MHCKA_DICDI
ID MHCKA_DICDI Reviewed; 1146 AA.
AC P42527; Q54EX1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Myosin heavy chain kinase A;
DE Short=MHCK-A {ECO:0000303|PubMed:7822274};
DE EC=2.7.11.7 {ECO:0000269|PubMed:7822274};
GN Name=mhkA; Synonyms=mhckA; ORFNames=DDB_G0291231;
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=AX3;
RX PubMed=7822274; DOI=10.1074/jbc.270.2.523;
RA Futey L.M., Medley Q.G., Cote G.P., Egelhoff T.T.;
RT "Structural analysis of myosin heavy chain kinase A from Dictyostelium.
RT Evidence for a highly divergent protein kinase domain, an amino-terminal
RT coiled-coil domain, and a domain homologous to the beta-subunit of
RT heterotrimeric G proteins.";
RL J. Biol. Chem. 270:523-529(1995).
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).
RN [3]
RP CHARACTERIZATION OF THE CATALYTIC DOMAIN.
RC STRAIN=AX3;
RX PubMed=9054368; DOI=10.1074/jbc.272.11.6846;
RA Cote G.P., Luo X., Murphy M.B., Egelhoff T.T.;
RT "Mapping of the novel protein kinase catalytic domain of Dictyostelium
RT myosin II heavy chain kinase A.";
RL J. Biol. Chem. 272:6846-6849(1997).
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:7822274). This
CC phosphorylation is critical for regulating the assembly and disassembly
CC of myosin II filament, affecting myosin localization during an array of
CC cellular contractile events, including cytokinesis and capping of cell
CC surface receptors as well as chemotactic cell locomotion
CC (PubMed:7822274). {ECO:0000269|PubMed:7822274,
CC ECO:0000303|PubMed:7822274}.
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:7822274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11425;
CC Evidence={ECO:0000269|PubMed:7822274};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- SUBUNIT: Oligomer.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U16856; AAA66070.1; -; mRNA.
DR EMBL; AAFI02000177; EAL61599.1; -; Genomic_DNA.
DR PIR; A55532; A55532.
DR RefSeq; XP_635119.1; XM_630027.1.
DR PDB; 3LKM; X-ray; 1.60 A; A=552-841.
DR PDB; 3LLA; X-ray; 2.11 A; A/B=552-841.
DR PDB; 3LMH; X-ray; 2.00 A; A/B=552-841.
DR PDB; 3LMI; X-ray; 2.20 A; A/B/C/D=552-841.
DR PDB; 3PDT; X-ray; 1.80 A; A=552-809.
DR PDB; 4ZME; X-ray; 1.98 A; A/B=552-841.
DR PDB; 4ZMF; X-ray; 2.39 A; A/B=552-841.
DR PDB; 4ZS4; X-ray; 2.40 A; A/B=552-841.
DR PDB; 5DYJ; X-ray; 2.50 A; A/B=552-841.
DR PDB; 5E4H; X-ray; 2.90 A; A/B/C/D/E/F/G/H=552-841.
DR PDB; 5E9E; X-ray; 2.40 A; A/B=552-841.
DR PDBsum; 3LKM; -.
DR PDBsum; 3LLA; -.
DR PDBsum; 3LMH; -.
DR PDBsum; 3LMI; -.
DR PDBsum; 3PDT; -.
DR PDBsum; 4ZME; -.
DR PDBsum; 4ZMF; -.
DR PDBsum; 4ZS4; -.
DR PDBsum; 5DYJ; -.
DR PDBsum; 5E4H; -.
DR PDBsum; 5E9E; -.
DR AlphaFoldDB; P42527; -.
DR SMR; P42527; -.
DR STRING; 44689.DDB0216274; -.
DR PaxDb; P42527; -.
DR EnsemblProtists; EAL61599; EAL61599; DDB_G0291231.
DR GeneID; 8628066; -.
DR KEGG; ddi:DDB_G0291231; -.
DR dictyBase; DDB_G0291231; mhkA.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_277130_0_0_1; -.
DR InParanoid; P42527; -.
DR OMA; CNAVCAL; -.
DR PhylomeDB; P42527; -.
DR BRENDA; 2.7.11.7; 1939.
DR EvolutionaryTrace; P42527; -.
DR PRO; PR:P42527; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IDA:dictyBase.
DR GO; GO:0043531; F:ADP binding; IDA:dictyBase.
DR GO; GO:0016208; F:AMP binding; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IDA:dictyBase.
DR GO; GO:0030552; F:cAMP binding; IDA:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IPI: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:0004672; F:protein kinase activity; IDA:dictyBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:dictyBase.
DR GO; GO:0051764; P:actin crosslink formation; IDA:dictyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0031037; P:myosin II filament disassembly; IDA:dictyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA: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; 4.
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; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; WD repeat.
