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Database: UniProt
Entry: A0A3F3QHB8_9EURO
LinkDB: A0A3F3QHB8_9EURO
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ID   A0A3F3QHB8_9EURO        Unreviewed;       801 AA.
AC   A0A3F3QHB8;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=BDQ94DRAFT_44591 {ECO:0000313|EMBL:RDH38495.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH38495.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH38495.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH38495.1,
RC   ECO:0000313|Proteomes:UP000253729};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KZ852033; RDH38495.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3QHB8; -.
DR   SMR; A0A3F3QHB8; -.
DR   STRING; 1341132.A0A3F3QHB8; -.
DR   OrthoDB; 124793at2759; -.
DR   Proteomes; UP000253729; 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 1.10.275.40; -; 1.
DR   Gene3D; 1.10.30.20; Bacterial XPD DNA helicase, FeS cluster domain; 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   InterPro; IPR042493; XPD_DNA_FeS.
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; 2.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT   DOMAIN          7..283
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          772..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          248..297
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   801 AA;  91265 MW;  413D857C73423D15 CRC64;
     MKFFIDDLPV LFPYPRIYPE QYAYMCDLKK TLDAGGHCVL EMPSGTGKTV SLLSLIVAYQ
     QHYPEHRKLI YCSRTMSEIE KALAELKALM KFRAKELGYT EDFRALGLTS RKNLCLHPSV
     KREKSGAVVD ARCRSLTAGF VKEKKERGED VELCVYHENL DLLEPHNLVP PGVFTLDGLL
     KYGEEHKQCP YFSARRMMPF CNVIIYSYHY LLDPKIAERV SRELSKDCIV VFDEAHNIDN
     VCIESLSIDL TEDSLRKATR GANNLERKIN EMKTSDAEKL QNEYSKLVEG LQAAEQAREE
     DQFISNPVLP DDLLKEAVPG NIRRAEHFVS FLKRFIEYLK TRMKVMHTIS ETPPSFLTHV
     KDLTYIERKP LRFCAERLTS LVRTLELINI EDYQPLQEVA TFATLVATYE KGFLLILEPF
     ESEAATVPNP VLHFTCLDAA IAIKPVFERF SSVIITSGTL SPLEMYPKML GFNAVMQESY
     SMTLARRSFL PMIVTRGSDQ AQISSSFQIR NDPGVVRNYG NLVLEFSRIT PDGVVVFFPS
     YLYMESIISM WQGMGILDSI WNYKLILVET PDAQESSLAL ETYRTACCNG RGALLLCVAR
     GKVSEGIDFD HHYGRAVINI GVPFQYTESR ILKARLEFLR ENYRIRENDF LSFDAMRHAA
     QCLGRVLRGK DDYGVMVLAD RRFQKKRNQL PKWINQAMLE SETNLSTDMA AATAKNFLRT
     MAQPFKARDQ EGISTWSLAD IERHREKQKL EEERALREVP PNLAYGAAAA APHNGVRNGA
     GGADEFEDEI DNEDLMMLDA Q
//
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