MPS1_ENCCU
ID MPS1_ENCCU Reviewed; 586 AA.
AC Q8SSH4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable serine/threonine-protein kinase MPS1 homolog;
DE EC=2.7.12.2;
DE AltName: Full=Monopolar spindle protein 1;
GN Name=MPS1; OrderedLocusNames=ECU02_0510;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP PREDICTION OF FUNCTION.
RX PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA Barton G.J.;
RT "The complement of protein kinases of the microsporidium Encephalitozoon
RT cuniculi in relation to those of Saccharomyces cerevisiae and
RT Schizosaccharomyces pombe.";
RL BMC Genomics 8:309-309(2007).
CC -!- FUNCTION: Involved in the regulation of the onset of mitosis. Involved
CC in a pathway that coordinates cell proliferation and differentiation.
CC Implicated in spindle pole body (SPD) duplication. Dual specificity
CC kinase that can phosphorylate serine, threonine and tyrosine residues
CC (By similarity). {ECO:0000250}.
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=2.7.12.2;
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=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AL590442; CAD25082.1; -; Genomic_DNA.
DR RefSeq; NP_584578.1; NM_001040767.1.
DR AlphaFoldDB; Q8SSH4; -.
DR SMR; Q8SSH4; -.
DR STRING; 284813.Q8SSH4; -.
DR PRIDE; Q8SSH4; -.
DR GeneID; 858568; -.
DR KEGG; ecu:ECU02_0510; -.
DR VEuPathDB; MicrosporidiaDB:ECU02_0510; -.
DR HOGENOM; CLU_466934_0_0_1; -.
DR InParanoid; Q8SSH4; -.
DR OMA; CAFENSK; -.
DR OrthoDB; 496458at2759; -.
DR Proteomes; UP000000819; Chromosome II.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0051304; P:chromosome separation; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027084; Prot_kin_Mps1_fam.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22974:SF21; PTHR22974:SF21; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..586
FT /note="Probable serine/threonine-protein kinase MPS1
FT homolog"
FT /id="PRO_0000384424"
FT DOMAIN 289..540
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 167..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 295..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 586 AA; 66976 MW; CBE4BA154FBBBB6A CRC64;
MEGIFNSKSL YEYLEEQKQA GISKTKEISL YYKATSKSVG DDEYSLRIWL DYIRLLMDGT
KDVTEARETF KMIKMRFCKF YNYWEAYVRF EIEAGNGSLC KILQHSIDFV KVKEFTEKKR
VLEYLECVMS YARNGEDLSV FCRGPETSFK PGAQVLSPFE ARIGEQSKNK VLKKEHEESG
PGHRDDGKNL LSRSGRAHLA PDECKENDNK NRAREDGASL SPSFAAKSKN CGATFGTIPI
RFEKEDYSQG ITMEINAALG RTSPEGSNSS PRSGAVRSRE RIIIKGREIE ILKQIGKGGS
SKVYKVLFGS NVYALKRVEL IGDEKMLSSY INEINLLYKF KGTSEIVEII DHEVGEDYLH
ILLEYGETDL SKIIRKGGLS MNFIKDVWEQ MLLIVKRVHI ERIIHCDLKP ANFLFVKGRV
KLIDFGISKV IRNDTTSILS EEQCGTVNYM SPEAVTQNKS KVARSSDIWS LGCILYEMVH
SNPPLHEYPN LIQKIQRLQE YSEFKYTSKN KAAVMVMKEC LARDPKKRPT IDNLLNHRFL
TGEMCLESLR ELVEKILKID GGDRVDPEHV DRIAEQLHST HRQDQA
