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
//