MHCKB_DICDI
ID MHCKB_DICDI Reviewed; 732 AA.
AC P90648; Q54HZ5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Myosin heavy chain kinase B;
DE Short=MHCK-B {ECO:0000303|PubMed:9115238};
DE EC=2.7.11.7 {ECO:0000269|PubMed:9115238};
GN Name=mhkB; Synonyms=mhckB; ORFNames=DDB_G0289115;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=AX3;
RX PubMed=9115238; DOI=10.1074/jbc.272.18.11812;
RA Clancy C.E., Mendoza M.G., Naismith T.V., Kolman M.F., Egelhoff T.T.;
RT "Identification of a protein kinase from Dictyostelium with homology to the
RT novel catalytic domain of myosin heavy chain kinase A.";
RL J. Biol. Chem. 272:11812-11815(1997).
RN [2]
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: Catalyzes its autophosphorylation, which is needed for
CC enzymatic activity and phosphorylates myosin II heavy chain at a
CC threonine in the C-terminal tail region (PubMed:9115238). This
CC phosphorylation is critical in regulating the assembly and disassembly
CC of myosin II filament (PubMed:9115238). Participates in control of
CC myosin localization (PubMed:9115238). {ECO:0000269|PubMed:9115238,
CC ECO:0000303|PubMed:9115238}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[myosin heavy-chain] = ADP + H(+) + O-
CC phospho-L-threonyl-[myosin heavy-chain]; Xref=Rhea:RHEA:11424,
CC Rhea:RHEA-COMP:13718, Rhea:RHEA-COMP:13719, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.7;
CC Evidence={ECO:0000269|PubMed:9115238};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11425;
CC Evidence={ECO:0000269|PubMed:9115238};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000305}.
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DR EMBL; U90946; AAB50136.1; -; mRNA.
DR EMBL; AAFI02000130; EAL62865.1; -; Genomic_DNA.
DR RefSeq; XP_636368.1; XM_631276.1.
DR AlphaFoldDB; P90648; -.
DR SMR; P90648; -.
DR STRING; 44689.DDB0191333; -.
DR PaxDb; P90648; -.
DR EnsemblProtists; EAL62865; EAL62865; DDB_G0289115.
DR GeneID; 8626969; -.
DR KEGG; ddi:DDB_G0289115; -.
DR dictyBase; DDB_G0289115; mhkB.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_378764_0_0_1; -.
DR InParanoid; P90648; -.
DR OMA; CVLEFVD; -.
DR PhylomeDB; P90648; -.
DR BRENDA; 2.7.11.7; 1939.
DR PRO; PR:P90648; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0016905; F:myosin heavy chain kinase activity; IDA:dictyBase.
DR GO; GO:0045159; F:myosin II binding; IPI:dictyBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0031037; P:myosin II filament disassembly; IMP:dictyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
DR GO; GO:1903013; P:response to differentiation-inducing factor 1; HDA:dictyBase.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR004166; MHCK_EF2_kinase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; WD repeat.
FT CHAIN 1..732
FT /note="Myosin heavy chain kinase B"
FT /id="PRO_0000051048"
FT DOMAIN 124..328
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REPEAT 458..486
FT /note="WD 1"
FT REPEAT 500..528
FT /note="WD 2"
FT REPEAT 540..568
FT /note="WD 3"
FT REPEAT 580..608
FT /note="WD 4"
FT REPEAT 620..648
FT /note="WD 5"
FT REPEAT 660..688
FT /note="WD 6"
FT REPEAT 700..730
FT /note="WD 7"
FT REGION 331..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 732 AA; 83168 MW; A7233C4BD56D4088 CRC64;
MIFKVWFSYE DEEVELSELT NDTTVSAIRK ILHEGKIFRF PYGTSQTDLQ IGKMLPSGSG
GGATADSKFE KFKARNTLAD IQYKVGDTLY VRVKKSKPTN DSLLPTLNIA FLDGSERAIK
WEYDPYTTTA QWTCTATLVK VEPVPFAEGA FRKAYHTLDL SKSGASGRYV SKIGKKPTPR
PSYFEDVKMQ MIAKKWADKY NSFKPPKKIE FLQSCVLEFV DRTSSDLICG AEPYVEGQYR
KYNNNSGFVS NDERNTPQSF SHFTYEHSNH QLLIIDIQGV GDHYTDPQIH TYDGVGFGIG
NLGQKGFEKF LDTHKCNAIC QYLNLQSINP KSEKSDCGTV PRPDLIFPDT SERDNNNNNN
NNNNNNNNNN NNNSNNNNNN NSSISKSLVE ISSGSKERND RDSPSRQLFV SNDGNTLNTN
KERSKSKSID LEKPEILINN KKKESINLET IKLIETIKGY HVTSHLCICD NLLFTGCSDN
SIRVYDYKSQ NMECVQTLKG HEGPVESICY NDQYLFSGSS DHSIKVWDLK KLRCIFTLEG
HDKPVHTVLL NDKYLFSGSS DKTIKVWDLK TLECKYTLES HARAVKTLCI SGQYLFSGSN
DKTIKVWDLK TFRCNYTLKG HTKWVTTICI LGTNLYSGSY DKTIRVWNLK SLECSATLRG
HDRWVEHMVI CDKLLFTASD DNTIKIWDLE TLRCNTTLEG HNATVQCLAV WEDKKCVISC
SHDQSIRVWG WN
