ID   MYS2_DICDI              Reviewed;        2116 AA.
AC   P08799; Q54LU0;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 3.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Myosin-2 heavy chain;
DE   AltName: Full=Myosin II heavy chain;
GN   Name=mhcA; ORFNames=DDB_G0286355;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3540939; DOI=10.1073/pnas.83.24.9433;
RA   Warrick H.M., de Lozanne A., Leinwand L.A., Spudich J.A.;
RT   "Conserved protein domains in a myosin heavy chain gene from Dictyostelium
RT   discoideum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:9433-9437(1986).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2035-2116.
RX   PubMed=3901008; DOI=10.1073/pnas.82.20.6807;
RA   De Lozanne A., Lewis M., Spudich J.A., Leinwand L.A.;
RT   "Cloning and characterization of a nonmuscle myosin heavy chain cDNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:6807-6810(1985).
RN   [4]
RP   PHOSPHORYLATION AT THR-1823; THR-1833 AND THR-2029, AND MUTAGENESIS.
RC   STRAIN=AX2;
RX   PubMed=2387408; DOI=10.1016/0014-5793(90)81163-i;
RA   Lueck-Vielmeter D., Schleicher M., Grabatin B., Wippler J., Gerisch G.;
RT   "Replacement of threonine residues by serine and alanine in a
RT   phosphorylatable heavy chain fragment of Dictyostelium myosin II.";
RL   FEBS Lett. 269:239-243(1990).
RN   [5]
RP   PHOSPHORYLATION AT THR-1823; THR-1833 AND THR-2029.
RX   PubMed=2828113; DOI=10.1016/0014-5793(88)81416-9;
RA   Wagle G., Noegel A., Scheel J., Gerisch G.;
RT   "Phosphorylation of threonine residues on cloned fragments of the
RT   Dictyostelium myosin heavy chain.";
RL   FEBS Lett. 227:71-75(1988).
RN   [6]
RP   NOMENCLATURE.
RX   PubMed=16857047; DOI=10.1186/1471-2164-7-183;
RA   Kollmar M.;
RT   "Thirteen is enough: the myosins of Dictyostelium discoideum and their
RT   light chains.";
RL   BMC Genomics 7:183-183(2006).
RN   [7]
RP   INTERACTION WITH ELMOA.
RX   PubMed=18854143; DOI=10.1016/j.devcel.2008.08.006;
RA   Isik N., Brzostowski J.A., Jin T.;
RT   "An Elmo-like protein associated with myosin II restricts spurious F-actin
RT   events to coordinate phagocytosis and chemotaxis.";
RL   Dev. Cell 15:590-602(2008).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-762.
RX   PubMed=7619795; DOI=10.1021/bi00028a004;
RA   Fisher A.J., Smith C.A., Thoden J.B., Smith R., Sutoh K., Holden H.M.,
RA   Rayment I.;
RT   "X-ray structures of the myosin motor domain of Dictyostelium discoideum
RT   complexed with MgADP.BeFx and MgADP.AlF4-.";
RL   Biochemistry 34:8960-8972(1995).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-762.
RX   PubMed=7619796; DOI=10.1021/bi00028a005;
RA   Smith C.A., Rayment I.;
RT   "X-ray structure of the magnesium(II)-pyrophosphate complex of the
RT   truncated head of Dictyostelium discoideum myosin to 2.7-A resolution.";
RL   Biochemistry 34:8973-8981(1995).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-762.
RX   PubMed=8611530; DOI=10.1021/bi952633+;
RA   Smith C.A., Rayment I.;
RT   "X-ray structure of the magnesium(II).ADP.vanadate complex of the
RT   Dictyostelium discoideum myosin motor domain to 1.9-A resolution.";
RL   Biochemistry 35:5404-5417(1996).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-762.
RX   PubMed=9305951; DOI=10.1021/bi9712596;
RA   Gulick A.M., Bauer C.B., Thoden J.B., Rayment I.;
RT   "X-ray structures of the MgADP, MgATPgammaS, and MgAMPPNP complexes of the
RT   Dictyostelium discoideum myosin motor domain.";
RL   Biochemistry 36:11619-11628(1997).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-762.
RX   PubMed=9405148; DOI=10.1006/jmbi.1997.1325;
RA   Bauer C.B., Kuhlman P.A., Bagshaw C.R., Rayment I.;
RT   "X-ray crystal structure and solution fluorescence characterization of
RT   Mg.2'(3')-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium
RT   discoideum myosin motor domain.";
RL   J. Mol. Biol. 274:394-407(1997).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-761.
