ID B6JWI3_SCHJY Unreviewed; 422 AA.
AC B6JWI3;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=General transcription and DNA repair factor IIH {ECO:0000256|PIRNR:PIRNR015919};
GN Name=ssl1 {ECO:0000313|JaponicusDB:SJAG_00758};
GN ORFNames=SJAG_00758 {ECO:0000313|EMBL:EEB05734.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB05734.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB05734.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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}.
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DR EMBL; KE651166; EEB05734.1; -; Genomic_DNA.
DR RefSeq; XP_002172027.1; XM_002171991.1.
DR AlphaFoldDB; B6JWI3; -.
DR STRING; 402676.B6JWI3; -.
DR EnsemblFungi; EEB05734; EEB05734; SJAG_00758.
DR GeneID; 7052175; -.
DR JaponicusDB; SJAG_00758; ssl1.
DR VEuPathDB; FungiDB:SJAG_00758; -.
DR eggNOG; KOG2807; Eukaryota.
DR HOGENOM; CLU_028556_2_0_1; -.
DR OMA; INWVEVP; -.
DR OrthoDB; 276422at2759; -.
DR Proteomes; UP000001744; 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; IBA:GO_Central.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:EnsemblFungi.
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; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:EnsemblFungi.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd01453; vWA_transcription_factor_IIH_type; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 NCBIfam; TIGR00622; ssl1; 1.
DR PANTHER; PTHR12695; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2; 1.
DR PANTHER; PTHR12695:SF2; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2-RELATED; 1.
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 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|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR015919};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR015919};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR015919};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR015919};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR015919};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 89..267
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 390..412
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT ZN_FING 312..329
FT /note="C4-type"
FT /evidence="ECO:0000256|PIRSR:PIRSR015919-1"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 47041 MW; EE107194C7106BC1 CRC64;
MSTLTKDYDD SDNSDQDGDE RVSKNGSKQT KSQHKEGYTW EGEYQRSWDI VKEDAEGSLA
GVVEGLINAG KRKRILRDTT PLQRGIIRHL ILVVDLSIAM EERDFRTKRV DLQIKYGTEF
IINYFEQNPI SQLGIIAMKD GIAVKISDIH GNPQDHINKL KKLRECKGMA SLQNALEMAR
ASLAHIASHG TREVLIIFGS LLSSDPGDIF QTIDSLVKEN ISVHIIGLSA EVSVCKEICR
RTNNGAQNAY GVILNENHLE ELLMEKTIPP ATHSDEGIPA SLVKMGFPSK VIEPFPSLCS
CHSVASRGGF HCPRCKCKVC TLPIECPGCS LILILSTHLA RSYHHLFPLK NWREIPWSEK
PTSTYCFACQ APFPMTPQAK EDQNASSSRY ACPSCGHHFC IECDVFAHEQ LHECFGCQSH
TS
//