TFS2_YEAST
ID TFS2_YEAST Reviewed; 309 AA.
AC P07273; D6VU96; P24535;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 4.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Transcription elongation factor S-II;
DE AltName: Full=DNA strand transfer protein alpha;
DE Short=STP-alpha;
DE AltName: Full=DNA strand transferase 1;
DE AltName: Full=Pyrimidine pathway regulatory protein 2;
GN Name=DST1; Synonyms=PPR2; OrderedLocusNames=YGL043W;
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], AND PROTEIN SEQUENCE OF 18-30.
RX PubMed=1850099; DOI=10.1128/mcb.11.5.2576-2582.1991;
RA Clark A.B., Dykstra C.C., Sugino A.;
RT "Isolation, DNA sequence, and regulation of a Saccharomyces cerevisiae gene
RT that encodes DNA strand transfer protein alpha.";
RL Mol. Cell. Biol. 11:2576-2582(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1618824; DOI=10.1016/s0021-9258(18)42194-1;
RA Nakanishi T., Nakano A., Sekimizu K., Natori S.;
RT "Purification, gene cloning, and gene disruption of the transcription
RT elongation factor S-II in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 267:13200-13204(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-309.
RX PubMed=6139279; DOI=10.1002/j.1460-2075.1983.tb01702.x;
RA Hubert J.-C., Guyonvarch A., Kammerer B., Exinger F., Liljelund P.,
RA Lacroute F.;
RT "Complete sequence of a eukaryotic regulatory gene.";
RL EMBO J. 2:2071-2073(1983).
RN [7]
RP SIMILARITY TO S-II.
RX PubMed=1971423; DOI=10.1038/345298a0;
RA Davies C.J., Trgovchich J., Hutchison C.A. III;
RT "Homologue of TFIIS in yeast.";
RL Nature 345:298-298(1990).
RN [8]
RP IDENTITY OF PPR2 AND DST1.
RX PubMed=1922360; DOI=10.1038/353509a0;
RA Kipling D., Kearsey S.E.;
RT "TFIIS and strand-transfer proteins.";
RL Nature 353:509-509(1991).
RN [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Necessary for efficient RNA polymerase II transcription
CC elongation past template-encoded arresting sites. The arresting sites
CC in DNA have the property of trapping a certain fraction of elongating
CC RNA polymerases that pass through, resulting in locked ternary
CC complexes. Cleavage of the nascent transcript by S-II allows the
CC resumption of elongation from the new 3'-terminus.
CC -!- FUNCTION: Can promote the transfer of one strand of a double-stranded
CC DNA molecule to a homologous single strand and thus may be involved in
CC recombination.
CC -!- INTERACTION:
CC P07273; P38915: SPT8; NbExp=2; IntAct=EBI-19168, EBI-17964;
CC P07273; P38931: SSN2; NbExp=2; IntAct=EBI-19168, EBI-18059;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: S-II binds to RNA-polymerase II in the absence of
CC transcription.
CC -!- MISCELLANEOUS: Present with 6260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TFS-II family. {ECO:0000305}.
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; M36724; AAA88734.1; -; Genomic_DNA.
DR EMBL; D12478; BAA02046.1; -; Genomic_DNA.
DR EMBL; M60770; AAA34580.1; -; Genomic_DNA.
DR EMBL; Z72565; CAA96744.1; -; Genomic_DNA.
DR EMBL; X00047; CAA24928.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08057.1; -; Genomic_DNA.
DR PIR; A42921; A42921.
DR RefSeq; NP_011472.1; NM_001180908.1.
DR PDB; 1ENW; NMR; -; A=131-240.
DR PDB; 1EO0; NMR; -; A=1-77.
DR PDB; 1PQV; X-ray; 3.80 A; S=1-309.
DR PDB; 1Y1V; X-ray; 3.80 A; S=131-309.
DR PDB; 1Y1Y; X-ray; 4.00 A; S=131-309.
DR PDB; 3GTM; X-ray; 3.80 A; S=147-309.
DR PDB; 3PO3; X-ray; 3.30 A; S=132-309.