RX   PubMed=11226153; DOI=10.1093/emboj/20.1.40;
RA   Kliche W., Fujita-Becker S., Kollmar M., Manstein D.J., Kull F.J.;
RT   "Structure of a genetically engineered molecular motor.";
RL   EMBO J. 20:40-46(2001).
CC   -!- FUNCTION: Myosin is a protein that binds to actin and has ATPase
CC       activity that is activated by actin.
CC   -!- SUBUNIT: Myosin-2 heavy chain is two-headed. It self-assembles into
CC       filaments. Hexamer of 2 heavy chain subunits (MHC), 2 alkali light
CC       chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2).
CC       Associates with elmoA.
CC   -!- INTERACTION:
CC       P08799; Q54YW1: elmoA; NbExp=2; IntAct=EBI-2928504, EBI-2928498;
CC       P08799; P08799: mhcA; NbExp=4; IntAct=EBI-2928504, EBI-2928504;
CC       P08799; P68135: ACTA1; Xeno; NbExp=8; IntAct=EBI-2928504, EBI-367540;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Note=Highest
CC       concentration in the posterior cell cortex.
CC   -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
CC       meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
CC       cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment
CC       (S2). {ECO:0000305}.
CC   -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC       of a 28-residue repeat pattern composed of 4 heptapeptides,
CC       characteristic for alpha-helical coiled coils.
CC   -!- PTM: Phosphorylation inhibits thick filament formation and reduces the
CC       actin-activated ATPase activity. {ECO:0000269|PubMed:2387408,
CC       ECO:0000269|PubMed:2828113}.
CC   -!- MISCELLANEOUS: Dictyostelium myosin-2 has no K(2)EDTA ATPase activity,
CC       perhaps correlated with the absence of a Cys at the SH-1 position
CC       (688).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
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DR   EMBL; M14628; AAA33227.1; -; Genomic_DNA.
DR   EMBL; AAFI02000085; EAL64202.1; -; Genomic_DNA.
DR   PIR; A26655; A26655.
DR   RefSeq; XP_637740.1; XM_632648.1.
DR   PDB; 1D0X; X-ray; 2.00 A; A=1-759.
DR   PDB; 1D0Y; X-ray; 2.00 A; A=1-759.
DR   PDB; 1D0Z; X-ray; 2.00 A; A=1-759.
DR   PDB; 1D1A; X-ray; 2.00 A; A=1-759.
DR   PDB; 1D1B; X-ray; 2.00 A; A=1-759.
DR   PDB; 1D1C; X-ray; 2.30 A; A=1-759.
DR   PDB; 1FMV; X-ray; 2.10 A; A=1-759.
DR   PDB; 1FMW; X-ray; 2.15 A; A=1-759.
DR   PDB; 1G8X; X-ray; 2.80 A; A/B=1-761.
DR   PDB; 1JWY; X-ray; 2.30 A; A=3-765.
DR   PDB; 1JX2; X-ray; 2.30 A; A=3-765.
DR   PDB; 1LVK; X-ray; 1.90 A; A=1-759.
DR   PDB; 1MMA; X-ray; 2.10 A; A=1-759.
DR   PDB; 1MMD; X-ray; 2.00 A; A=1-759.
DR   PDB; 1MMG; X-ray; 2.10 A; A=1-759.
DR   PDB; 1MMN; X-ray; 2.10 A; A=1-759.
DR   PDB; 1MND; X-ray; 2.60 A; A=1-759.
DR   PDB; 1MNE; X-ray; 2.70 A; A=1-759.
DR   PDB; 1VOM; X-ray; 1.90 A; A=1-759.
DR   PDB; 1W9I; X-ray; 1.75 A; A=1-759.
DR   PDB; 1W9J; X-ray; 2.00 A; A=1-758.
DR   PDB; 1W9K; X-ray; 2.05 A; A=1-759.
DR   PDB; 1W9L; X-ray; 1.95 A; A=1-759.
DR   PDB; 1YV3; X-ray; 2.00 A; A=1-762.
DR   PDB; 2AKA; X-ray; 1.90 A; A=2-765.
DR   PDB; 2JHR; X-ray; 2.80 A; A=2-761.
DR   PDB; 2JJ9; X-ray; 2.30 A; A=2-761.
