ID C5M5W0_CANTT Unreviewed; 505 AA. AC C5M5W0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 14-DEC-2022, entry version 68. DE RecName: Full=General transcription and DNA repair factor IIH {ECO:0000256|PIRNR:PIRNR015919}; GN ORFNames=CTRG_01241 {ECO:0000313|EMBL:EER34380.1}; OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER34380.1, ECO:0000313|Proteomes:UP000002037}; RN [1] {ECO:0000313|EMBL:EER34380.1, ECO:0000313|Proteomes:UP000002037} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037}; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S., RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C., RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M., RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R., RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M., RA Cuomo C.A.; RT "Evolution of pathogenicity and sexual reproduction in eight Candida RT genomes."; RL Nature 459:657-662(2009). CC -!- FUNCTION: Component of the general transcription and DNA repair factor CC IIH (TFIIH) core complex, which is involved in general and CC transcription-coupled nucleotide excision repair (NER) of damaged DNA CC and, when complexed to TFIIK, in RNA transcription by RNA polymerase CC II. {ECO:0000256|PIRNR:PIRNR015919}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|PIRNR:PIRNR015919}. CC -!- SIMILARITY: Belongs to the GTF2H2 family. CC {ECO:0000256|ARBA:ARBA00006092, ECO:0000256|PIRNR:PIRNR015919}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG692396; EER34380.1; -; Genomic_DNA. DR RefSeq; XP_002546935.1; XM_002546889.1. DR AlphaFoldDB; C5M5W0; -. DR STRING; 5482.XP_002546935.1; -. DR EnsemblFungi; CTRG_01241-t43_1; CTRG_01241-t43_1-p1; CTRG_01241. DR GeneID; 8297513; -. DR KEGG; ctp:CTRG_01241; -. DR VEuPathDB; FungiDB:CTRG_01241; -. DR eggNOG; KOG2807; Eukaryota. DR HOGENOM; CLU_028556_2_0_1; -. DR OrthoDB; 768809at2759; -. DR Proteomes; UP000002037; Unassembled WGS sequence. DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IEA:EnsemblFungi. DR GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:UniProtKB-UniRule. DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IEA:UniProtKB-UniRule. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblFungi. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule. DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IEA:EnsemblFungi. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:EnsemblFungi. DR Gene3D; 3.30.40.10; -; 1. DR Gene3D; 3.40.50.410; -; 1. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR007198; Ssl1-like. DR InterPro; IPR004595; TFIIH_C1-like_dom. DR InterPro; IPR012170; TFIIH_SSL1/p44. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF07975; C1_4; 1. DR Pfam; PF04056; Ssl1; 1. DR PIRSF; PIRSF015919; TFIIH_SSL1; 1. DR SMART; SM01047; C1_4; 1. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR TIGRFAMs; TIGR00622; ssl1; 1. DR PROSITE; PS50234; VWFA; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 3: Inferred from homology; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR015919}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR015919}; KW Reference proteome {ECO:0000313|Proteomes:UP000002037}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, KW ECO:0000256|PIRNR:PIRNR015919}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, KW ECO:0000256|PIRNR:PIRNR015919}; Zinc {ECO:0000256|PIRNR:PIRNR015919}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00042}. FT DOMAIN 109..304 FT /note="VWFA" FT /evidence="ECO:0000259|PROSITE:PS50234" FT DOMAIN 475..498 FT /note="C2H2-type" FT /evidence="ECO:0000259|PROSITE:PS50157" FT ZN_FING 393..410 FT /note="C4-type" FT /evidence="ECO:0000256|PIRSR:PIRSR015919-1" FT REGION 1..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 24..47 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 505 AA; 56250 MW; 866C66D86232A515 CRC64; MDDSDEEYVR TNSPSSKLSS EVPEAKASPR DKNGVSTRTR SSRRGEVSDL KGANGYAWED EYQRSWDIVK DDESGSNSFE AMVQSIIENR KKKIMKNPST PFQRGIIRTL VIIIDGSSVM SEKDLRPNRL SMTLSYLQDF VTEFFDQNPI SRLGIILMRN GIANLVSEVS GSPQYHIDKI RQLKARQHNR FEPKGDPSLQ NSLEMARSLL KFNFGSTSNN TKNSKEVLII FGALFTSDPG DIHRTIDNLI KDEIKVSVIG LSAQVAICQE LVNRTNKEPR NSQSKHYGVI MNESHFKELL MDSVTPLPLT ESEKRLQDAQ SEDGGVPVLR MGFPSKVQPT LTSVVTGTDM IIEFPHLNAS FPTQGSEDSK DAVEIQNNRA VAAASSSVIG YQCPQCKSKV CNLPTLCPVC GLMLILSTHL ARSYHHLVPL AQFKEVPVAP VYDSEFCFGC QLKFPDGVKA GTQKGSLESM TSSRYRCKRC EKSFCINCDV FVHEVLHTCP GCENM //