RBA50_SCHPO
ID RBA50_SCHPO Reviewed; 452 AA.
AC O43088;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=RNA polymerase II-associated protein rba50;
GN Name=rba50; ORFNames=SPBC947.13;
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).
CC -!- FUNCTION: Forms an interface between the RNA polymerase II enzyme and
CC chaperone/scaffolding proteins, suggesting that it is required to
CC connect RNA polymerase II to regulators of protein complex formation.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RNA polymerase II. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the RPAP1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17041.1; -; Genomic_DNA.
DR PIR; T40769; T40769.
DR RefSeq; NP_595263.1; NM_001021170.2.
DR AlphaFoldDB; O43088; -.
DR BioGRID; 277785; 3.
DR STRING; 4896.SPBC947.13.1; -.
DR iPTMnet; O43088; -.
DR MaxQB; O43088; -.
DR PaxDb; O43088; -.
DR PRIDE; O43088; -.
DR EnsemblFungi; SPBC947.13.1; SPBC947.13.1:pep; SPBC947.13.
DR GeneID; 2541271; -.
DR KEGG; spo:SPBC947.13; -.
DR PomBase; SPBC947.13; rba50.
DR VEuPathDB; FungiDB:SPBC947.13; -.
DR eggNOG; KOG1894; Eukaryota.
DR HOGENOM; CLU_031074_1_0_1; -.
DR InParanoid; O43088; -.
DR PhylomeDB; O43088; -.
DR PRO; PR:O43088; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISO:PomBase.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:PomBase.
DR InterPro; IPR013929; RNA_pol_II_AP1_C.
DR InterPro; IPR013930; RNA_pol_II_AP1_N.
DR InterPro; IPR039913; RPAP1/Rba50.
DR PANTHER; PTHR21483; PTHR21483; 1.
DR Pfam; PF08620; RPAP1_C; 1.
DR Pfam; PF08621; RPAP1_N; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..452
FT /note="RNA polymerase II-associated protein rba50"
FT /id="PRO_0000374018"
FT REGION 60..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 50797 MW; D8C11A66055B1DD3 CRC64;
MENHRSVFSN VIGDIVEKPP KQLVEVKRSV QRHARGFPAV SRTLPKRESK SMSAYKEKML
RKNKESPGLE GKGNLDDQGI DEENRVRLER MNDLEIEGAQ EEIRATIRDD LLEMLKKRAF
KKKAERELAQ RKDRSSQVNT PDLSQRPSDD SFLSNEKLRS SEKLNRNLQS VLSSEAVDSS
SGSPSPPMAL SQAEIRSRQT KRVMFPDKAE ELTKIFSLPT LAPIKGNEED DASEDAKHSP
KKHSPALSDG TTSNDGAPLE FDTTHLPEKQ VTLDPNDPSF YEQLHDKYFP NLPVDEKQMQ
WLHDPSPAEN SYHPSVESLH AHEIRFGFKG EIITPSQSQT IPVNEGLHHH GDAPFSAGYT
LVELAHLLRS SFPTQRCIAI QTIGRIIYRL NSGEFREVLS PELHTLVEDA HIYELLAAAA
SDQVKHLTVR SLAIEALWLC SQSQHGSSRS AV
