UniProt: A0A2H3GSD9

Database: UniProt
Entry: A0A2H3GSD9_FUSOX

LinkDB:  A0A2H3GSD9_FUSOX 
Original site:  A0A2H3GSD9_FUSOX

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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (2)   
   PubMed (2)   
All databases (30)   

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ID   A0A2H3GSD9_FUSOX        Unreviewed;      1694 AA.
AC   A0A2H3GSD9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=AU210_009667 {ECO:0000313|EMBL:PCD33441.1};
OS   Fusarium oxysporum f. sp. radicis-cucumerinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD33441.1, ECO:0000313|Proteomes:UP000219602};
RN   [1] {ECO:0000313|EMBL:PCD33441.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD33441.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA   van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA   Rep M.;
RT   "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL   Environ. Microbiol. 18:4087-4102(2016).
RN   [2] {ECO:0000313|EMBL:PCD33441.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD33441.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA   van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA   Brankovics B., Houterman P.M., Arie T., Rep M.;
RT   "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT   multiple cucurbit species.";
RL   Sci. Rep. 7:9042-9042(2017).
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   -!- 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}.
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:PCD33441.1}.
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DR   EMBL; MABQ02000006; PCD33441.1; -; Genomic_DNA.
DR   STRING; 327505.A0A2H3GSD9; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000219602; Chromosome 8.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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   CDD; cd05778; DNA_polB_zeta_exo; 1.
DR   CDD; cd05534; POLBc_zeta; 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; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA 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|RuleBase:RU000442};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
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   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};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219602};
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          857..1036
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1103..1549
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1590..1662
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          281..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1694 AA;  192911 MW;  B4F44A95FB7984CD CRC64;
     MDLFRVRLNC IDHYQATPSR YDPQLRNDIR PSQISKGPRV PVVRVFGSTE TGQKVCAHIH
     GAFPYLYVEY EGGLSPDEVG AYIYRFHLSI DHALAVSYRR DQKGGSARFV ARITLVKAVP
     FYGFHVGYRF FLKIYMFNPI VMTRLADLLQ QGVIMKNKFQ PYEAHLQYLL QFMTDFNLYG
     CDYLDASVTR FRSPVPEYEQ GSSSLHKWHS RSISVDHITD ETTLPRSSHC SIEVDICVQD
     IINRHKVKER PLHHGFTERT NPLPGDMKLV YSMAGLWKDE TKRRKRKMQD PTEGSSPFPP
     EVLVSMSANA RDSQPQGWLH EEEFRTEIQN LISEEKLSVD PEELTFETFA KPHPYEEHVN
     TTLESVEDLF PSKLAPALGL PFGMEAEQDL RSSIVVDEGK VRQVGEAHND FYPEDSDEDA
     IAALVAIEKA AAKVSRGPTD QLPQEDLELA AALNINPDKF DKKTFWRSAL GVCQSRLVTG
     ELPDLPVNQE LLDYAEDEGF IGRTEKAPTL TSSNLTQLKR PLDDLLSSQA SNKRTRLNQL
     SMVDEDEMDL VPVPSADANK NLASSFRGAS ILKGPPSLNK NTGSVLKGAS GSNQKLNFPT
     VKDQNDPNTK LRLSQMSQKS ASQQTDDGRH TKHVSFDPSG FLPAEAELPQ MALSSSMKSS
     GGREEDESHE SKIQRAMSRF ASQQVYLVSS LPPSAAAVAS SLKQYGLPDV IYQDAYYSRE
     KDVPGRMREY AGKEFRLESN TLPFLPEFDP TGTAPANYGL KYETFDKTTA ELRYERQRKK
     CSLRSWELTN PPPTYQEVEE WWAEKERRAN ATEGFKISLT PRQYQSQIDG PTPKNKHGFK
     YTPGKKSTSV QHEIQYMSTM SLEVHVNTRG KFVPNPEEDE VQCVFWAIKS DGTASGSQDS
     AGVQTGILLL SNDAEFTQRI QRQTNAEVIE ENSELDLMVR MVEIVRNHDP DILTGYEVHG
     SSWGYLIERA RLKYDYNLCD EFSRMKTESH GRFGKENDRW GFNTTSTIRV TGRHMVNVWR
     AMRGELNLLQ YTMENVVWHM LHRRIPRYSW QSLTNWYKGG KHRELNRMLR YYQNRTKIDL
     EILDANELVS RTSEQARLLG VDFFSVFSRG SQFKVESIMF RIAKPENFLL VSPNRKQVGG
     QNALECLPLV MEPQSAFYNS PLLVLDFQSL YPSVMIAYNY CYSTFLGRVT DWRGMNKMGF
     TEYKRQKGLL ALLEDYINIA PNGMMYAKTE IRKSLLAKML TEILETRVMV KSGMKQDKDD
     KTLQQLLNNR QLALKLLANV TYGYTSASFS GRMPCSEIAD SIVQTGRETL ERAIAYIHSV
     EKWGAEVVYG DTDSLFIYLK GRTKDEAFDI GNEISKAITE MNPRPIKLKF EKVYHPCVLL
     AKKRYVGYKY ESKDQVKPEF DAKGIETVRR DGTPAEQKIE EKALRLLFET ADLSQVKDYF
     QKQCQKIMRN NVSVQDFCFA KEVRLGTYSD KGAPPAGALI STKRMLQDAR AEPQYGERVP
     YVVITGAPGA RLIDRCVAPE ELLSNPHWQL DAEYYISKNL IPPLERIFNL VGANVRQWYD
     EMPKVQRIYH ATTLGKKKTT LESYMKSTNC LVCGLKFSQE DNALCPSCRK NVPSSLLTLQ
     TRLTTEERRL QEVLSLCRSC SGLGPIEDVQ CDSKDCPVFW TRMRQASKTK GQRNASQPVI
     QSLVDSVEKL SLEW
//

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