DR   PDB; 2X9H; X-ray; 2.70 A; A=3-696.
DR   PDB; 2XEL; X-ray; 2.50 A; A=2-761.
DR   PDB; 2XO8; X-ray; 2.40 A; A=3-761.
DR   PDB; 2Y0R; X-ray; 2.85 A; X=2-759.
DR   PDB; 2Y8I; X-ray; 3.13 A; X=2-759.
DR   PDB; 2Y9E; X-ray; 3.40 A; X=2-759.
DR   PDB; 3BZ7; X-ray; 2.00 A; A=2-759.
DR   PDB; 3BZ8; X-ray; 2.20 A; A=2-759.
DR   PDB; 3BZ9; X-ray; 2.10 A; A=2-759.
DR   PDB; 3MJX; X-ray; 2.20 A; A=2-761.
DR   PDB; 3MKD; X-ray; 2.40 A; A=2-693.
DR   PDB; 3MNQ; X-ray; 2.20 A; A=3-761.
DR   PDB; 3MYH; X-ray; 2.01 A; X=2-759.
DR   PDB; 3MYK; X-ray; 1.84 A; X=2-759.
DR   PDB; 3MYL; X-ray; 2.00 A; X=2-759.
DR   PDB; 4AE3; X-ray; 2.50 A; A=2-761.
DR   PDB; 4PJK; X-ray; 2.15 A; A=1-761.
DR   PDB; 6Z2S; X-ray; 3.20 A; A=2-761.
DR   PDB; 6Z7T; X-ray; 1.88 A; A/B=2-761.
DR   PDB; 6Z7U; X-ray; 2.58 A; A=2-761.
DR   PDB; 7B1A; X-ray; 2.60 A; A=2-761.
DR   PDBsum; 1D0X; -.
DR   PDBsum; 1D0Y; -.
DR   PDBsum; 1D0Z; -.
DR   PDBsum; 1D1A; -.
DR   PDBsum; 1D1B; -.
DR   PDBsum; 1D1C; -.
DR   PDBsum; 1FMV; -.
DR   PDBsum; 1FMW; -.
DR   PDBsum; 1G8X; -.
DR   PDBsum; 1JWY; -.
DR   PDBsum; 1JX2; -.
DR   PDBsum; 1LVK; -.
DR   PDBsum; 1MMA; -.
DR   PDBsum; 1MMD; -.
DR   PDBsum; 1MMG; -.
DR   PDBsum; 1MMN; -.
DR   PDBsum; 1MND; -.
DR   PDBsum; 1MNE; -.
DR   PDBsum; 1VOM; -.
DR   PDBsum; 1W9I; -.
DR   PDBsum; 1W9J; -.
DR   PDBsum; 1W9K; -.
DR   PDBsum; 1W9L; -.
DR   PDBsum; 1YV3; -.
DR   PDBsum; 2AKA; -.
DR   PDBsum; 2JHR; -.
DR   PDBsum; 2JJ9; -.
DR   PDBsum; 2X9H; -.
DR   PDBsum; 2XEL; -.
DR   PDBsum; 2XO8; -.
DR   PDBsum; 2Y0R; -.
DR   PDBsum; 2Y8I; -.
DR   PDBsum; 2Y9E; -.
DR   PDBsum; 3BZ7; -.
DR   PDBsum; 3BZ8; -.
DR   PDBsum; 3BZ9; -.
DR   PDBsum; 3MJX; -.
DR   PDBsum; 3MKD; -.
DR   PDBsum; 3MNQ; -.
DR   PDBsum; 3MYH; -.
DR   PDBsum; 3MYK; -.
DR   PDBsum; 3MYL; -.
DR   PDBsum; 4AE3; -.
DR   PDBsum; 4PJK; -.
DR   PDBsum; 6Z2S; -.
DR   PDBsum; 6Z7T; -.
DR   PDBsum; 6Z7U; -.
DR   PDBsum; 7B1A; -.
DR   AlphaFoldDB; P08799; -.
DR   EMDB; EMD-8164; -.
DR   SMR; P08799; -.
DR   DIP; DIP-46078N; -.
DR   IntAct; P08799; 2.
DR   STRING; 44689.P08799; -.
DR   BindingDB; P08799; -.
DR   ChEMBL; CHEMBL4295703; -.
DR   iPTMnet; P08799; -.
DR   MetOSite; P08799; -.
DR   PaxDb; 44689-DDB0191444; -.
