ID   D3ZEG9_RAT              Unreviewed;       760 AA.
AC   D3ZEG9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 110.
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   Name=Ercc2 {ECO:0000313|Ensembl:ENSRNOP00000024247.4,
GN   ECO:0000313|RGD:1309109};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000024247.4, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000024247.4, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000024247.4,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000024247.4}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000024247.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; NP_001166280.1; NM_001172809.1.
DR   AlphaFoldDB; D3ZEG9; -.
DR   SMR; D3ZEG9; -.
DR   STRING; 10116.ENSRNOP00000024247; -.
DR   PhosphoSitePlus; D3ZEG9; -.
DR   PaxDb; 10116-ENSRNOP00000024247; -.
DR   Ensembl; ENSRNOT00000024246.8; ENSRNOP00000024247.4; ENSRNOG00000017753.8.
DR   GeneID; 308415; -.
DR   KEGG; rno:308415; -.
DR   AGR; RGD:1309109; -.
DR   CTD; 2068; -.
DR   RGD; 1309109; Ercc2.
DR   eggNOG; KOG1131; Eukaryota.
DR   GeneTree; ENSGT00950000182970; -.
DR   HOGENOM; CLU_011312_1_0_1; -.
DR   OrthoDB; 124793at2759; -.
DR   TreeFam; TF101232; -.
DR   Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-RNO-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-RNO-5696400; Dual Incision in GG-NER.
DR   Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-RNO-6782135; Dual incision in TC-NER.
DR   Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-RNO-72086; mRNA Capping.
DR   Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-RNO-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-RNO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR   Reactome; R-RNO-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-RNO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-RNO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000017753; Expressed in testis and 19 other cell types or tissues.
DR   GO; GO:0070516; C:CAK-ERCC2 complex; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0071817; C:MMXD complex; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005819; C:spindle; ISO:RGD.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISO:RGD.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; IDA:RGD.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; ISO:RGD.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR   GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR   GO; GO:0032289; P:central nervous system myelin formation; ISO:RGD.
DR   GO; GO:0007059; P:chromosome segregation; ISO:RGD.
DR   GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR   GO; GO:0006281; P:DNA repair; ISO:RGD.
DR   GO; GO:0040016; P:embryonic cleavage; ISO:RGD.
DR   GO; GO:0048568; P:embryonic organ development; IEP:RGD.
DR   GO; GO:0043249; P:erythrocyte maturation; ISO:RGD.
DR   GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR   GO; GO:0035315; P:hair cell differentiation; ISO:RGD.
DR   GO; GO:0022405; P:hair cycle process; ISO:RGD.
DR   GO; GO:0048820; P:hair follicle maturation; ISO:RGD.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; ISO:RGD.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR   GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISO:RGD.
DR   GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISO:RGD.
DR   GO; GO:0045951; P:positive regulation of mitotic recombination; IBA:GO_Central.
DR   GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISO:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR   GO; GO:0009411; P:response to UV; ISO:RGD.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; ISO:RGD.
DR   GO; GO:0043588; P:skin development; ISO:RGD.
DR   GO; GO:0021510; P:spinal cord development; ISO:RGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006362; P:transcription elongation by RNA polymerase I; ISO:RGD.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISO:RGD.
DR   GO; GO:0009650; P:UV protection; ISO:RGD.
DR   CDD; cd17969; DEAHc_XPD; 1.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 1.10.275.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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   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};
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:UP000002494}.
SQ   SEQUENCE   760 AA;  86814 MW;  AC4316E1F21BCF67 CRC64;
     MKLNVDGLLV YFPYDYIYPE QFSYMLELKR TLDAKGHGVL EMPSGTGKTV SLLALIVAYQ
     RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LSFYEQQEGE KLPFLGLALS SRKNLCIHPE
     VTPLRFGKDV DGKCHSLTAS YVRAQYQQDA SLPHCRFYEE FDTHGRQVPL PAGIYNLDDL
     KALGQRQGWC PYFLARYSIL HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID
     NVCIDSMSVN LTRRTLDRCQ SNLDTLQKTV LRIKETDEQR LRDEYRRLVE GLREASAARE
     TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV QESPPAFLSG
     LAQRVCIQRK PLRFCAERLR SLLHTLEIAD LADFSPLTLL ANFATLVSTY AKGFTIIIEP
     FDDRTPTITN PILHFSCMDA SLAIKPVFER FQSVIITSGT LSPLDIYPKI LDFHPVTMAT
     FTMTLARVCL CPMIIGRGND QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT
     SYQYMESTVA SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA
     RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND FLTFDAMRHA
     AQCVGRAIRG KTDYGLMVFA DKRFARADKR GKLPRWIQEH LTDSNLNLTV DEGVQVAKYF
     LRQMAQPFHR EDQLGLSLLS LEQLQSEETL QRIEQIAQQL
//