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 27-MAR-2024, entry version 225. 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 PDB; 7FAW; X-ray; 2.44 A; A/B/C=1-73. DR PDB; 7UI9; EM; 3.30 A; S=1-309. DR PDB; 7UIF; EM; 4.60 A; S=1-309. DR PDB; 7UIO; EM; 3.30 A; AS/BS=1-309. 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 PDBsum; 7FAW; -. DR PDBsum; 7UI9; -. DR PDBsum; 7UIF; -. DR PDBsum; 7UIO; -. DR AlphaFoldDB; P07273; -. DR BMRB; P07273; -. DR EMDB; EMD-26542; -. DR EMDB; EMD-26544; -. DR EMDB; EMD-26551; -. DR SMR; P07273; -. DR BioGRID; 33205; 601. DR DIP; DIP-2307N; -. DR IntAct; P07273; 7. DR MINT; P07273; -. DR STRING; 4932.YGL043W; -. DR iPTMnet; P07273; -. DR MaxQB; P07273; -. DR PaxDb; 4932-YGL043W; -. DR PeptideAtlas; P07273; -. DR EnsemblFungi; YGL043W_mRNA; YGL043W; YGL043W. DR GeneID; 852839; -. DR KEGG; sce:YGL043W; -. DR AGR; SGD:S000003011; -. DR SGD; S000003011; DST1. DR VEuPathDB; FungiDB:YGL043W; -. DR eggNOG; KOG1105; Eukaryota. DR HOGENOM; CLU_037637_1_0_1; -. DR InParanoid; P07273; -. DR OMA; RFVVMTH; -. DR OrthoDB; 1383197at2759; -. DR BioCyc; YEAST:G3O-30554-MONOMER; -. 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 BioGRID-ORCS; 852839; 0 hits in 10 CRISPR screens. 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:0006351; P:DNA-templated transcription; IBA:GO_Central. DR GO; GO:0001193; P:maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II; 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 by RNA polymerase II; 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 by RNA polymerase I; IDA:SGD. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:SGD. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:SGD. DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IMP:SGD. DR CDD; cd00183; TFIIS_I; 1. DR CDD; cd13749; Zn-ribbon_TFIIS; 1. DR Gene3D; 2.20.25.10; -; 1. DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1. DR Gene3D; 1.10.472.30; Transcription elongation factor S-II, central domain; 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 NCBIfam; TIGR01385; TFSII; 1. DR PANTHER; PTHR11477:SF0; IP08861P-RELATED; 1. DR PANTHER; PTHR11477; TRANSCRIPTION FACTOR S-II ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1. 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; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1. DR SUPFAM; SSF46942; Elongation factor TFIIS domain 2; 1. DR SUPFAM; SSF57783; Zinc beta-ribbon; 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..15 FT /evidence="ECO:0007829|PDB:7FAW" FT TURN 16..18 FT /evidence="ECO:0007829|PDB:7FAW" FT HELIX 20..33 FT /evidence="ECO:0007829|PDB:7FAW" FT HELIX 38..44 FT /evidence="ECO:0007829|PDB:7FAW" FT HELIX 46..51 FT /evidence="ECO:0007829|PDB:7FAW" FT HELIX 52..55 FT /evidence="ECO:0007829|PDB:7FAW" FT HELIX 59..73 FT /evidence="ECO:0007829|PDB:7FAW" 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 //