DR   ABCD; P08799; 2 sequenced antibodies.
DR   EnsemblProtists; EAL64202; EAL64202; DDB_G0286355.
DR   GeneID; 8625606; -.
DR   KEGG; ddi:DDB_G0286355; -.
DR   dictyBase; DDB_G0286355; mhcA.
DR   eggNOG; KOG0161; Eukaryota.
DR   HOGENOM; CLU_000192_5_3_1; -.
DR   InParanoid; P08799; -.
DR   OMA; QRAMDIE; -.
DR   PhylomeDB; P08799; -.
DR   BRENDA; 5.6.1.8; 1939.
DR   Reactome; R-DDI-5627123; RHO GTPases activate PAKs.
DR   EvolutionaryTrace; P08799; -.
DR   PRO; PR:P08799; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0042641; C:actomyosin; IDA:dictyBase.
DR   GO; GO:0005826; C:actomyosin contractile ring; IDA:dictyBase.
DR   GO; GO:0045179; C:apical cortex; IDA:dictyBase.
DR   GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR   GO; GO:0031254; C:cell trailing edge; IDA:dictyBase.
DR   GO; GO:0032154; C:cleavage furrow; IDA:dictyBase.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IDA:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:dictyBase.
DR   GO; GO:0005856; C:cytoskeleton; IDA:dictyBase.
DR   GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR   GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR   GO; GO:1990753; C:equatorial cell cortex; IDA:dictyBase.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR   GO; GO:0032982; C:myosin filament; IDA:dictyBase.
DR   GO; GO:0016460; C:myosin II complex; IDA:dictyBase.
DR   GO; GO:0140220; C:pathogen-containing vacuole; HDA:dictyBase.
DR   GO; GO:0097204; C:phagocytic cup base; IDA:dictyBase.
DR   GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR   GO; GO:0001931; C:uropod; IDA:dictyBase.
DR   GO; GO:0071889; F:14-3-3 protein binding; IPI:dictyBase.
DR   GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR   GO; GO:0030554; F:adenyl nucleotide binding; IDA:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IDA:dictyBase.
DR   GO; GO:0030899; F:calcium-dependent ATPase activity; IDA:dictyBase.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IDA:dictyBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000146; F:microfilament motor activity; IDA:dictyBase.
DR   GO; GO:0033275; P:actin-myosin filament sliding; IDA:dictyBase.
DR   GO; GO:0031152; P:aggregation involved in sorocarp development; IEP:dictyBase.
DR   GO; GO:0032060; P:bleb assembly; IMP:dictyBase.
DR   GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR   GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR   GO; GO:0030038; P:contractile actin filament bundle assembly; IMP:dictyBase.
DR   GO; GO:0033298; P:contractile vacuole organization; IMP:dictyBase.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:dictyBase.
DR   GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0060328; P:cytoplasmic actin-based contraction involved in forward cell motility; IMP:dictyBase.
DR   GO; GO:0050982; P:detection of mechanical stimulus; IMP:dictyBase.
DR   GO; GO:0046847; P:filopodium assembly; IMP:dictyBase.
DR   GO; GO:0006971; P:hypotonic response; IMP:dictyBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR   GO; GO:0031034; P:myosin filament assembly; IDA:dictyBase.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:dictyBase.
DR   GO; GO:0008104; P:protein localization; IMP:dictyBase.
DR   GO; GO:0031270; P:pseudopodium retraction; IMP:dictyBase.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:dictyBase.
DR   GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
DR   GO; GO:1903013; P:response to differentiation-inducing factor 1; HDA:dictyBase.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IDA:dictyBase.
DR   GO; GO:0009612; P:response to mechanical stimulus; IMP:dictyBase.
