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Database: UniProt
Entry: B6JWI3_SCHJY
LinkDB: B6JWI3_SCHJY
Original site: B6JWI3_SCHJY 
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
//
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