MUG51_SCHPO
ID MUG51_SCHPO Reviewed; 306 AA.
AC Q9P7Q6;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Serine/threonine-protein kinase mug51;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P49842};
DE AltName: Full=Meiotically up-regulated gene 51 protein;
GN Name=mug51; ORFNames=SPAC1834.09;
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 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).
CC -!- FUNCTION: Serine/threonine-protein kinase (By similarity). Has a role
CC in meiosis (PubMed:16303567). {ECO:0000250|UniProtKB:P49842,
CC ECO:0000269|PubMed:16303567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P49842};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P49842};
CC -!- SIMILARITY: Belongs to the STK19 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB75777.1; -; Genomic_DNA.
DR PIR; T50120; T50120.
DR RefSeq; NP_594688.1; NM_001020117.2.
DR AlphaFoldDB; Q9P7Q6; -.
DR BioGRID; 278635; 17.
DR PaxDb; Q9P7Q6; -.
DR PRIDE; Q9P7Q6; -.
DR EnsemblFungi; SPAC1834.09.1; SPAC1834.09.1:pep; SPAC1834.09.
DR GeneID; 2542159; -.
DR KEGG; spo:SPAC1834.09; -.
DR PomBase; SPAC1834.09; mug51.
DR VEuPathDB; FungiDB:SPAC1834.09; -.
DR HOGENOM; CLU_909615_0_0_1; -.
DR InParanoid; Q9P7Q6; -.
DR OMA; FFGWKFR; -.
DR PhylomeDB; Q9P7Q6; -.
DR PRO; PR:Q9P7Q6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; ISS:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR018865; Ser/Thr_kinase_19.
DR PANTHER; PTHR15243; PTHR15243; 1.
DR Pfam; PF10494; Stk19; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Meiosis; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..306
FT /note="Serine/threonine-protein kinase mug51"
FT /id="PRO_0000116748"
SQ SEQUENCE 306 AA; 35596 MW; 5B2B40648C2DEAAA CRC64;
MPALLKINKK KNGQTKIDRL FSKRRKTSLA IEKNHSKASM CTGQSPLNII SYNVPPLIVL
RNKTIRNSIE VLVEEMFRDI QMRQQTNVLV AQCPRMIVET QLIGLFQSNY TSVAEELEQS
IRTGDIRRLY LNRSDKFCGE SCLILRPEFD KLFTYYLCKF KDQEHIYTLI FKLHKLLIEN
PLPSYTSEEL KFNWEERRLL ISMGFLILAG TDSYGISLPN LGIFTHILRN SRNDLSNYLK
KRPYREVIES SLYNRNVSVA CKKKNEAFFG WKFRLCDAIG AGLVDSFMTT CGRAFRLTKK
GLEMKF