DR   GO; GO:0034461; P:uropod retraction; IMP:dictyBase.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 6.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 2.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 11.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
KW   Cytoplasm; Methylation; Motor protein; Myosin; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..2116
FT                   /note="Myosin-2 heavy chain"
FT                   /id="PRO_0000123373"
FT   DOMAIN          30..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          86..759
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          762..791
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          638..660
FT                   /note="Actin-binding"
FT   REGION          738..752
FT                   /note="Actin-binding"
FT   REGION          1295..1314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1363..1399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1415..1444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1711..1731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1771..1791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1805..1844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          817..2116
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1415..1443
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1805..1831
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   MOD_RES         130
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1823
FT                   /note="Phosphothreonine; by MHCK"
FT                   /evidence="ECO:0000269|PubMed:2387408,
FT                   ECO:0000269|PubMed:2828113"
FT   MOD_RES         1833
FT                   /note="Phosphothreonine; by MHCK"
FT                   /evidence="ECO:0000269|PubMed:2387408,
FT                   ECO:0000269|PubMed:2828113"
FT   MOD_RES         2029
FT                   /note="Phosphothreonine; by MHCK"
FT                   /evidence="ECO:0000269|PubMed:2387408,
FT                   ECO:0000269|PubMed:2828113"
FT   CONFLICT        249
FT                   /note="S -> N (in Ref. 1; AAA33227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="C -> Y (in Ref. 1; AAA33227)"
FT                   /evidence="ECO:0000305"
FT   TURN            3..5
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:2Y8I"
FT   HELIX           10..15
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           22..28
FT                   /evidence="ECO:0007829|PDB:3MYK"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:6Z7T"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:1D1A"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:2Y9E"
FT   STRAND          48..55
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          57..63
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:1LVK"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:2Y8I"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           99..111
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          122..126
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           137..143
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           155..169
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          173..178
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           185..200
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:3MNQ"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:3MNQ"
FT   HELIX           210..226
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:1W9L"
FT   STRAND          236..247
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          249..251
FT                   /evidence="ECO:0007829|PDB:2XO8"
FT   STRAND          253..261
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           265..268
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           279..287
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           290..296
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           301..303
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   TURN            305..307
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          308..311
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           320..334
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           338..355
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          359..361
FT                   /evidence="ECO:0007829|PDB:1VOM"
FT   STRAND          363..368
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           373..382
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           386..394
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          397..400
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          403..406
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           411..441
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          447..454
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          462..464
FT                   /evidence="ECO:0007829|PDB:6Z7T"
FT   HELIX           466..495
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   TURN            496..498
