ID MSA1_SCHPO Reviewed; 533 AA. AC Q10277; Q9US63; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 29-MAY-2013, entry version 89. DE RecName: Full=Multicopy suppressor of sporulation protein msa1; GN Name=msa1; ORFNames=SPAC13G7.13c, SPAC6C3.01c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX PubMed=15166138; DOI=10.1534/genetics.167.1.77; RA Jeong H.T., Ozoe F., Tanaka K., Nakagawa T., Matsuda H., Kawamukai M.; RT "A novel gene, msa1, inhibits sexual differentiation in RT Schizosaccharomyces pombe."; RL Genetics 167:77-91(2004). 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., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 210-384, AND RP SUBCELLULAR LOCATION. RC STRAIN=ATCC 38364 / 968; RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x; RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., RA Hiraoka Y.; RT "Large-scale screening of intracellular protein localization in living RT fission yeast cells by the use of a GFP-fusion genomic DNA library."; RL Genes Cells 5:169-190(2000). CC -!- FUNCTION: Negative regulator of sexual differentiation. Acts by CC repressing the transcription of meiosis-inducing, ste11-regulated CC genes. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains. 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; CU329670; CAA93601.1; -; Genomic_DNA. DR EMBL; AB028018; BAA87322.1; -; Genomic_DNA. DR PIR; T39025; T39025. DR RefSeq; NP_593715.2; NM_001019146.2. DR ProteinModelPortal; Q10277; -. DR MINT; MINT-4698346; -. DR STRING; 4896.SPAC13G7.13c-1; -. DR EnsemblFungi; SPAC13G7.13c.1; SPAC13G7.13c.1:pep; SPAC13G7.13c. DR GeneID; 2542861; -. DR KEGG; spo:SPAC13G7.13c; -. DR PomBase; SPAC13G7.13c; -. DR eggNOG; NOG322326; -. DR OrthoDB; EOG41ZJKV; -. DR NextBio; 20803902; -. DR GO; GO:0005829; C:cytosol; IDA:PomBase. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IMP:PomBase. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.330; -; 3. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. PE 4: Predicted; KW Complete proteome; Cytoplasm; Reference proteome; Repeat; Repressor; KW RNA-binding; Transcription; Transcription regulation. FT CHAIN 1 533 Multicopy suppressor of sporulation FT protein msa1. FT /FTId=PRO_0000081648. FT DOMAIN 79 158 RRM 1. FT DOMAIN 365 441 RRM 2. SQ SEQUENCE 533 AA; 59118 MW; A2A8A1633A0EC572 CRC64; MVVSSPSVSL LHSPVEKLSA QLEKTTLLQD IPPGSLSEND NSTTFIKPPL ETASSSTPIP SSSSSGVLNP SSVRGKPVAC LFVASLNSSR SEEELTATVK DYFQQWGPLL HVKVLKDWLQ RPYSFVQFQN TDDASKALSE AQNTILDGRH IRIERAKVNR TIRISSAPHQ PYITKKDIDN LLEPYGEVED VTEIPDQSAF LVRFVYRDEA IAAYTALKHS AWPVLWAENV TYQNGHYKKK GSSPFSPPNA HSRRRKSQGK DQSNTPVIKA PAPIPFSVSS DPPSTMGRSN SAVQSPSYFA HSLVNSTEFS TPNESLSSLP SILPSIPSLE SGKAELPTDG SFEQPGYPMN PSMMFAAMPP PIDPYSIFVG QLDPVNCTHY LLVDLFSKYG KVIDCKIIHQ SKKPAFAFLR FDSQQAAYAA VCGKTRSPHQ KKPLRVEFRQ LRPMQQFSPQ YQYPSYPYPM FPAPFSPPRN AMMPIPAPMD QFSTFHQSMA TLPPGAVPTS IPQSYYPIYS PEMAMPQSYS PMYYTHNPPM DGN //