MBK1_CAEBR
ID MBK1_CAEBR Reviewed; 904 AA.
AC A8X4H1;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase mbk-1 {ECO:0000250|UniProtKB:Q13627};
DE EC=2.7.12.1 {ECO:0000250|UniProtKB:Q9XTF3};
DE AltName: Full=Dual specificity Yak1-related kinase mbk-1 {ECO:0000250|UniProtKB:Q13627};
DE AltName: Full=Minibrain Kinase 1 {ECO:0000250|UniProtKB:Q9XTF3};
GN Name=mbk-1 {ECO:0000312|EMBL:CAP27531.2}; ORFNames=CBG07597;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP27531.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP27531.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Possible role in the function of olfactory neurons.
CC {ECO:0000250|UniProtKB:Q8WQL7}.
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=2.7.12.1;
CC Evidence={ECO:0000250|UniProtKB:Q9XTF3};
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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:Q9XTF3};
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=2.7.12.1;
CC Evidence={ECO:0000250|UniProtKB:Q9XTF3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9XTF3};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WQL7}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MNB/DYRK subfamily. {ECO:0000255}.
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DR EMBL; HE601041; CAP27531.2; -; Genomic_DNA.
DR AlphaFoldDB; A8X4H1; -.
DR SMR; A8X4H1; -.
DR STRING; 6238.CBG07597; -.
DR PRIDE; A8X4H1; -.
DR WormBase; CBG07597a; CBP40416; WBGene00029589; Cbr-mbk-1.
DR eggNOG; KOG0667; Eukaryota.
DR HOGENOM; CLU_014959_0_0_1; -.
DR InParanoid; A8X4H1; -.
DR OMA; DGIYYCK; -.
DR OrthoDB; 870358at2759; -.
DR Proteomes; UP000008549; Chromosome X.
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; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:InterPro.
DR CDD; cd14226; PKc_DYRK1; 1.
DR InterPro; IPR028318; DYRK1A/B_MNB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR044131; PKc_DYR1A/1B.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24058:SF121; PTHR24058:SF121; 2.
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; Magnesium; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..904
FT /note="Dual specificity tyrosine-phosphorylation-regulated
FT kinase mbk-1"
FT /id="PRO_0000390714"
FT DOMAIN 367..690
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 495
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 373..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 904 AA; 102612 MW; 6553A1ABAC918CA4 CRC64;
MNSGEKQDNL QAWGQQPSSS YSNTQQQHGQ ITGQIPLTIT NQVEAHDNDF HMQDASNDEL
EKSKKIAEQP TEHPQQHHQQ QPAVPRFPPQ SRQPQAILRF PQPPITSINK ANNSNSQNFF
PQQEVLQSRP KKHRVSMTNA EAANTPGMPP EKLPAKKLSA DSQRPLFRDS NVFQRSAGQF
TNDNGPSSSS AIVGAPFDAN SSSKPVHIQQ FRNPNDAPVT KLTSDLIKTY KAINEKFQSF
YLRKNVRRST VGRHTSLDSS GKPKTGKEAS SSDANLIETF SIHNAVPNTS SSGNQPHYDS
HVNAPPLLDT NAPPTSTMVV PMRTETESQQ QMRQKSSRGG PYNNGYDDQN YDYILKNGEI
FDKRYVILSD TPVGKGSFGQ VTKAYDTVTK EEVAIKIIKN KKTFFDQAQI EIHLLELTNA
HDKDNKYNIV TLKGHFVHRA HLCLVFELLS YNLYDLLKNT NFRGVSLNLA RKFAQQLGKT
LLFLSSPELS IIHCDLKPEN VLLVNAKRSQ IRVIDFGSSC QTGHRIYQYI QSRFYRSPEV
LLGIAYDTKI DMWSLGCILV EMHTGEPLFA GSSEVDQMMK IVEVLGMPPK EMLDIGPKTH
KYFDKTEDGI YYCKKTRDGY RHTYKAPGAR KLHEILGVTS GGPGGRRLGE PGHSVEDYSK
FKDLIKRMLN FDPKQRILRT TLFPVSHTAY NQNLYHQQQI DQVPAVGSVY IEDNGMYRPV
PTSSHPISVT SSFDDGDVIE IDPNRRRYSQ QNYHNPNYQY SQQPQSSSQQ QQQQYQQSQR
AQLEKQQQLQ QQQQQQQQQR QHLSHQPSQS VQQHSSSSSR SRPRQQDQAE WRTQLELEEA
FKQRKAEEAT APRSLQYNPQ QVVGVQLIKR VLISKLFQGS MSHGNVNAGS SRDMEKHDYP
NNKL
