TFS2_SCHPO
ID TFS2_SCHPO Reviewed; 293 AA.
AC P49373;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Transcription elongation factor S-II;
DE AltName: Full=TFIIS;
GN Name=tfs1; ORFNames=SPAC20H4.03c;
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].
RX PubMed=8904334;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<227::aid-yea905>3.0.co;2-9;
RA Williams L.A., Kane C.M.;
RT "Isolation and characterization of the Schizosaccharomyces pombe gene
RT encoding transcript elongation factor TFIIS.";
RL Yeast 12:227-236(1996).
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).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649,
CC ECO:0000255|PROSITE-ProRule:PRU00651}.
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; U20526; AAA74048.1; -; Genomic_DNA.
DR EMBL; CU329670; CAC19733.1; -; Genomic_DNA.
DR PIR; S63845; S63845.
DR RefSeq; NP_593623.1; NM_001019054.2.
DR AlphaFoldDB; P49373; -.
DR SMR; P49373; -.
DR BioGRID; 278428; 160.
DR STRING; 4896.SPAC20H4.03c.1; -.
DR iPTMnet; P49373; -.
DR MaxQB; P49373; -.
DR PaxDb; P49373; -.
DR PRIDE; P49373; -.
DR EnsemblFungi; SPAC20H4.03c.1; SPAC20H4.03c.1:pep; SPAC20H4.03c.
DR GeneID; 2541941; -.
DR KEGG; spo:SPAC20H4.03c; -.
DR PomBase; SPAC20H4.03c; tfs1.
DR VEuPathDB; FungiDB:SPAC20H4.03c; -.
DR eggNOG; KOG1105; Eukaryota.
DR HOGENOM; CLU_037637_1_1_1; -.
DR InParanoid; P49373; -.
DR OMA; TTFCECT; -.
DR PhylomeDB; P49373; -.
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-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:P49373; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0001139; F:RNA polymerase II complex recruiting activity; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003711; F:transcription elongation regulator activity; NAS:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0031564; P:transcription antitermination; IBA:GO_Central.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:PomBase.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
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 3: Inferred from homology;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..293
FT /note="Transcription elongation factor S-II"
FT /id="PRO_0000121442"
FT DOMAIN 4..81
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT DOMAIN 133..248
FT /note="TFIIS central"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT ZN_FING 251..291
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT REGION 81..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
SQ SEQUENCE 293 AA; 32734 MW; 73A1BF2838D97A9F CRC64;
MDSADIRSAK AALEKAIQGK NIETIINIMT RLKNEVVATE ELLKETRLGL VVGKLRSHPN
EKVGEQAREI VKKWKADVSK GRPLKTTTTT SSTPSKHADV GSQAQKQVQK QSSSGQRTFK
SDNVNVNVTD DKIRNNCIGL MYNALVIDSD ESSSLIIAKA KEIDAQVLAR AAGKTGSEYR
NRMRSLYMNL KDKNNPKLRA SVLRNEITPQ RLSTMTSAEL ASEDRRKEDA KLEQENLFHA
QGAKPQKAVT DLFTCGKCKQ KKVSYYQMQT RSADEPMTTF CECTVCGNRW KFS
