MHCKD_DICDI
ID MHCKD_DICDI Reviewed; 941 AA.
AC Q54SF9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Myosin heavy chain kinase D;
DE Short=MHCK-D;
DE EC=2.7.11.7;
GN Name=mhkD; Synonyms=mhckD; ORFNames=DDB_G0282489;
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 NOMENCLATURE.
RX PubMed=12952069; DOI=10.1023/a:1024467426244;
RA De la Roche M.A., Smith J.L., Betapudi V., Egelhoff T.T., Cote G.P.;
RT "Signaling pathways regulating Dictyostelium myosin II.";
RL J. Muscle Res. Cell Motil. 23:703-718(2002).
RN [3]
RP FUNCTION.
RX PubMed=15987738; DOI=10.1091/mbc.e05-03-0219;
RA Yumura S., Yoshida M., Betapudi V., Licate L.S., Iwadate Y., Nagasaki A.,
RA Uyeda T.Q.P., Egelhoff T.T.;
RT "Multiple myosin II heavy chain kinases: roles in filament assembly control
RT and proper cytokinesis in Dictyostelium.";
RL Mol. Biol. Cell 16:4256-4266(2005).
CC -!- FUNCTION: Phosphorylates threonine (By similarity). Not critical for
CC regulating the assembly and disassembly of myosin II filament.
CC {ECO:0000250, ECO:0000269|PubMed:15987738}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000047; EAL66104.1; -; Genomic_DNA.
DR RefSeq; XP_640080.1; XM_634988.1.
DR AlphaFoldDB; Q54SF9; -.
DR SMR; Q54SF9; -.
DR STRING; 44689.DDB0220109; -.
DR PaxDb; Q54SF9; -.
DR EnsemblProtists; EAL66104; EAL66104; DDB_G0282489.
DR GeneID; 8623609; -.
DR KEGG; ddi:DDB_G0282489; -.
DR dictyBase; DDB_G0282489; mhkD.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_312032_0_0_1; -.
DR InParanoid; Q54SF9; -.
DR OMA; SAWVIEV; -.
DR PhylomeDB; Q54SF9; -.
DR Reactome; R-DDI-166208; mTORC1-mediated signalling.
DR PRO; PR:Q54SF9; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0016905; F:myosin heavy chain kinase activity; ISS:dictyBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:dictyBase.
DR GO; GO:0031037; P:myosin II filament disassembly; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS: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; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase; WD repeat.
FT CHAIN 1..941
FT /note="Myosin heavy chain kinase D"
FT /id="PRO_0000361272"
FT DOMAIN 337..582
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REPEAT 635..674
FT /note="WD 1"
FT REPEAT 683..720
FT /note="WD 2"
FT REPEAT 741..780
FT /note="WD 3"
FT REPEAT 783..820
FT /note="WD 4"
FT REPEAT 824..861
FT /note="WD 5"
FT REPEAT 864..902
FT /note="WD 6"
FT REPEAT 909..941
FT /note="WD 7"
FT REGION 57..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 8..48
FT /evidence="ECO:0000255"
FT COILED 289..317
FT /evidence="ECO:0000255"
FT COMPBIAS 57..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 941 AA; 105417 MW; EDFBF131EA8F400A CRC64;
MEDNSFLKLS KKIEKILEKN DYLKKKVEQL TKSVDNHEFK IQELLLLLRK NNIHPTTTTT
TTTTTNNNST CVGISNSPPL SPRTSTDSMT NSNNSSATSS TTPSPTQTST ITTTSQIDPN
SLTNSNNSFI PINSPISQTT VNNNNNNNNN NNNNNNNNNN NNNNNNNNNL NNQTITSPLS
TSSSNSNSNS NSSSPIVSPV SSPQLSGSGN RPRIQFLGNG RMPSTGNLFK KEDSSDSLLK
YSKDSEHLYI VPTTPRPSKS PSMDFIASTS LINTVSSNNT DSTNNDNSSI LNDQQNQQQN
QQQQNQQQQQ EEINFITTED KLPNLPDSNC QWAIIWEYSA NDDEWTKALI IVEIDAKPFA
KGALRNAYQL KIRSNAMQCF NHFATPIHEK YMEGKKLNLS QIPKLNQNLS LDTLYVAKDS
KTSVNFNRYF EDVKMQMVCK SYGERYNSNH PPKKIEFLSA WVIEIQGTTN YRVGNRNSSN
NTLYGLELFM KGEFKKQNSN FGTVFTERNT PQSFSHFTYE CTTHEMVVVD IQGVDDIYTD
PQVHTKDGKG YGEGNLGQKG IEKFLISHKC SPICLQFGLP PIGLETGRNA HRVIRGTMLL
PDLTPDLYEP EYPLIENQPS NPLNSELTSI VHLSGHDERV CSLLINQDKT KLYSASADGY
VKIWNLTNNE DLSKIQMIDS FRAHRRSIEK MLLNEKYLFT ASSDGTIKIW SLPTTTTTTT
TSKQSSSSSS SSYECIGKLE DHTAEVNDMC IDIENNFLVS CSFDKQIKIY DLSTFKCIKS
LNAHGKSIKS IYMSGKYLFS SSNDQSIKIW DLEMCMCVYG MNDAHDAPIT SLRMFGNRLF
SASKDGEIKD WNLSTFQPTT TLDQHNMAIT DILVTSNGYL FVSSDDSTIR IIDISNQNEP
IKIISSTKAH RSGVNSLATD GKRIFSGGCD NLIKVWNWKN K
