SSL1_YEAST
ID SSL1_YEAST Reviewed; 461 AA.
AC Q04673; D6VY07; E9P8Y6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 193.
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;
GN Name=SSL1; OrderedLocusNames=YLR005W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1340463; DOI=10.1101/gad.6.12b.2463;
RA Yoon H., Miller S.P., Pabich E.K., Donahue T.F.;
RT "SSL1, a suppressor of a HIS4 5'-UTR stem-loop mutation, is essential for
RT translation initiation and affects UV resistance in yeast.";
RL Genes Dev. 6:2463-2477(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 400-461.
RX PubMed=8183345; DOI=10.1038/369242a0;
RA Maeda T., Wurgler-Murphy S.M., Saito H.;
RT "A two-component system that regulates an osmosensing MAP kinase cascade in
RT yeast.";
RL Nature 369:242-245(1994).
RN [6]
RP FUNCTION.
RX PubMed=8269516; DOI=10.1016/0092-8674(93)90624-y;
RA Feaver W.J., Svejstrup J.Q., Bardwell L., Bardwell A.J., Buratowski S.,
RA Gulyas K.D., Donahue T.F., Friedberg E.C., Kornberg R.D.;
RT "Dual roles of a multiprotein complex from S. cerevisiae in transcription
RT and DNA repair.";
RL Cell 75:1379-1387(1993).
RN [7]
RP FUNCTION OF TFIIH IN RNA POLYMERASE II TRANSCRIPTION, AND IDENTIFICATION IN
RP THE TFIIH COMPLEX.
RX PubMed=7961739; DOI=10.1016/s0021-9258(18)46892-5;
RA Svejstrup J.Q., Feaver W.J., LaPointe J., Kornberg R.D.;
RT "RNA polymerase transcription factor IIH holoenzyme from yeast.";
RL J. Biol. Chem. 269:28044-28048(1994).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=7813015; DOI=10.1016/0092-8674(95)90447-6;
RA Svejstrup J.Q., Wang Z., Feaver W.J., Wu X., Bushnell D.A., Donahue T.F.,
RA Friedberg E.C., Kornberg R.D.;
RT "Different forms of TFIIH for transcription and DNA repair: holo-TFIIH and
RT a nucleotide excision repairosome.";
RL Cell 80:21-28(1995).
RN [9]
RP FUNCTION OF THE TFIIH CORE COMPLEX IN DNA REPAIR.
RX PubMed=8631896; DOI=10.1074/jbc.271.18.10821;
RA Sung P., Guzder S.N., Prakash L., Prakash S.;
RT "Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3
RT and Rad25, in the incision step of nucleotide excision repair.";
RL J. Biol. Chem. 271:10821-10826(1996).
RN [10]
RP IDENTIFICATION IN THE TFIIH CORE COMPLEX.
RX PubMed=14500720; DOI=10.1074/jbc.c300417200;
RA Takagi Y., Komori H., Chang W.-H., Hudmon A., Erdjument-Bromage H.,
RA Tempst P., Kornberg R.D.;
RT "Revised subunit structure of yeast transcription factor IIH (TFIIH) and
RT reconciliation with human TFIIH.";
RL J. Biol. Chem. 278:43897-43900(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 119-310.
RX PubMed=25681444; DOI=10.1074/jbc.m115.636514;
RA Kim J.S., Saint-Andre C., Lim H.S., Hwang C.S., Egly J.M., Cho Y.;
RT "Crystal structure of the Rad3/XPD regulatory domain of Ssl1/p44.";
RL J. Biol. Chem. 290:8321-8330(2015).
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:0000269|PubMed:7813015,
CC ECO:0000269|PubMed:7961739, ECO:0000269|PubMed:8269516,
CC ECO:0000269|PubMed:8631896}.
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in
CC NER. The core complex associates with the 3-subunit CTD-kinase module
CC TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit
CC holoenzyme (holo-TFIIH) active in transcription.
CC {ECO:0000269|PubMed:14500720, ECO:0000269|PubMed:7813015,
CC ECO:0000269|PubMed:7961739}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 2340 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GTF2H2 family. {ECO:0000305}.
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DR EMBL; Z17385; CAA78992.1; -; Genomic_DNA.
DR EMBL; Z73177; CAA97527.1; -; Genomic_DNA.
DR EMBL; AY692893; AAT92912.1; -; Genomic_DNA.
DR EMBL; L26523; AAA35101.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09323.1; -; Genomic_DNA.
DR PIR; A46394; A46394.
DR RefSeq; NP_013105.1; NM_001181892.1.
DR PDB; 4WFQ; X-ray; 2.40 A; A=119-310.
