MPS1_DICDI
ID MPS1_DICDI Reviewed; 983 AA.
AC Q54UL8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable serine/threonine-protein kinase mps1;
DE EC=2.7.11.1;
DE AltName: Full=Monopolar spindle protein 1;
GN Name=mps1; Synonyms=ttkA; ORFNames=DDB_G0280995;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=15548420; DOI=10.1016/s0074-7696(04)41003-1;
RA Graef R., Daunderer C., Schulz I.;
RT "Molecular and functional analysis of the dictyostelium centrosome.";
RL Int. Rev. Cytol. 241:155-202(2004).
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 -!- 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;
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; AAFI02000040; EAL66794.1; -; Genomic_DNA.
DR RefSeq; XP_640758.1; XM_635666.1.
DR AlphaFoldDB; Q54UL8; -.
DR SMR; Q54UL8; -.
DR STRING; 44689.DDB0220499; -.
DR PaxDb; Q54UL8; -.
DR EnsemblProtists; EAL66794; EAL66794; DDB_G0280995.
DR GeneID; 8622811; -.
DR KEGG; ddi:DDB_G0280995; -.
DR dictyBase; DDB_G0280995; mps1.
DR eggNOG; KOG0596; Eukaryota.
DR HOGENOM; CLU_303152_0_0_1; -.
DR InParanoid; Q54UL8; -.
DR OMA; ILYEMAF; -.
DR PRO; PR:Q54UL8; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005813; C:centrosome; TAS:dictyBase.
DR GO; GO:0000776; C:kinetochore; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; ISS:dictyBase.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051304; P:chromosome separation; IEA:InterPro.
DR GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0034501; P:protein localization to kinetochore; IBA:GO_Central.
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 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.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..983
FT /note="Probable serine/threonine-protein kinase mps1"
FT /id="PRO_0000362023"
FT DOMAIN 714..981
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 380..430
FT /evidence="ECO:0000255"
FT COILED 474..517
FT /evidence="ECO:0000255"
FT COILED 588..665
FT /evidence="ECO:0000255"
FT COMPBIAS 252..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..404
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 838
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 720..728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 742
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 983 AA; 113573 MW; D5AA50138AF11D86 CRC64;
MDTHQSFNEN QHPNFNSGNH GGINMNRFQR FSKPTISPIQ QQQQPQPQQP SSIIQRQSII
MTQPQPQPQP QMIPIFREPN EWYKLIDMEM NKFNNESRPS PEYIKYLTQL FQQALDSLEH
KNTPEFYLFL LNRATFQSKI GENEDAKGTL KYMKVLKMES FEVFVLLSEI ESKSFRFSKA
RSIINRGIQK IPSRSKEFEG FLMVIDIQED EFSRNGCIIS NNNNISFNNG DVNNNSIIMN
ENDQPMVINL NPQQQQQQQQ QPYEISSSSS LMSTPASSRH LSNRSSIVPT PNSSTKLSES
IKTIGLRSVQ PRRVIHKQTT TNFNTTTTTI PENSYDDDAD QPMDHDGNNN NNFRIHSNNN
NNSSANSSYN KSENDEDDQD EEDEEEEDED EDDDEEDEEE YEDNNNNNNN NNNNNNNNNN
NNNNNNNNNY FKYNRQQYIL NNDSDTSTNP NSPASSNSSV NDIINSISIT DDSKLDYENN
VKLQQQQQQQ QQQQQQQQQQ QQQQQQQQYI QQQQQQQPKI HPQRFSLQNN TPTTTTTTTA
ATNVQNPSSS SSYISPPLSS QSSELQHQRR HSIQAQRANK PPVIPPPSKL HQNNLQQQQQ
QQQQQQQQQQ QQQQQQLLLQ QQALLQQQQQ QQILLQQQQQ QQQQQQQQQQ QQKQQEQQLK
KTNMQPPPPK QPQPQTQTQQ QQKNINNSEI VDKEKSFEVA KSWSEVAMVN GKPYLRIEFI
GKGGSGKVYK VLSGDLKIYA LKYVCLSDPN EIEAQLNEIE MLKRLRKQVN IIQLIDYEVN
MAKNYILLVL EFGEIDLSKL LQRLQTPNGT NVNFIRIYWQ QMLQAVHTIH EEKIIHGDLK
PANFVSVQGS LKLIDFGIAK AIQSDDTTNI VRESQIGTIN YISPEALIDT SQGGPKQCMK
LGRASDIWSL GCILYEMAFG YPPFKSFSNI ISKYQAIINP HHKIEFPVHP NENLLKVLKL
CLIRNPHERP TIPTLLNHDF LKI
