MYS2_DICDI
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 03-AUG-2022, entry version 194.
DE RecName: Full=Myosin-2 heavy chain;
DE AltName: Full=Myosin II heavy chain;
GN Name=mhcA; ORFNames=DDB_G0286355;
OS Dictyostelium discoideum (Slime mold).
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 SMR; P08799; -.
DR DIP; DIP-46078N; -.
DR IntAct; P08799; 2.
DR STRING; 44689.DDB0191444; -.
DR BindingDB; P08799; -.
DR ChEMBL; CHEMBL4295703; -.
DR iPTMnet; P08799; -.
DR MetOSite; P08799; -.
DR PaxDb; P08799; -.
DR PRIDE; P08799; -.
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; NAHNEAQ; -.
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: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: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 Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 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 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; SSF52540; SSF52540; 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
