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Database: UniProt
Entry: A0A2V1AYV9_9ASCO
LinkDB: A0A2V1AYV9_9ASCO
Original site: A0A2V1AYV9_9ASCO 
ID   A0A2V1AYV9_9ASCO        Unreviewed;       792 AA.
AC   A0A2V1AYV9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   08-NOV-2023, 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=CXQ85_002994 {ECO:0000313|EMBL:PVH23260.1};
OS   [Candida] haemuloni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH23260.1, ECO:0000313|Proteomes:UP000244309};
RN   [1] {ECO:0000313|EMBL:PVH23260.1, ECO:0000313|Proteomes:UP000244309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B11899 {ECO:0000313|EMBL:PVH23260.1,
RC   ECO:0000313|Proteomes:UP000244309};
RA   Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA   Litvintseva A.P.;
RT   "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT   Patient with Chronic Leg Ulcers in Israel.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
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:PVH23260.1}.
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DR   EMBL; PKFO01000010; PVH23260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1AYV9; -.
DR   STRING; 45357.A0A2V1AYV9; -.
DR   EnsemblFungi; CXQ85_002994-t46_1; CXQ85_002994-t46_1-p1; CXQ85_002994.
DR   VEuPathDB; FungiDB:CXQ85_002994; -.
DR   OrthoDB; 124793at2759; -.
DR   Proteomes; UP000244309; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PVH23260.1};
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:UP000244309}.
FT   DOMAIN          7..295
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          758..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..772
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   792 AA;  90831 MW;  9E4564E3E6A3ECB4 CRC64;
     MKFYIDDLPV LFPYPRIYPE QYAYMSDIKK TLDVGGNCIL EMPSGTGKTV SLLSLTVAYQ
     MHYPEHRKIV YCSRTMSEIE KALIELQKLM DFRSAQLGYV EDFRGLGLTS RKNLCLHPEV
     SQERKGAVVD EKCRRLTNGQ LKSKLESDGV SQEQMIQNPD QLGLCSYHEK LNDFDQHDLL
     PQGVFSFESL LEYCKKEGTC PYFTVRRMIS FCNVIIYSYH YLLDPKIAER VSKELSRDSI
     IIFDEAHNID NVCIESLSLY LTDDTMKRAS RGANKLADAV DDMKAQDSEK LQNEYEKLVE
     GLRQNEIARE EDLFMANPVL PKDLLDEAIP GNIRKAEHFI SFLKRFIEYL KTRMKVLHVI
     SETPVSFLQH LKELTFIDRK PLRFCSERLS LLVRTLELSD VEDLNALKDI ATFATLVSTY
     ETGFQLILEP FETEGATVPN PILHFTCLDA SIAIKPVFDR FSSVIITSGT ISPLDMYPKM
     MNFQTVIQES YTMTLARRSF LPMIVTKGSD QVSISSRFEI RNDPSVVRNY GSLLIEFSKI
     TPDGMVVFFP SYLYMESIIS MWQSMGVLDE VWKYKLILVE TPDAQETSLA LETYRKACSN
     GRGAVLLSVA RGKVSEGIDF DHHYGRTVLM IGIPFQYTES RILKARLEFM RDHFQIKEND
     FLSFDAMRHA AQCLGRVLRG KDDYGIMVLA DRRFARKKSQ LPKWIAQGLY DSDTNLSTDM
     ALANAKKFLR SLAQPTNPED AEGVSVWDLK QLEDHQKQQQ KKIDKRIEDD EAADDKGEDD
     FMDLDDADLE LL
//
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