MYLKF_DICDI
ID MYLKF_DICDI Reviewed; 928 AA.
AC Q54W86;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable myosin light chain kinase DDB_G0279831;
DE EC=2.7.11.18;
GN ORFNames=DDB_G0279831;
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).
CC -!- FUNCTION: May phosphorylate a specific serine in the N-terminus of a
CC myosin light chain.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-
CC seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-
CC COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; EC=2.7.11.18;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O-
CC phospho-L-threonyl-[myosin light chain]; Xref=Rhea:RHEA:53900,
CC Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.18;
CC -!- ACTIVITY REGULATION: Does not have a calmodulin-binding domain.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000033; EAL67529.1; -; Genomic_DNA.
DR RefSeq; XP_641506.1; XM_636414.1.
DR AlphaFoldDB; Q54W86; -.
DR SMR; Q54W86; -.
DR STRING; 44689.DDB0229351; -.
DR PaxDb; Q54W86; -.
DR PRIDE; Q54W86; -.
DR EnsemblProtists; EAL67529; EAL67529; DDB_G0279831.
DR GeneID; 8622246; -.
DR KEGG; ddi:DDB_G0279831; -.
DR dictyBase; DDB_G0279831; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_315097_0_0_1; -.
DR InParanoid; Q54W86; -.
DR OMA; NYTEEHA; -.
DR Reactome; R-DDI-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-DDI-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR PRO; PR:Q54W86; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0004687; F:myosin light chain kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..928
FT /note="Probable myosin light chain kinase DDB_G0279831"
FT /id="PRO_0000367465"
FT DOMAIN 566..868
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 53..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..440
FT /evidence="ECO:0000255"
FT COMPBIAS 485..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 699
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 572..580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 928 AA; 102891 MW; DB5D20031337D6A3 CRC64;
MGHQISKEDN GEQSNSNNLK KERRYTTNSS NLHFLYQQEE GIGINYKTGS ANNSLSNSTN
SNNNNYNNTN SSNNNNNSGN NKKITESTSL EDFKQFSTTL SISSTTPPDT PIISYNNSNN
NNNNNNNNKS NKAVHFTRTR SRSLNITNTS RNLKVTSSPI IDSQVCAPNN SYNSSIQSLN
SLSSTNSLSI NTNTNTSSSL SLSSNSSNNS LSTLTNTTTT TTTTTTTNTT QQQQPIKGRK
SKSSNALFKS LRSSLTGSSS SNSNSGKKRS SSISSSTNSL DINSANNNNN NNNSLKVSSK
KSSKGGSPNS STESLQSLST SASASSLTST PPLPPKSNAF SKSQNSSASS LNKQVISSLP
PLAPTSTLTT TTTNLEVSKE SLKPSSTPID NNSVADSSYN NNNNNNNNNN NNNNNNNNNN
NNNNNKNNNN LLDRLTDQLH RDPFFYNTNT AYQEENIIVE EVVVKEEEKS LPPKKLPPPL
PPKNFKQTTT TTATTTTTTT TTMNPPSPII QNVNRNNSSS NNSSRHELLR KSSGILPPQT
EPTYPSETSS KRSSVEIKYL EENHKYQIFD RLGSGTFSDV YLCINKENGK QYAMKIIDKS
LVTMIAQHTD MKVETEVNIL KQSFHPHVIQ IIDHFESELY YYIVTELLQG GELLYQLEKN
HPSTNENVSN YTEEHARKII KQVIQAVGFL HSNKIVHRDL KPENILFRDK SLGSILKIID
FGLASYVDHD CNCNNNNDNN NNNNNNNNNN TNGEVIQPSS PPPTKLIDVC GTPEFQAPEM
VKRLGYSYPV DIWSTGIILY ILLCGHPPFQ GKNNMIVMSL IIKGELNFDS SVGWDNVSES
AKDLIRKMLN PDPEKRLTAQ QVLLHEWITT SSDVNGSPQL GAPLFYKQLR RYNSQRHFEK
IGDTLLKSQR FIYMSPEKDY LKRRSIQL