FT CHAIN 1..1146
FT /note="Myosin heavy chain kinase A"
FT /id="PRO_0000051047"
FT DOMAIN 564..808
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REPEAT 867..897
FT /note="WD 1"
FT REPEAT 910..938
FT /note="WD 2"
FT REPEAT 952..980
FT /note="WD 3"
FT REPEAT 993..1021
FT /note="WD 4"
FT REPEAT 1033..1061
FT /note="WD 5"
FT REPEAT 1073..1101
FT /note="WD 6"
FT REPEAT 1114..1142
FT /note="WD 7"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..551
FT /note="Pseudosubstrate/autoinhibitory domain"
FT /evidence="ECO:0000255"
FT REGION 515..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..852
FT /note="Catalytic"
FT COILED 100..120
FT /evidence="ECO:0000255"
FT COILED 187..241
FT /evidence="ECO:0000255"
FT COILED 297..502
FT /evidence="ECO:0000255"
FT BINDING 778..783
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 391
FT /note="S -> A (in Ref. 1; AAA66070)"
FT /evidence="ECO:0000305"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:4ZME"
FT STRAND 558..566
FT /evidence="ECO:0007829|PDB:3LKM"
FT TURN 567..570
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 571..581
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 590..605
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 614..618
FT /evidence="ECO:0007829|PDB:5E4H"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:5E4H"
FT HELIX 632..635
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 641..647
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:5DYJ"
FT HELIX 652..654
FT /evidence="ECO:0007829|PDB:5DYJ"
FT HELIX 657..679
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 692..695
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 709..714
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 726..728
FT /evidence="ECO:0007829|PDB:3LKM"
FT HELIX 735..747
FT /evidence="ECO:0007829|PDB:3LKM"
FT TURN 748..750
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:3LKM"
FT STRAND 763..765
FT /evidence="ECO:0007829|PDB:4ZME"
FT STRAND 768..770
FT /evidence="ECO:0007829|PDB:3LKM"
FT HELIX 783..793
FT /evidence="ECO:0007829|PDB:3LKM"
FT HELIX 798..802
FT /evidence="ECO:0007829|PDB:3LKM"
SQ SEQUENCE 1146 AA; 128962 MW; 54A651F6CC38CA8E CRC64;
MFNIKKRKES ITGIPPINVN SPQSVPLSGT LQSPLITPNS PNFVSRQCPF KKFGCSSFLV
SKAEFDNHLK DDAQFHLQLA VEKFDHQFDL HTQLMAHFTE QMEDQLEKTM KVVRNHTDSL
GGNVQTKLDE GIEKCMAFAK KVEQQQQQLA KRLITQQIQE KKSTSSPLVK GGISGGGGSG
GDDSFDGANI SSMSTSKQEL QQELQSLSIK MKKELTELSD ELSQKLERST GNIDIKIKRI
EGEVNEKIDK RQLVSTIDDS IGKKTDSIGY TLESSIIKKV EEKEKKKSEQ NQLLFDSKIE
SLKDKIKIIE TQQLDTSSEV RKLKLESTSS GNLMAGLNGT SGRPSSSSHF IPSSVSAAAN
NINKNEIMEE VKKVEEKLQK KIREEIDNTK SELSKVERSV KDNRSEIEGL EKDCKNQFDK
QDNKIKQVED DLKKSDSLLL LMQNNLKKYN EFVDRERDRE SERLKLQDSI KRLEQNQKKI
EAEIQEGNEQ VERVLREEAS ISPISSVPKS PITTKRSSII LNSPPMTSQQ SSPKIQDLLS
SSGSSSVSGI NISSETGEMG ILWEFDPIIN KWIRLSMKLK VERKPFAEGA LREAYHTVSL
GVGTDENYPL GTTTKLFPPI EMISPISKNN EAMTQLKNGT KFVLKLYKKE AEQQASRELY
FEDVKMQMVC RDWGNKFNQK KPPKKIEFLM SWVVELIDRS PSSNGQPILC SIEPLLVGEF
KKNNSNYGAV LTNRSTPQAF SHFTYELSNK QMIVVDIQGV DDLYTDPQIH TPDGKGFGLG
NLGKAGINKF ITTHKCNAVC ALLDLDVKLG GVLSGNNKKQ LQQGTMVMPD ILPELMPSDN
TIKVGAKQLP KAEFSKKDLK CVSTIQSFRE RVNSIAFFDN QKLLCAGYGD GTYRVFDVND
NWKCLYTVNG HRKSIESIAC NSNYIFTSSP DNTIKVHIIR SGNTKCIETL VGHTGEVNCV
VANEKYLFSC SYDKTIKVWD LSTFKEIKSF EGVHTKYIKT LALSGRYLFS GGNDQIIYVW
DTETLSMLFN MQGHEDWVLS LHCTASYLFS TSKDNVIKIW DLSNFSCIDT LKGHWNSVSS
CVVKDRYLYS GSEDNSIKVW DLDTLECVYT IPKSHSLGVK CLMVFNNQII SAAFDGSIKV
WEWQSK
