MUG58_SCHPO
ID MUG58_SCHPO Reviewed; 277 AA.
AC Q9UUH3; P78883; Q9UU30;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Uncharacterized kinase mug58;
DE EC=2.7.-.-;
DE AltName: Full=Meiotically up-regulated gene 58 protein;
GN Name=mug58; ORFNames=SPAC630.09c;
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 MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
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., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 75-225, AND SUBCELLULAR
RP 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).
RN [4]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [5]
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: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the GLYK kinase family. {ECO:0000305}.
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DR EMBL; D89234; BAA13895.1; -; mRNA.
DR EMBL; CU329670; CAB52731.1; -; Genomic_DNA.
DR EMBL; AB027848; BAA87152.1; -; Genomic_DNA.
DR PIR; T38987; T38987.
DR PIR; T43138; T43138.
DR RefSeq; NP_592905.1; NM_001018305.2.
DR AlphaFoldDB; Q9UUH3; -.
DR SMR; Q9UUH3; -.
DR BioGRID; 279803; 12.
DR STRING; 4896.SPAC630.09c.1; -.
DR MaxQB; Q9UUH3; -.
DR PaxDb; Q9UUH3; -.
DR EnsemblFungi; SPAC630.09c.1; SPAC630.09c.1:pep; SPAC630.09c.
DR GeneID; 2543381; -.
DR KEGG; spo:SPAC630.09c; -.
DR PomBase; SPAC630.09c; mug58.
DR VEuPathDB; FungiDB:SPAC630.09c; -.
DR eggNOG; KOG2878; Eukaryota.
DR HOGENOM; CLU_056986_1_0_1; -.
DR InParanoid; Q9UUH3; -.
DR OMA; THEARRW; -.
DR PhylomeDB; Q9UUH3; -.
DR PRO; PR:Q9UUH3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008887; F:glycerate kinase activity; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010488; Zeta_toxin_domain.
DR Pfam; PF06414; Zeta_toxin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..277
FT /note="Uncharacterized kinase mug58"
FT /id="PRO_0000214077"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97QZ1"
FT CONFLICT 120
FT /note="K -> Q (in Ref. 1; BAA13895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 31809 MW; 84D3DF65FFEEDBDF CRC64;
MSSLEIIVDK ILKFLEKQPK PEGRPFILGI SGPQGSGKST LASALDTELT RKNESVVKFS
LDDFYLTHAE QVELAKNNPN NPLVQHRGLA GTHDVTFLNN VLNAFVKGSD EEVSIPFYDK
SKFGGYGDRG DESQWKKANP KTTTYVIFEG WMVGFEPLDS CMLSVRARST RWQNIEGSLL
WVNRKLADYQ PIFQKIDSLV ELEAQEINYV YRWRLQQEHA LKARIHKGMS DEEVIEFVNH
YMPQYVFYLG TLSNKVHLNP HCLEIILDEN RYPVVMH
