MSC1_SCHPO
ID MSC1_SCHPO Reviewed; 1588 AA.
AC Q9UT79;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Multicopy suppressor of chk1 protein 1;
GN Name=msc1; ORFNames=SPAC343.11c;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15082762; DOI=10.1128/mcb.24.9.3660-3669.2004;
RA Ahmed S., Palermo C., Wan S., Walworth N.C.;
RT "A novel protein with similarities to Rb binding protein 2 compensates for
RT loss of Chk1 function and affects histone modification in fission yeast.";
RL Mol. Cell. Biol. 24:3660-3669(2004).
CC -!- FUNCTION: Has a role in regulating chromatin structure via global
CC deacetylation of histone H3. This function is associated with the
CC activity of a histone deacetylase. {ECO:0000269|PubMed:15082762}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537,
CC ECO:0000269|PubMed:15082762}. Note=Associates with chromatin.
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DR EMBL; CU329670; CAB52274.1; -; Genomic_DNA.
DR PIR; T38660; T38660.
DR RefSeq; NP_593431.1; NM_001018864.2.
DR AlphaFoldDB; Q9UT79; -.
DR SMR; Q9UT79; -.
DR BioGRID; 278205; 124.
DR IntAct; Q9UT79; 1.
DR STRING; 4896.SPAC343.11c.1; -.
DR iPTMnet; Q9UT79; -.
DR MaxQB; Q9UT79; -.
DR PaxDb; Q9UT79; -.
DR PRIDE; Q9UT79; -.
DR EnsemblFungi; SPAC343.11c.1; SPAC343.11c.1:pep; SPAC343.11c.
DR GeneID; 2541710; -.
DR KEGG; spo:SPAC343.11c; -.
DR PomBase; SPAC343.11c; msc1.
DR VEuPathDB; FungiDB:SPAC343.11c; -.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_247392_0_0_1; -.
DR InParanoid; Q9UT79; -.
DR OMA; DYHCISS; -.
DR PhylomeDB; Q9UT79; -.
DR PRO; PR:Q9UT79; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000812; C:Swr1 complex; IDA:PomBase.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IBA:GO_Central.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IPI:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR Gene3D; 3.30.40.10; -; 3.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF57903; SSF57903; 3.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 3.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1588
FT /note="Multicopy suppressor of chk1 protein 1"
FT /id="PRO_0000096590"
FT DOMAIN 82..124
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 475..645
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 298..345
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1171..1220
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1454..1505
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 38..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 180352 MW; 2D18248ABB3DBC55 CRC64;
MRKNSSHENQ SSENIIEFPY VDFEELNVHS NIFSELEHAK PSTQQQQQQQ NISNETTSTG
PRICISRDEF KAVNLLTKEE INVRVTPKKE EFSRGLDFIS DLYDQTARKS GAVRVIPPDN
WKCPLTINTT TFKFLTRKNN PSSMSLVSNY PLDAISSQQK FHGNDKTLEK NSAKATINKS
NSTAETSSTA TVEPYDSNDL YRIFDRPDAV VLSYIFVLGK AVDLLQIKQW LQLSKQKNLL
EFEFWSQAAQ HYKLDVNSLR NAYNLYAETG VTTRTGNDGG SPINRPAKRV KRQNHIPKCK
LCAQEGSSLV TCCICQSNYH YACVEAPFAP FSDIHYWTCN SCIPSSLKIL WKEVDYHCIS
SFLQSSNELA SSLKKQLPSF LAQTPLTLPS NTKTPPASAR QSSRRTRSTS GKGFETKISI
NLDSDIKLLN TLSPLETFFW CCSFPSTAST SSPFSYYPES LPTPLLGRAV NTTAFPTSRQ
NAYYNDPWNL YFIHFSKLSP LRFTPPGILT STISLGQPLT CQGWQRDSMS LFGMHYHHYG
AQRIWYVIPE VDGPKYEKLL NDLSPSFIQE KPETLIKSKI LLPISMLISN GIQVLTFVQN
SNEFVITSPN TYYTVLDTGF SLSESVPFAT KEWIQDMHAE NSFNMYKNLH ISAPFSLDHI
LLANATLDKT VHSAYWLMTC LKDRVDRELT LRNEFRKRHP LLTWIPTPLE SSVMACAFCK
TFAYLASIEE KNGTKTACLS HKDECFPNTD SDLTVLVRYD DNALLAAYSK VVERAHKADT
WLENYKEALG SDNSRPSLKV LKTLLNEAET ICCPLQEVSL VRNLVKTAQQ WLDKFAIIFK
KKSMVKKEKR KPKRGSATHS HLESPSEEVE DLNSSNINEA DLLINLVEEA EQFTFDFPEM
AVAFEKAESL KIFREKANAM KERSLSYEEC LAIVEEGESL QLKTPELLYF KQYMEKTEWI
DSFNQISQKT DSTMEELVEL IERGEKIGLT SDNENMATAL LLKEKSENWM KQVEGLLSQE
TLSTSKLFQL KSEANSICIN RGLLEQLNEV LQKSENFHTQ LVSLISRARD PDYYSRPTIE
EAKTVLAESE NLTNKPEEYT VAQKLLTQTY EWVRRGKRLF GKANAPLEIF NQHLEFVEQR
NTNAMVDEGS DAPFHVGNEY YVIAGSDPSD FHYCFCRQPE AGMMIECELC HEWYHAKCMK
MSKKKLRADE KFICPICDYR VEVPRHSHRP PLIELQKMVD DIPTLPFQPI EIELLKRVVK
QAEEFKNKMQ SEVCDPTQLS EKDVPLLQFY LRKLEGSEIL FTEELNVFRQ KLHEFMPVAP
QPPPFIGESR SNRKPRPTKR QREIMEQVES GKLTSAEGAA AIAATQTRNQ NNFISKPFNV
HTLSTTLSPW AMKSLAQAAI SPNPMPSAHD LLPTSNPAEL FTNISPEIKE LSVDSTSTLG
GLNSSHLVSD QNASVICLCR QPFAISDGTV QCHNCLEWFH YECVGLSSDI VSTLSNYACP
DCCSKEGKLY PWNTRPRSTP SVWLSQAYSP SVLQGTTENV AFLNKAFSAS ANLFDVLPVS
NTPSHFSKMD YVLEDRKPDL FTETYLSM
