ID I3EG22_NEMP3 Unreviewed; 730 AA.
AC I3EG22;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=NEQG_01613 {ECO:0000313|EMBL:EIJ88169.1};
OS Nematocida parisii (strain ERTm3) (Nematode killer fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nematocida.
OX NCBI_TaxID=935791 {ECO:0000313|EMBL:EIJ88169.1, ECO:0000313|Proteomes:UP000002872};
RN [1] {ECO:0000313|EMBL:EIJ88169.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ERTm3 {ECO:0000313|EMBL:EIJ88169.1};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C., Troemel E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Nematocida parisii strain ERTm3.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; GL870879; EIJ88169.1; -; Genomic_DNA.
DR AlphaFoldDB; I3EG22; -.
DR STRING; 935791.I3EG22; -.
DR EnsemblFungi; EIJ88169; EIJ88169; NEQG_01613.
DR VEuPathDB; MicrosporidiaDB:NEQG_01613; -.
DR HOGENOM; CLU_011312_1_0_1; -.
DR InParanoid; I3EG22; -.
DR OMA; IREQFFR; -.
DR Proteomes; UP000002872; 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:InterPro.
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; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
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 Pfam; PF04851; ResIII; 1.
DR PRINTS; PR00852; XRODRMPGMNTD.
DR SMART; SM00487; DEXDc; 1.
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 Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EIJ88169.1};
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:UP000002872}.
FT DOMAIN 7..291
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 730 AA; 82774 MW; 904C8E160A62A346 CRC64;
MIIKMGNIEV FFPKNKIYPE QMQYIKELHE VVQAKGHCLI EMPTGTGKTI VLLSFLVSYQ
IHLMTKEEGY ERIQKNGFKR KEGIFKIVYC TRTTAEIEKV LEELKELYEY IKTYIPDIEY
TGLGLAARRT LCLNPDINAV SSLVNRRCRQ EKEECSFYKE YLKTAEGMPS GVYTLDDLKE
IGNKKGTCAY YTARSSIFLA DCIVYTYNYM IDPRINDLVS SGLGSNCVVV FDEAHNIDSV
CVEVLTVHIN RACLDKAWKS LSDISEYSVS KSLSLNNRNK EKTAYNKGKG IRSDFSSLLE
GHKSSRKFTS LVPGTLRSIN GFISAAKRII EFFKTKLKNV NLTTETTDVF IKNLENTVYV
DFSSIVHLSR RLREIMGELE MHGFIEDYSE LSRVCDFCSL CGQFKKGFSV VFEPFNSYSV
YEPVLHLSCL DSSIAMKHVF SGYNNVIITS GTLSPISIYP RLLDFTPIKS VEIDVSSKRG
LHALIVTKGS DQMTLAMDGS NALSSTFSLR AEPAVVRNYG NLLLEMSMSV PDGLVCFFPS
YKYMEEAVAA WTESGIIKKI MECKLIFVES FEHAETERAL DGYKRACETG RGGLMLSVAR
GKVSEGVDFS GCYGRAVLVF GVPFQYTESP RLKKRLEFLA EEFGIRESEF LSFDAMRQTA
QCVGRVLRTS TDYGLAVLAD RRFNVPEKKT QLPRWIQRHL EETSVNLSID MSITQARQFF
RRAPSAKYYN
//
