TFH47_SCHPO
ID TFH47_SCHPO Reviewed; 421 AA.
AC O74995;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=General transcription and DNA repair factor IIH subunit ssl1;
DE Short=TFIIH subunit ssl1;
DE AltName: Full=RNA polymerase II transcription factor B subunit ssl1;
DE Short=TFB subunit ssl1;
DE AltName: Full=Suppressor of stem-loop protein 1 homolog;
DE Short=SSL1 homolog;
DE AltName: Full=TFIIH basal transcription factor complex p47 subunit;
GN Name=ssl1; Synonyms=tfh47; ORFNames=SPCC1682.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JY741;
RX PubMed=10077189;
RX DOI=10.1002/(sici)1097-0061(199902)15:3<255::aid-yea359>3.0.co;2-a;
RA Adachi N., Matsumoto M., Hasegawa S., Yamamoto T., Horikoshi M.;
RT "Analysis of TFIIH subunit through isolation of the gene from
RT Schizosaccharomyces pombe corresponding to that of Saccharomyces cerevisiae
RT SSL1, reveals the presence of conserved structural motifs.";
RL Yeast 15:255-262(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-421.
RA Kawamukai M.;
RT "S.pombe SSL1 homolog.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBUNIT.
RX PubMed=14534314; DOI=10.1074/jbc.m306750200;
RA Spaehr H., Khorosjutina O., Baraznenok V., Linder T., Samuelsen C.O.,
RA Hermand D., Maekelae T.P., Holmberg S., Gustafsson C.M.;
RT "Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent
RT transcription in vitro.";
RL J. Biol. Chem. 278:51301-51306(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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. In NER, TFIIH acts by opening DNA around the lesion to allow the
CC excision of the damaged oligonucleotide and its replacement by a new
CC DNA fragment. In transcription, TFIIH has an essential role in
CC transcription initiation. When the pre-initiation complex (PIC) has
CC been established, TFIIH is required for promoter opening and promoter
CC escape. Phosphorylation of the C-terminal tail (CTD) of the largest
CC subunit of RNA polymerase II by the kinase module TFIIK controls the
CC initiation of transcription. {ECO:0000250|UniProtKB:Q04673}.
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC XPB/ptr8, XPD/rad15, ssl1, tfb1, tfb2, tfb4 and tfb5, which is active
CC in NER. The core complex associates with the 3-subunit CTD-kinase
CC module TFIIK composed of mcs2/cyclin H, mcs6/cdk7 and pmh1/tfb3 to form
CC the 10-subunit holoenzyme (holo-TFIIH) active in transcription.
CC {ECO:0000269|PubMed:14534314}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GTF2H2 family. {ECO:0000305}.
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DR EMBL; AF017646; AAC29144.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20673.1; -; Genomic_DNA.
DR EMBL; AB016221; BAA31745.1; -; mRNA.
DR PIR; T43534; T43534.
DR RefSeq; NP_587800.1; NM_001022793.2.
DR AlphaFoldDB; O74995; -.
DR SMR; O74995; -.
DR BioGRID; 275765; 4.
DR IntAct; O74995; 1.
DR STRING; 4896.SPCC1682.07.1; -.
DR iPTMnet; O74995; -.
DR MaxQB; O74995; -.
DR PaxDb; O74995; -.
DR PRIDE; O74995; -.
DR EnsemblFungi; SPCC1682.07.1; SPCC1682.07.1:pep; SPCC1682.07.
DR GeneID; 2539194; -.
DR KEGG; spo:SPCC1682.07; -.
DR PomBase; SPCC1682.07; ssl1.
DR VEuPathDB; FungiDB:SPCC1682.07; -.
DR eggNOG; KOG2807; Eukaryota.
DR HOGENOM; CLU_028556_1_1_1; -.
DR InParanoid; O74995; -.
DR OMA; CMCHIEN; -.
DR PhylomeDB; O74995; -.
DR Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SPO-72086; mRNA Capping.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SPO-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SPO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SPO-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SPO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:O74995; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:PomBase.
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; IC:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 from RNA polymerase II promoter; IC:PomBase.
DR CDD; cd01453; vWA_transcription_factor_IIH_type; 1.
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; SSF53300; SSF53300; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR TIGRFAMs; TIGR00622; ssl1; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..421
FT /note="General transcription and DNA repair factor IIH
FT subunit ssl1"
FT /id="PRO_0000046856"
FT DOMAIN 88..267
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 311..328
FT /note="C4-type"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 421 AA; 47067 MW; 4EB838661170AE05 CRC64;
MNENQKSFDS DKSESEDEQK NGRVKVRSRK TDDNEGYTWE GEYQRSWDIV QEDAEGSLVG
VIAGLIQSGK RKRLLRDTTP LQRGIIRHMV LVLDLSNSME ERDFHHKRFD LQIKYASEFV
LEFFEQNPIS QLSIIGVMDG IAHRITDLHG NPQSHIQKLK SLRDCSGNFS LQNALEMARA
SLSHIASHGT REVLIIFGSI LSSDPGDIFK TIDALVHDSI RVRIVGLAAE VAICKEICNK
TNSSTKNAYG VVISEQHFRE LLLESTIPPA TDSAKTTDAS LVMMGFPSKV VEQLPSLCAC
HSIPSRGGFH CPRCKAKVCT LPIECPSCSL VLILSTHLAR SYHHLFPLKN WSEIPWSANP
KSTHCFACQL PFPKPPVSPF DESTSSMRYA CPSCKNHFCL DCDVFAHEQL HECYGCQCSG
N
