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Database: UniProt
Entry: A0A2C5XFQ9_9PEZI
LinkDB: A0A2C5XFQ9_9PEZI
Original site: A0A2C5XFQ9_9PEZI 
ID   A0A2C5XFQ9_9PEZI        Unreviewed;      1812 AA.
AC   A0A2C5XFQ9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   05-JUN-2019, entry version 10.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   Name=REV3 {ECO:0000313|EMBL:PHH55286.1};
GN   ORFNames=CFIMG_003946RAa {ECO:0000313|EMBL:PHH55286.1};
OS   Ceratocystis fimbriata CBS 114723.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Microascales; Ceratocystidaceae;
OC   Ceratocystis.
OX   NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH55286.1, ECO:0000313|Proteomes:UP000222788};
RN   [1] {ECO:0000313|EMBL:PHH55286.1, ECO:0000313|Proteomes:UP000222788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH55286.1,
RC   ECO:0000313|Proteomes:UP000222788};
RX   PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA   Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J.,
RA   Wingfield B.D.;
RT   "Analysis of microsatellite markers in the genome of the plant
RT   pathogen Ceratocystis fimbriata.";
RL   Fungal Biol. 117:545-555(2013).
RN   [2] {ECO:0000313|EMBL:PHH55286.1, ECO:0000313|Proteomes:UP000222788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH55286.1,
RC   ECO:0000313|Proteomes:UP000222788};
RX   PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA   Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W.,
RA   Wingfield B.D.;
RT   "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence
RT   for the plant pathogen, Ceratocystis fimbriata.";
RL   IMA Fungus 4:357-358(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:PHH55286.1}.
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DR   EMBL; APWK03000013; PHH55286.1; -; Genomic_DNA.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000222788; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
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; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; PTHR45812; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 2.
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   Complete proteome {ECO:0000313|Proteomes:UP000222788};
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   Reference proteome {ECO:0000313|Proteomes:UP000222788};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       49    194       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      935   1122       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1199   1659       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1699   1788       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      616    652       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2C5XFQ9}.
FT   REGION      902    928       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2C5XFQ9}.
FT   COMPBIAS    616    633       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A2C5XFQ9}.
FT   COMPBIAS    912    928       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A2C5XFQ9}.
SQ   SEQUENCE   1812 AA;  201406 MW;  39B38A146748D942 CRC64;
     MDGFRVQINA IDHYQAPPSP YTPVLRNDVS ASQAYQLPHV PVIRIFGATT AGQKVCAHVH
     GFFPYVYVPY EGSLEPKKVG AYIYRLHVSI DHALSLIVRR PTSRLSRDPK FVARITLVKG
     VPFYGFHVGY SFFLKIYMFN PNIMNRLVDV LQNGAIMQTR FQPYEAHIQY LSQFMIDYNL
     FGCDWLDADK THFRAPLPEA CEGDARQLPD DGNKNRLRGS ESSLSLLYND STVPACFVTD
     DSTLPRSSYC TLEVDITVCD ITNRRSLTER CLHHDFIERL YPVPESVKLV PSMAGLWRSE
     EQRRRALGLL ASNSSPFPPD VLVSMSPDKK GTIETGFMGE EEQRKQVAQL IKAEYDPNIT
     PSFETFVKHH PRADTVRTVM ESVEDLYPDN LQAVLGLAPQ GVDDASVENP SLEDIEVDEV
     QISLSQDPIN DDVANEIQDA EDIDHMNGQA QRDFGAQSPE AAENEEANIE GLLASFVGLS
     RSGLYSGTPP KISVDTNLIE AACSDRFSPG LRRVPGTTKA RGKRFFTSSP AVTPDFNRKK
     MKIGPDPSFV PAAIKESGPL DVEETLAKGK ANYDKKRVSF KPLMDANQAL SVQRDSQPAM
     TEDGHNIEGW LQRNTDLISS SPESPSTPAT SRHNRAGFMH HSPLPVRSSQ DALSPAGSQL
     FIASSRAPPV SPFLLRTPRN AQRSLIFTTP FKTPLSKLSW AVSSSPFSIR KVGCSSSPFP
     ACKQTPGSTT RSLLLQRTAR THTFVFSTPP PQVAEVCSSF EQYDLPEVIN EEVTYSVEAD
     VPARPHEYGG KTFRLRSNTL PFLPEFEIDA GHASSNSNLL DEPGSKINKA RAIASQSRSL
     PQDVRCQMCS IKSWDFFPPP PSFQEVKAWD MARHVASMSS SRPNQCLSSQ SILRSQRFAS
     QIDGPTPAKR GSVAITASQR QRSTGLKPET RSMSILAIEV HVNTRGKLMP NPEHDSVQFV
     FWSLQTDQSY DDVVDLEDPT PDQAGIVSGV IVLSEESTEL AQRIKKQTKW VVQAEDTELE
     VLTAVAAMVR RFDPDILTGF EVHSGSWGFL LERAATKYEY DLGEDLSRMR GDLASRLHKD
     GNGARWAFTK TSTVKVTGRH TINIWRAMRG EMSLSQYTME NVAWHLLGRR IPHYSHAVLT
     AWHKASSSAD ACAGGGHRAM ARLLRYYQLR TRLDLEILEA NELVARTREQ ARLLGVDFFS
     VISRGSQFKV ESMMGRIAKP ENYVFVSPSR KQVGGQNALE CLPLVMEPQS ALYTDPVVVL
     DFQSLYPSVM IAYNYCYSTF LGRIVGWGSG ATNKMGFTQY TRAKHLLTLV QNSVTIAPNG
     MMYVTPAVRT SLLAKMLREI LETRVMVKSG MKNAKKSVHQ LLNNRQLALK LLANVTYGYT
     SASYSGRMPC AEIADSIVQT SRETLERAIA LIHTHPSWKA EVVYGDTDSL FIRLPGRTKA
     SAFSIANEMA VAITAANPRP VKIKFEKIYQ PCVLLAKKRY VGYKWEHPSQ DIPVFEAKGI
     ETVRRDGTPG EQKIQEKVLR TLFDTADLSR VKAYFQRQCD KILRGHVSLQ DFCFAKEVKL
     GTYADSSGGV HNYRRPNQPQ PPALPPGALL AARKMLVDGR AEPQYGERVP YLVIAGAPGS
     RLSDRCVAPS EVLDSPDAEL DADYYINKNI IPAIDRILQL VGASAKRWYD EMPKVKRVRR
     IDPKRRSAIL EAYLSVAACI ACKSHLPPRT AGTAITAKAT PGGGAGDALI CMRCLAQRPQ
     TLTTIQRRMS ALSTSLGNIR AVCRSCAATA FGDDIDCDSL DCSVFWTRSK MEARTRSEGE
     MLREAERKLL EW
//
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