ID B6QC92_TALMQ Unreviewed; 794 AA.
AC B6QC92;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=PMAA_066900 {ECO:0000313|EMBL:EEA25586.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA25586.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995900; EEA25586.1; -; Genomic_DNA.
DR RefSeq; XP_002146133.1; XM_002146097.1.
DR AlphaFoldDB; B6QC92; -.
DR STRING; 441960.B6QC92; -.
DR VEuPathDB; FungiDB:PMAA_066900; -.
DR HOGENOM; CLU_011312_1_0_1; -.
DR OrthoDB; 124793at2759; -.
DR PhylomeDB; B6QC92; -.
DR Proteomes; UP000001294; 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; 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 Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EEA25586.1};
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:UP000001294}.
FT DOMAIN 7..283
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 752..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 248..297
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 752..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 90595 MW; E4354E8B35374CE7 CRC64;
MRFKIDELEV LFPYPKIYPE QWQYMCDLKK ALDASGHCVL EMPSGTGKTV TLLSLIVAYQ
QHHGDSRKLI YCSRTMSEID KALHELKALM KYRASQLGYT EDFRGLGLSS RKNLCLHPSV
KREKSGAVVD ARCRSLTASF VVQKKERGED VETCTYHDNL DLLEPHNLIE PGVFTFGDLL
RYCQEKVTCP YFTVRRMLPY CNVIIYSYHY LLDPKIAERV SRELSKDCIV VFDEAHNIDN
VAIESLSIDL TEDSLRKASR GAKNLERKIE EMKSSDAEKL QSEYTKLVEG LKATEEARDE
DLIMSNPVLP QDLLSEAVPG NIRRAEHFIA FLQRFIQYLM TRMKVTHTIS ETTPSFLQHL
RELVFIEAKP LRFCSERLTS LVRTLELMNI EDYQPLQEVA MFATLVSTYD RGFLLILEPF
ESEAATVPNP VLHLACLDAA IAFRPVVERF SSIVVTSGTL TPLDMFPKML NFTPVLQESY
TMTLARRSFL PMIVTRGSDQ SQISSSFQTR NDPSNLRNFG SLLLDFAKIV PDGIVVFFPS
YLYMESTLHV WSGMGILDMI WNYKLILVET PDAQESSLAL ETYRTACCNG RGAILMSVAR
GKVAEGVDFD HQYGRAVICI GVPFQYTESR ILRARLEFLR ENYGIRENDF LSFDAMRHAS
QCLGRVIRGK DDYGIMVLAD KRFARKRSQL PKWISQNILE SEVNLSTDMA VATAKNFLRT
MAQPFRAKDH EGISSWTPAQ LEEQIVKRKM EEERVERGEE PVAARQRDGG NRAVGAQADE
FDDDIDDEMM MLDA
//