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           506..510
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           511..518
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   TURN            520..523
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           525..533
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          534..537
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           540..551
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   TURN            552..554
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          556..559
FT                   /evidence="ECO:0007829|PDB:2Y9E"
FT   STRAND          565..572
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          575..580
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           584..589
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           594..601
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           608..613
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           615..618
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          624..626
FT                   /evidence="ECO:0007829|PDB:2AKA"
FT   HELIX           630..646
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          648..656
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           669..678
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           681..687
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           688..690
FT                   /evidence="ECO:0007829|PDB:2Y0R"
FT   STRAND          694..698
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   HELIX           699..701
FT                   /evidence="ECO:0007829|PDB:3MNQ"
FT   TURN            702..704
FT                   /evidence="ECO:0007829|PDB:4AE3"
FT   HELIX           706..708
FT                   /evidence="ECO:0007829|PDB:6Z7T"
FT   STRAND          709..711
FT                   /evidence="ECO:0007829|PDB:1D0Y"
FT   HELIX           719..729
FT                   /evidence="ECO:0007829|PDB:6Z7T"
FT   STRAND          730..732
FT                   /evidence="ECO:0007829|PDB:2Y9E"
FT   HELIX           734..736
FT                   /evidence="ECO:0007829|PDB:6Z7T"
FT   STRAND          737..739
FT                   /evidence="ECO:0007829|PDB:3MYK"
FT   STRAND          741..746
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   TURN            748..752
FT                   /evidence="ECO:0007829|PDB:1W9I"
FT   STRAND          754..756
FT                   /evidence="ECO:0007829|PDB:1MMA"
FT   STRAND          757..760
FT                   /evidence="ECO:0007829|PDB:2XO8"
SQ   SEQUENCE   2116 AA;  243786 MW;  97DE4FB422AD3D56 CRC64;
     MNPIHDRTSD YHKYLKVKQG DSDLFKLTVS DKRYIWYNPD PKERDSYECG EIVSETSDSF
     TFKTVDGQDR QVKKDDANQR NPIKFDGVED MSELSYLNEP AVFHNLRVRY NQDLIYTYSG
     LFLVAVNPFK RIPIYTQEMV DIFKGRRRNE VAPHIFAISD VAYRSMLDDR QNQSLLITGE
     SGAGKTENTK KVIQYLASVA GRNQANGSGV LEQQILQANP ILEAFGNAKT TRNNNSSRFG
     KFIEIQFNSA GFISGASIQS YLLEKSRVVF QSETERNYHI FYQLLAGATA EEKKALHLAG
     PESFNYLNQS GCVDIKGVSD SEEFKITRQA MDIVGFSQEE QMSIFKIIAG ILHLGNIKFE
     KGAGEGAVLK DKTALNAAST VFGVNPSVLE KALMEPRILA GRDLVAQHLN VEKSSSSRDA
     LVKALYGRLF LWLVKKINNV LCQERKAYFI GVLDISGFEI FKVNSFEQLC INYTNEKLQQ
     FFNHHMFKLE QEEYLKEKIN WTFIDFGLDS QATIDLIDGR QPPGILALLD EQSVFPNATD
     NTLITKLHSH FSKKNAKYEE PRFSKTEFGV THYAGQVMYE IQDWLEKNKD PLQQDLELCF
     KDSSDNVVTK LFNDPNIASR AKKGANFITV AAQYKEQLAS LMATLETTNP HFVRCIIPNN
     KQLPAKLEDK VVLDQLRCNG VLEGIRITRK GFPNRIIYAD FVKRYYLLAP NVPRDAEDSQ
     KATDAVLKHL NIDPEQYRFG ITKIFFRAGQ LARIEEAREQ RISEIIKAIQ AATRGWIARK
     VYKQAREHTV AARIIQQNLR AYIDFKSWPW WKLFSKARPL LKRRNFEKEI KEKEREILEL
     KSNLTDSTTQ KDKLEKSLKD TESNVLDLQR QLKAEKETLK AMYDSKDALE AQKRELEIRV
     EDMESELDEK KLALENLQNQ KRSVEEKVRD LEEELQEEQK LRNTLEKLKK KYEEELEEMK
     RVNDGQSDTI SRLEKIKDEL QKEVEELTES FSEESKDKGV LEKTRVRLQS ELDDLTVRLD
     SETKDKSELL RQKKKLEEEL KQVQEALAAE TAAKLAQEAA NKKLQGEYTE LNEKFNSEVT
     ARSNVEKSKK TLESQLVAVN NELDEEKKNR DALEKKKKAL DAMLEEMKDQ LESTGGEKKS
     LYDLKVKQES DMEALRNQIS ELQSTIAKLE KIKSTLEGEV ARLQGELEAE QLAKSNVEKQ
     KKKVELDLED KSAQLAEETA AKQALDKLKK KLEQELSEVQ TQLSEANNKN VNSDSTNKHL
     ETSFNNLKLE LEAEQKAKQA LEKKRLGLES ELKHVNEQLE EEKKQKESNE KRKVDLEKEV
     SELKDQIEEE VASKKAVTEA KNKKESELDE IKRQYADVVS SRDKSVEQLK TLQAKNEELR
     NTAEEAEGQL DRAERSKKKA EFDLEEAVKN LEEETAKKVK AEKAMKKAET DYRSTKSELD
     DAKNVSSEQY VQIKRLNEEL SELRSVLEEA DERCNSAIKA KKTAESALES LKDEIDAANN
     AKAKAERKSK ELEVRVAELE ESLEDKSGTV NVEFIRKKDA EIDDLRARLD RETESRIKSD
     EDKKNTRKQF ADLEAKVEEA QREVVTIDRL KKKLESDIID LSTQLDTETK SRIKIEKSKK
     KLEQTLAERR AAEEGSSKAA DEEIRKQVWQ EVDELRAQLD SERAALNASE KKIKSLVAEV
     DEVKEQLEDE ILAKDKLVKA KRALEVELEE VRDQLEEEED SRSELEDSKR RLTTEVEDIK
     KKYDAEVEQN TKLDEAKKKL TDDVDTLKKQ LEDEKKKLNE SERAKKRLES ENEDFLAKLD
     AEVKNRSRAE KDRKKYEKDL KDTKYKLNDE AATKTQTEIG AAKLEDQIDE LRSKLEQEQA
     KATQADKSKK TLEGEIDNLR AQIEDEGKIK MRLEKEKRAL EGELEELRET VEEAEDSKSE
     AEQSKRLVEL ELEDARRNLQ KEIDAKEIAE DAKSNLQREI VEAKGRLEEE SIARTNSDRS
     RKRLEAEIDA LTAQVDAEQK AKNQQIKENK KIETELKEYR KKFGESEKTK TKEFLVVEKL
     ETDYKRAKKE AADEQQQRLT VENDLRKHLS EISLLKDAID KLQRDHDKTK RELETETASK
     IEMQRKMADF FGGFKA
//