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Database: UniProt
Entry: A0A2J7PH41_9NEOP
LinkDB: A0A2J7PH41_9NEOP
Original site: A0A2J7PH41_9NEOP 
ID   A0A2J7PH41_9NEOP        Unreviewed;       720 AA.
AC   A0A2J7PH41;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=B7P43_G15603 {ECO:0000313|EMBL:PNF15638.1};
OS   Cryptotermes secundus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX   NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF15638.1, ECO:0000313|Proteomes:UP000235965};
RN   [1] {ECO:0000313|EMBL:PNF15638.1, ECO:0000313|Proteomes:UP000235965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole body {ECO:0000313|EMBL:PNF15638.1};
RA   Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA   Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA   Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA   Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA   Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA   Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA   Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA   Bornberg-Bauer E.;
RT   "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
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:PNF15638.1}.
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DR   EMBL; NEVH01025150; PNF15638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J7PH41; -.
DR   Proteomes; UP000235965; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PNF15638.1};
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:UP000235965};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..720
FT                   /note="General transcription and DNA repair factor IIH
FT                   helicase subunit XPD"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014342351"
FT   DOMAIN          1..242
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   COILED          215..257
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   720 AA;  82180 MW;  15B3CD5DB8031CCD CRC64;
     MPSGTGKTVS LLSLIVAYMI ANPLSVTKLI YCSRTVPEIE KVLEELKKLM TYYEKERGQA
     PKMVGLVLSS RKNMCIHPQV SKERDGKIVD GRCHSLTASY VRERHNYDDS IPICSFYEGF
     DIEGREVQLE PGVYSLDDLK EYGQERNWCP YFLARYTILH ANIVVYSYHY LLDPKIADVV
     SKELSRSSVV VFDEAHNIDN VCIDSMSVKI NRRIIDRSTA NIQLLEQTVN EMKEDDAKKL
     KEEYQRLVEG LRDASVARET DVVLSNPVLP DEVLKEAVPG SIRTAEHFVG FLKRFVEYLK
     TRLRVQHVVL ESPASFLKDV YQKVCIERKP LRFCHERLAS LLRTLEIADL TDFSPLILIT
     HLATLVSTYT KGFTIIVEPF DDKTPTVSNP ILHFSCLDSS IAIKPVFDRF QTVVITSGTL
     SPLDMYPKIL DFHPVIMSSF TMTLARPCLL PMIVSKGNDQ VAISSRFETR EDVAVVRNYG
     QLLVEIATIV PDGVVCFFTS YLYLESVVAS WYDQGVVDSL QRNKLLFIET QDAAETSLAL
     LNYIRACESG RGAVLLSVAR GKVSEGVDFD HHLGRAVLMF GIPYVYTQSR ILRARLEYLR
     DQFQIRENDF LTFDAMRHAA QCVGRAIRGK TDYGIMIFAD KRFSRADKRN KLPKWIQEHL
     KDSLCNLSTE EAVQISKRWL RQMAQPFSRE DQLGVSLLTL EQLHSEEMQR KQQNTADQKL
//
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