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Database: UniProt
Entry: A0A2W1H2Y2_9PLEO
LinkDB: A0A2W1H2Y2_9PLEO
Original site: A0A2W1H2Y2_9PLEO 
ID   A0A2W1H2Y2_9PLEO        Unreviewed;       796 AA.
AC   A0A2W1H2Y2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPD {ECO:0000256|ARBA:ARBA00014344};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=Ptr86124_000599 {ECO:0000313|EMBL:KAI1520231.1}, PtrM4_006450
GN   {ECO:0000313|EMBL:KAF7576405.1}, PtrM4_02947
GN   {ECO:0000313|EMBL:PWO15637.1};
OS   Pyrenophora tritici-repentis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=45151 {ECO:0000313|EMBL:KAF7576405.1, ECO:0000313|Proteomes:UP000245464};
RN   [1] {ECO:0000313|EMBL:KAF7576405.1, ECO:0000313|Proteomes:UP000245464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M4 {ECO:0000313|EMBL:KAF7576405.1,
RC   ECO:0000313|Proteomes:UP000245464};
RX   PubMed=29685100; DOI=10.1186/s12864-018-4680-3;
RA   Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P.,
RA   Moffat C.S.;
RT   "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici-
RT   repentis reveals chromosomal variations and genome plasticity.";
RL   BMC Genomics 19:279-279(2018).
RN   [2] {ECO:0000313|EMBL:KAI1520231.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=86-124 {ECO:0000313|EMBL:KAI1520231.1};
RA   Moolhuijzen P.M., Moffat C.S.;
RL   Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAI1520231.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=86-124 {ECO:0000313|EMBL:KAI1520231.1};
RA   Moolhuijzen P., See P.T., Shi G., Powell H.R., Cockram J., Jorgensen L.N.,
RA   Benslimane H., Strelkov S.E., Turner J., Liu Z., Moffat C.S.;
RT   "A global pangenome for the wheat fungal pathogen Pyrenophora tritici-
RT   repentis and prediction of effector protein structural homology.";
RL   bioRxiv 0:0-0(2022).
CC   -!- FUNCTION: ATP-dependent DNA helicase important for chromosome
CC       transmission and normal cell cycle progression in G(2)/M (By
CC       similarity). May have a role in changing DNA topology to allow the
CC       loading of proteins involved in maintaining sister chromatid cohesion
CC       in the vicinity of the centromeres (By similarity). Has a specific role
CC       in chromosome segregation during meiosis II.
CC       {ECO:0000256|ARBA:ARBA00025396}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009146}.
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:KAF7576405.1}.
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DR   EMBL; NQIK02000001; KAF7576405.1; -; Genomic_DNA.
DR   EMBL; NRDI02000001; KAI1520231.1; -; Genomic_DNA.
DR   EMBL; NQIK01000002; PWO15637.1; -; Genomic_DNA.
DR   Proteomes; UP000245464; Unassembled WGS sequence.
DR   Proteomes; UP000249757; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR010643; HBB.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   InterPro; IPR001945; RAD3/XPD.
DR   NCBIfam; TIGR00604; rad3; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   PANTHER; PTHR11472:SF1; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPD; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF06777; HBB; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   PRINTS; PR00852; XRODRMPGMNTD.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KAF7576405.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          7..295
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
SQ   SEQUENCE   796 AA;  90660 MW;  A2256AFCCFA85D54 CRC64;
     MKFYIDNLPV LFPYPRVYPE QYAYMCDLKR TLDQGGHCVL EMPSGTGKTV SLLSLIVAYQ
     QHYPEKRKLI YCSRTMSEIE KALAELKALM KYRTTELGYE EDFRGLGLTS RKNLCLHPSV
     KREKSGTVVD ARCRSLTAGF VKEKKERGEP VELCVYHENL DLLEPHNLIP PGVWTFDGML
     KYGEQQKQCP YFTARRMMPH CNVIIYSYHY LLDPKIADRV SKELSKDCIV VFDEAHNIDN
     VCIESLSIDL TEDVLRKATK GVNNLDRKIT EMKSSDAEKL QNEYAKLVEG LRAADEARNE
     DAFMANPALP DDLLTEAVPG NIRRAEHFVA FLKRFIEYLK TRMKVLNVVA DTPPEFLKHL
     RDLTFIERKP LRFCAERLTS LVRTLELTNI EDYQPLQEVA TFATLVATYE TGFLLIIEPF
     ESATATVPNP VLHLTCLDAA IAIKPVFERF YSVIVTSGTM SPLDMYPRML NFNTVVQESF
     TMTLTRKSFL PMIVDRGNDQ NQVTSQFEHR NDLQVQRNFG NLLIEFCKLT PDGVVVFFPS
     YLYMESIISA WQGMEILDTV WKYKLILVET PDAQETALAL ETFRTACNNG RGAVLLCVAR
     GKVSEGIDFD HHYGRTVICM GVPYQYTESR ILKARLEFLR ETYRIKEADF LSFDAMRHAA
     QCLGRVIRGK DDYGIMVLAD KRFNKKQTQL PKWIQQGLDA KSTKLSIDQA VGAAKNFLKD
     MSIPWSRAEQ EGHSSWSLED LEAHQRKKVA QGISGTDNPA MRALEGRAEI EHVEVEEVDE
     FGGSAAVDAV MAEVDA
//
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