.Q013X2; -.
DR GeneID; 9833439; -.
DR KEGG; ota:OT_ostta08g00710; -.
DR InParanoid; Q013X2; -.
DR OMA; WCELAKS; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000009170; Chromosome 8.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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:UP000009170};
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 19..88
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 445..762
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 827..1284
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1323..1525
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 75..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..253
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1530 AA; 168782 MW; 670F04514FCBE498 CRC64;
MSDRRARSSK AAKALELTAR LREQREGDKK RSRIDEAADE ADAIENVYDE LDEDAYRALV
AKRREAGVDF VVNDAGEGYD DLGEEEDWTT ANPNYSDDEE DAPKAKGAKA TEKKAKATAD
EKAAKANAKA KGNAGMLLGG VQKKKKLDEV AADADADAIL EDIFAEVDMF NASTPATVLA
RRAAPVAATA PVAPRRSPRK IAQATAAAAN VRSPVKADPS PAKKSVRFET EEDEPAPQGD
IGGFDDDDND VDLDEAMPEV DPIDTDEPNY KSVEIAKAVQ PPAPQSILKT LDEDEHEEDL
ATITQDAAPV TFNGVELPKD ADGSIPFFFM DAHEERESPG TVFLFGRVPV SSEPGAETIS
ACAVVQNMER CMYVIPTAST FDDPDDELME LADKMDEARR KFKTCTDADK LEEAKVAAQK
AKADLMKRLV PKSGALRAEI KELLKKRGIE NSKITIVRRH YCFERKDIPH GSLFVLKVKT
PATQSAFPSD LKGTNFIAMM GTQAPMLELL TLKSKLKGPS WISLHGASIV PSEKQKSWCK
LEMSIPHAHK GVRPASNEAA TRSAPKLTVA SLNLQTIVNH QTNVNEIALA SVQYIRDVDC
EGTTAPQQIR QGVRHFSVVR KLDGLELPQG WQNAVANENS TNVVAKRTGT VVLSSQNNEL
GLLNFLLAKL HQLDPDVIVG HNIGGFNLDV LLRRFQANKI GHWSRIGRMK RTRMPNINGS
GGAYGGGASL GAMQCITGRL LADTYLSAKD LLGKEVSYTL SSLSQTQLNV RREEIAGAEI
PNHYMQTQSL MHLIKCTEID AKLSLHLMFK MEVIPLTKQL SNIAGNLWSK TLGHTRAQRV
EYLLLHEFHK RKHILPDRLS SKERRRVAAV NGDEEDDGGK KGPSYAGGLV LEPKKGLYDD
FVLVLDYQSL YPSIIQEYNI CYTTVKRHFN DGDDPTIQLP PSVSNDKDFA VLPAVIASIV
RSRKDVKGLM AKESDPARKK QYDLRQLALK LTANSMYGCL GFSQSRFYAE AIAALITSQG
RTILQHTVDL ARQKCDLDVI YGDTDSIMVN TGTKNLDQAR AAGNKLIRFV NREYRKLVLE
EDYAFRSMLL LKKKKYAAMK VVNGPNGTKM TELEMKGLDI VRRDWAPLVK EIGKQTLEEL
LEVDGELEER VTAIHDLLRE IRVEMVANRV PLDKYIITKQ LTKAVEEYPD AKHQPHVMVA
KRRLEAGKQD GVRAGETVPY IIAMESDASL EDIASGKAGA TGGKGLAERA YHPDEVKERN
LKIDLHYYLS QQVHPVISRL CAPIEETDGA KMAECLGMDS NKFKSQSRED DLDDGSGGGV
FGLDDQERFH DCAPLLLRTS DGVEFPFRGV REVADGKLHV NEALAPPTPD ADKENTPATQ
GKSTKKFVSG ASLTNQVILA ARARIKEFYA APLRSNDDVD RTETHNIALR VHHTNAALTG
TLSADPMSTG TMEKTVPEEK LYNQLLFYKK LLSIEDAKRG MTDDEQRKTF LAGTELEKSL
TAANEALDKI MDKSSYKWIA LSELFRVGSV
//
