ID A0A166BET0_9AGAM Unreviewed; 794 AA.
AC A0A166BET0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 37.
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=PENSPDRAFT_587603 {ECO:0000313|EMBL:KZV64933.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV64933.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV64933.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV64933.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR EMBL; KV424635; KZV64933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166BET0; -.
DR STRING; 1314672.A0A166BET0; -.
DR InParanoid; A0A166BET0; -.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000077086; 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; 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; 1.
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:KZV64933.1};
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:UP000077086}.
FT DOMAIN 7..293
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 757..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 90021 MW; 8B0B8025E50C13FE CRC64;
MKFFIDDLPV VFPYDRIYPE QYAYMCDLKR TLDATGHCVL EMPSGTGKTV SLLSLIVSYQ
QFFPTKRKLV YCSRTVPEIE KALAELKRLM DYRISLAETP EEREKEQNFT GLGLTSRKNL
CIHPEVSKEK KGKVVDARCR DLTCSSTMNR ARNEPGSIET CSFHDNLEGL EQQIPSGVWT
LAEVLQYGRD HGTCPYFTVR RMASPQLPFV DVVIYSFHYL LDPKVAEQVS KDMSKDSIVV
FDEAHNIDNV CIESLSIDLT RPMLDSAARS VTKLADTIEE IKKTDASKLQ DEYQKLVEGL
QDAANAEDSF ASNPILPEDL LQEAIPGNIR KAEHFIAFLK RFVEYLKTRM RVLHVVAETP
PSFLQHLKDI TYIERRPLRF CAERLQSLVK TLELSRIDEF SSLQKVANFA TLVSTYEKGF
LLILEPFETE NATVPNPIFH FVCLDPSIAI KPVFERFSSV VITSGTISPL DMYPKMLQFT
PRVQETYAMT LTRNAFLPLV ITRGSDQVAI SSRFEVRNDP AVVRNFGTIL VEYSKIVPDG
IVAFFPSYLY MESIVAAWND MGILNEVWKN KLIFVETPDA NETSIALENY RRACDNGRGA
VLLSVARGKV SEGIDFDHNY GRAVIMFGVP YQYTESRILK ARLEYLRDVH RIRESEFLSF
DAIRNAAQCV GRALRGKTDW GLMVFADKRF ARADKRAKLP RWINQYITET AANLSTDMAL
TLSKLFMRTI SQTQDVNQTG VSLWTLEDIE KAQVAQREAE AAAEREAAAA RAREDEDDYG
DGGITDGMLL DVPA
//
