RTF1_SCHPO
ID RTF1_SCHPO Reviewed; 560 AA.
AC O94667;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=RNA polymerase-associated protein C651.09c;
DE AltName: Full=Protein RTF1 homolog;
GN ORFNames=SPBC651.09c;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-502 AND SER-506, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: The PAF1 complex is a multifunctional complex. Involved in
CC transcription initiation via genetic interactions with TATA-binding
CC proteins. Involved in elongation. Also has a role in transcription-
CC coupled histone modification. Important for TATA site selection by TBP.
CC Directly or indirectly regulates the DNA-binding properties of the TATA
CC box-binding protein, and the relative activities of different TATA
CC elements (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the PAF1 complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAB37605.1; -; Genomic_DNA.
DR PIR; T40608; T40608.
DR RefSeq; NP_595507.1; NM_001021417.2.
DR AlphaFoldDB; O94667; -.
DR SMR; O94667; -.
DR BioGRID; 277638; 13.
DR STRING; 4896.SPBC651.09c.1; -.
DR iPTMnet; O94667; -.
DR MaxQB; O94667; -.
DR PaxDb; O94667; -.
DR PRIDE; O94667; -.
DR EnsemblFungi; SPBC651.09c.1; SPBC651.09c.1:pep; SPBC651.09c.
DR GeneID; 2541123; -.
DR KEGG; spo:SPBC651.09c; -.
DR PomBase; SPBC651.09c; -.
DR VEuPathDB; FungiDB:SPBC651.09c; -.
DR eggNOG; KOG2402; Eukaryota.
DR HOGENOM; CLU_036626_0_0_1; -.
DR InParanoid; O94667; -.
DR OMA; SGCKSAV; -.
DR PhylomeDB; O94667; -.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:O94667; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000405; F:bubble DNA binding; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IPI:PomBase.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISO:PomBase.
DR Gene3D; 3.90.70.200; -; 1.
DR InterPro; IPR004343; Plus-3_dom.
DR InterPro; IPR036128; Plus3-like_sf.
DR Pfam; PF03126; Plus-3; 1.
DR SMART; SM00719; Plus3; 1.
DR SUPFAM; SSF159042; SSF159042; 1.
DR PROSITE; PS51360; PLUS3; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..560
FT /note="RNA polymerase-associated protein C651.09c"
FT /id="PRO_0000315631"
FT DOMAIN 214..345
FT /note="Plus3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00693"
FT REGION 15..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 387..456
FT /evidence="ECO:0000255"
FT COMPBIAS 18..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 560 AA; 63680 MW; 7AC07BB88504D7AD CRC64;
MADFQDELLA LAGIDDSDVA SNRKRAHDDL DDVLSSSSDE DNNENVGQDY AEESGGEGNE
KSEDEFEEKF KNPYRLEGKF KDEADRAKIM AMTEIERESI LFEREEEISK LMERRELAIR
LHQQNAQYMA QSTRRSTRDK PLTSAAAGKR DKLTELKKRR QERSARSVSE RTRKRSPVSD
YEEQNESEKS EEEEGYSPSY AEEKVEQVSK DNASANLYDL NAIRLGRKHV AEYMYHPIFE
STVTGCFVRV KIGERDGQGV YRLCQVKGIL ESRKPYRVDG VLTKVSLECF HGRSKRVFDV
NVLSNEPFSD HDFQRWHHQM MEDKLSMPSK NFVQRKLNDL RDMSKYVLSE KEVSDIINRK
KELSRVPSNI AAEKTRLRQR RQAAYVAGNA ELVKEIDDQL NTLEELSMGS NQNSNSAMDQ
LAKVNERNRR RNHTEIRLAE QRMNEERRRL SAAATATPMS APTSVLTGTS PQPSPSLSTS
IMSTPKLNPS ESVVVASEKA SSPDLSPKLL PSESQIFDEG IAVTQTPNTL EDKDFKLHEK
AVHGIDDIIA TVDFGIDINI