DR PDB; 5OQJ; EM; 4.70 A; 6=1-461.
DR PDB; 5OQM; EM; 5.80 A; 6=1-461.
DR PDB; 6GYM; EM; 6.70 A; 6=1-461.
DR PDB; 7K01; EM; 3.90 A; 6=1-461.
DR PDB; 7K04; EM; 9.25 A; 6=1-461.
DR PDB; 7M2U; EM; 8.20 A; 6=1-461.
DR PDB; 7O4I; EM; 3.20 A; 6=1-461.
DR PDB; 7O4J; EM; 2.90 A; 6=1-461.
DR PDB; 7O4K; EM; 3.60 A; 6=1-461.
DR PDB; 7O4L; EM; 3.40 A; 6=1-461.
DR PDB; 7O72; EM; 3.40 A; 6=1-461.
DR PDB; 7O73; EM; 3.40 A; 6=1-461.
DR PDB; 7O75; EM; 3.20 A; 6=1-461.
DR PDBsum; 4WFQ; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 7K01; -.
DR PDBsum; 7K04; -.
DR PDBsum; 7M2U; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O4K; -.
DR PDBsum; 7O4L; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; Q04673; -.
DR SMR; Q04673; -.
DR BioGRID; 31278; 475.
DR ComplexPortal; CPX-1659; General transcription factor complex TFIIH.
DR DIP; DIP-2435N; -.
DR IntAct; Q04673; 14.
DR MINT; Q04673; -.
DR STRING; 4932.YLR005W; -.
DR iPTMnet; Q04673; -.
DR MaxQB; Q04673; -.
DR PaxDb; Q04673; -.
DR PRIDE; Q04673; -.
DR EnsemblFungi; YLR005W_mRNA; YLR005W; YLR005W.
DR GeneID; 850691; -.
DR KEGG; sce:YLR005W; -.
DR SGD; S000003995; SSL1.
DR VEuPathDB; FungiDB:YLR005W; -.
DR eggNOG; KOG2807; Eukaryota.
DR GeneTree; ENSGT00490000043395; -.
DR HOGENOM; CLU_028556_2_0_1; -.
DR InParanoid; Q04673; -.
DR OMA; CMCHIEN; -.
DR BioCyc; YEAST:G3O-32166-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:Q04673; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q04673; protein.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IDA:SGD.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IDA:SGD.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:SGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:ComplexPortal.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
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 3D-structure; DNA damage; DNA repair; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..461
FT /note="General transcription and DNA repair factor IIH
FT subunit SSL1"
FT /id="PRO_0000046852"
FT DOMAIN 125..304
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 349..366
FT /note="C4-type"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 131
FT /note="D -> G (in Ref. 4; AAT92912)"
FT /evidence="ECO:0000305"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:7O75"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:7O75"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:4WFQ"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:4WFQ"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4WFQ"
FT HELIX 145..163
FT /evidence="ECO:0007829|PDB:4WFQ"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:4WFQ"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:4WFQ"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:4WFQ"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:4WFQ"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:7O4L"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:4WFQ"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:4WFQ"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:4WFQ"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:4WFQ"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:4WFQ"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:4WFQ"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:4WFQ"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:7O4I"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:7O4L"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:7O4L"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 378..382
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:7O4L"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 438..446
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 452..456
FT /evidence="ECO:0007829|PDB:7O4J"
SQ SEQUENCE 461 AA; 52290 MW; 57ADCB630B790B4F CRC64;
MAPVVISESE EDEDRVAITR RTKRQVHFDG EGDDRVDQQQ QQHSSSHRDR DKHVQRKKKK
RLSNRNLQGS NGGYAWEDEI KRSWDLVKVD DEGDMASLVA SIVEARKKRT AKKNITPYQR
GIIRSLILTL DCSEAMLEKD LRPNRHAMII QYAIDFVHEF FDQNPISQMG IIIMRNGLAQ
LVSQVSGNPQ DHIDALKSIR KQEPKGNPSL QNALEMARGL LLPVPAHCTR EVLIVFGSLS
TTDPGDIHQT IDSLVSEKIR VKVLGLSAQV AICKELCKAT NYGDESFYKI LLDETHLKEL
FNEAVTPLPV NKINKGFTLV KMGFPTRIFE DTPTFCSCHS KLVYGGYFCP NCHSKVCSLP
TVCPCCDLML ILSTHLARSY HHLMPLKTFA EVPTTEKFRS EDCFSCQSRF PILKNHKNGK
LLTSSRYRCE DCKQEFCVDC DVFIHEILHN CPGCESKPVI T