DR PDB; 5FMF; EM; 6.00 A; 2=136-309.
DR PDBsum; 1ENW; -.
DR PDBsum; 1EO0; -.
DR PDBsum; 1PQV; -.
DR PDBsum; 1Y1V; -.
DR PDBsum; 1Y1Y; -.
DR PDBsum; 3GTM; -.
DR PDBsum; 3PO3; -.
DR PDBsum; 5FMF; -.
DR AlphaFoldDB; P07273; -.
DR BMRB; P07273; -.
DR SMR; P07273; -.
DR BioGRID; 33205; 591.
DR DIP; DIP-2307N; -.
DR IntAct; P07273; 7.
DR MINT; P07273; -.
DR STRING; 4932.YGL043W; -.
DR iPTMnet; P07273; -.
DR MaxQB; P07273; -.
DR PaxDb; P07273; -.
DR PRIDE; P07273; -.
DR EnsemblFungi; YGL043W_mRNA; YGL043W; YGL043W.
DR GeneID; 852839; -.
DR KEGG; sce:YGL043W; -.
DR SGD; S000003011; DST1.
DR VEuPathDB; FungiDB:YGL043W; -.
DR eggNOG; KOG1105; Eukaryota.
DR HOGENOM; CLU_037637_1_0_1; -.
DR InParanoid; P07273; -.
DR OMA; TTFCECT; -.
DR BioCyc; YEAST:G3O-30554-MON; -.
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-75955; RNA Polymerase II Transcription Elongation.
DR EvolutionaryTrace; P07273; -.
DR PRO; PR:P07273; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P07273; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IPI:SGD.
DR GO; GO:0001139; F:RNA polymerase II complex recruiting activity; IMP:SGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001193; P:maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0031564; P:transcription antitermination; IDA:SGD.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IMP:SGD.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR035100; TF_IIS-typ.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR036575; TFIIS_cen_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR006289; TFSII.
DR InterPro; IPR001222; Znf_TFIIS.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR PIRSF; PIRSF006704; TF_IIS; 1.
DR SMART; SM00510; TFS2M; 1.
DR SMART; SM00509; TFS2N; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR SUPFAM; SSF46942; SSF46942; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR TIGRFAMs; TIGR01385; TFSII; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..309
FT /note="Transcription elongation factor S-II"
FT /id="PRO_0000121443"
FT DOMAIN 5..79
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT DOMAIN 148..264
FT /note="TFIIS central"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT ZN_FING 267..307
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT REGION 78..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 35
FT /note="V -> F (in Ref. 1; AAA88734/AAA34580)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..77
FT /note="DAIN -> AQLI (in Ref. 1; AAA88734/AAA34580)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="S -> C (in Ref. 1; AAA88734/AAA34580)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="A -> P (in Ref. 1; AAA88734/AAA34580)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:1EO0"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1EO0"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1EO0"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1EO0"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:1EO0"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1EO0"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:1EO0"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:1ENW"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:3PO3"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3PO3"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:3PO3"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:3PO3"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:3PO3"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3PO3"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:3PO3"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:3PO3"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:3PO3"
FT HELIX 240..255
FT /evidence="ECO:0007829|PDB:3PO3"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:3PO3"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3PO3"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:3PO3"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:3PO3"
SQ SEQUENCE 309 AA; 34843 MW; D133938319C015FF CRC64;
MDSKEVLVHV KNLEKNKSND AAVLEILHVL DKEFVPTEKL LRETKVGVEV NKFKKSTNVE
ISKLVKKMIS SWKDAINKNK RSRQAQQHHQ DHAPGNAEDK TTVGESVNGV QQPASSQSDA
MKQDKYVSTK PRNSKNDGVD TAIYHHKLRD QVLKALYDVL AKESEHPPQS ILHTAKAIES
EMNKVNNCDT NEAAYKARYR IIYSNVISKN NPDLKHKIAN GDITPEFLAT CDAKDLAPAP
LKQKIEEIAK QNLYNAQGAT IERSVTDRFT CGKCKEKKVS YYQLQTRSAD EPLTTFCTCE
ACGNRWKFS
