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SRB11_SCHPO
ID   SRB11_SCHPO             Reviewed;         228 AA.
AC   O94503;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=RNA polymerase II holoenzyme cyclin-like subunit;
DE   AltName: Full=Suppressor of RNA polymerase B srb11;
GN   Name=srb11; ORFNames=SPBC12D12.06;
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 [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   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 5-228.
RX   PubMed=15979093; DOI=10.1016/j.jmb.2005.05.041;
RA   Hoeppner S., Baumli S., Cramer P.;
RT   "Structure of the mediator subunit cyclin C and its implications for CDK8
RT   function.";
RL   J. Mol. Biol. 350:833-842(2005).
CC   -!- FUNCTION: Component of the Cdk8 module/Srb8-11 module which is a
CC       regulatory module of the Mediator complex that regulates basal RNA
CC       polymerase II transcription. The Cdk8 module may sterically hinder the
CC       interaction between Mediator and RNA polymerase II leading to
CC       transcriptional repression of a subset of genes regulated by Mediator.
CC   -!- SUBUNIT: Component of the Cdk8 module of the Mediator complex. The Cdk8
CC       module is composed of srb8, srb9, srb10 and srb11.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA22680.1; -; Genomic_DNA.
DR   PIR; T39386; T39386.
DR   RefSeq; NP_595953.1; NM_001021862.2.
DR   PDB; 1ZP2; X-ray; 3.00 A; A=5-228.
DR   PDBsum; 1ZP2; -.
DR   AlphaFoldDB; O94503; -.
DR   SMR; O94503; -.
DR   BioGRID; 276206; 176.
DR   STRING; 4896.SPBC12D12.06.1; -.
DR   PaxDb; O94503; -.
DR   EnsemblFungi; SPBC12D12.06.1; SPBC12D12.06.1:pep; SPBC12D12.06.
DR   GeneID; 2539651; -.
DR   KEGG; spo:SPBC12D12.06; -.
DR   PomBase; SPBC12D12.06; srb11.
DR   VEuPathDB; FungiDB:SPBC12D12.06; -.
DR   eggNOG; KOG0794; Eukaryota.
DR   HOGENOM; CLU_1215393_0_0_1; -.
DR   InParanoid; O94503; -.
DR   OMA; HIRTICN; -.
DR   PhylomeDB; O94503; -.
DR   EvolutionaryTrace; O94503; -.
DR   PRO; PR:O94503; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0016592; C:mediator complex; IPI:PomBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IC:PomBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00043; CYCLIN; 1.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR043198; Cyclin/Ssn8.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR028367; CyclinC/Ssn8.
DR   PANTHER; PTHR10026; PTHR10026; 1.
DR   PANTHER; PTHR10026:SF7; PTHR10026:SF7; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; SSF47954; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cyclin; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..228
FT                   /note="RNA polymerase II holoenzyme cyclin-like subunit"
FT                   /id="PRO_0000080427"
FT   DOMAIN          10..134
FT                   /note="Cyclin N-terminal"
FT   HELIX           9..11
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           30..45
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           50..66
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           75..89
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           96..104
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           115..128
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   TURN            129..131
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           139..147
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           153..166
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   TURN            167..170
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           177..189
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           195..202
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   HELIX           205..222
FT                   /evidence="ECO:0007829|PDB:1ZP2"
FT   STRAND          224..226
FT                   /evidence="ECO:0007829|PDB:1ZP2"
SQ   SEQUENCE   228 AA;  26176 MW;  53DACF4A8A12FDC6 CRC64;
     MAANYWASSQ LTQLFLSTDL ESLEPTCLSK DTIYQWKVVQ TFGDRLRLRQ RVLATAIVLL
     RRYMLKKNEE KGFSLEALVA TCIYLSCKVE ECPVHIRTIC NEANDLWSLK VKLSRSNISE
     IEFEIISVLD AFLIVHHPYT SLEQAFHDGI INQKQLEFAW SIVNDSYASS LCLMAHPHQL
     AYAALLISCC NDENTIPKLL DLIKSTDAFK VILCVQRIIS IYYFEDIE
 
 
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