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Database: UniProt
Entry: J8PQB5_SACAR
LinkDB: J8PQB5_SACAR
Original site: J8PQB5_SACAR 
ID   J8PQB5_SACAR            Unreviewed;      1097 AA.
AC   J8PQB5;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   05-JUN-2019, entry version 42.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=SU7_0510 {ECO:0000313|EMBL:EJS44355.1};
OS   Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS44355.1};
RN   [1] {ECO:0000313|EMBL:EJS44355.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H-6 {ECO:0000313|EMBL:EJS44355.1};
RX   PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA   Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA   Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA   Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT   "High quality de novo sequencing and assembly of the Saccharomyces
RT   arboricolus genome.";
RL   BMC Genomics 14:69-69(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={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|RuleBase:RU000442}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EJS44355.1}.
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DR   EMBL; ALIE01000036; EJS44355.1; -; Genomic_DNA.
DR   EnsemblFungi; EJS44355; EJS44355; SU7_0510.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005657; C:replication fork; IEA:EnsemblFungi.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:EnsemblFungi.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:EnsemblFungi.
DR   GO; GO:0045005; P:DNA-dependent DNA replication maintenance of fidelity; IEA:EnsemblFungi.
DR   GO; GO:0006278; P:RNA-dependent DNA biosynthetic process; IEA:EnsemblFungi.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 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; IPR042087; DNA_pol_B_C.
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   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; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      143    482       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      546    973       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1009   1080       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     38       Disordered. {ECO:0000256|MobiDB-lite:
FT                                J8PQB5}.
FT   COILED       72     92       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS      1     32       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                J8PQB5}.
SQ   SEQUENCE   1097 AA;  124612 MW;  24E7507CDF0B16E3 CRC64;
     MSEKRSLPMV DVKMDDEDTP KLEKKIKRQS IDHGVGSEPV STIEIIPTDS FRKYNSQGFK
     AKDTDLMGTQ LESTFEQELS QMEHDLADKE ERDLSSFERN KLPSDFDPNT YDISFQQIDA
     EQSVLNSMKD ENTSTVVRFF GVTSEGYSVL CNVTGFKNYL YVPAPNSSDA DDQEQINKFI
     HYLNETFDHA VDSIEVVSKQ SIWGYSGDTK LPFWKIYVTY PHMVNKLRTA FERGHLSFNS
     WFSNGTTTYD NIAYTLRLMV DCGIVGMSWI TLTKGKYSMI EENNRVSSCQ LEVSINYRNL
     IAHPAEGDWS HTAPLRIMSF DIECAGRIGV FPEPEYDPVI QIANVVSIAG AKKPFIRNVF
     TLNTCSPITG SMIFSHATEE EMLSKWRDFI IKADPDVIIG YNTTNFDIPY LLNRAKALKV
     NDFPYFGRLK NVKQEIKESV FSSKAYGTRE TKNVNIDGRL QLDLLQFIQR EYKLRSYTLN
     AVSAHFLGEQ KEDVHYSIIS DLQNGDSETR RRLAVYCLKD AYLPLRLMEK LMALVNYTEM
     ARVTGVPFSY LLARGQQIKV VSQLFRKCLE IDTVIPNMQS QASDDQYEGA TVIEPIRGYY
     DVPIATLDFN SLYPSIMMAH NLCYTTLCNK GTVERLDFKL DEDYVITPNG DFFVTAKRRR
     GILPIILDEL ISARKRAKKD LRDEKDPFKR DVLNGRQLAL KISANSVYGF TGATVGKLPC
     LAISSSVTAY GRTMILKTKN AVQEKYCIKN GYTHDAVVVY GDTDSVMVKF GTTDLKEAMD
     LGTEAAKYVS TLFKHPINLE FEKAYFPYLL INKKRYAGLF WTSPEKFDKL DQKGLASVRR
     DSCSLVSIVM NKVLKKILIE RNVDGALAFV KETINDILHN KVDISKLIIS KTLAPNYTNP
     QPHAVLAERM KRREGVGPNV GDRVDYVIIG GNDKLYNRAE DPLFVLENNI QVDSRYYLTN
     QLQNPIISIV APIIGDKQAN GMFVVKSIKI NTGSQKGGLM SFIKKVEACK SCKGPLKKGE
     GPLCSNCLAR SGELYIKALY DVRDLEEKYA RLWTQCQRCA GNLHSEVLCS NKNCDIFYMR
     VKIKKELQEK VEQLSKW
//
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