P08799 (MYS2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myosin-2 heavy chain

Alternative name(s):
Myosin II heavy chain

Gene names

Name:	mhcA
ORF Names:	DDB_G0286355

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	2116 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.
Subunit structure	Myosin-2 heavy chain is two-headed. It self-assembles into filaments. Hexamer of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Associates with elmoA.
Subcellular location	Cytoplasm › cell cortex. Note: Highest concentration in the posterior cell cortex.
Domain	Each myosin heavy chain can be split into 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). It can be further split into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.
Post-translational modification	Phosphorylation inhibits thick filament formation and reduces the actin-activated ATPase activity.
Miscellaneous	Dictyostelium myosin-2 has no K2EDTA ATPase activity, perhaps correlated with the absence of a Cys at the SH-1 position (688).
Sequence similarities	Contains 1 IQ domain. Contains 1 myosin head-like domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Coiled coil
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Motor protein Myosin
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin-myosin filament sliding Inferred from direct assay PubMed 16901894PubMed 19955408. Source: dictyBase bleb assembly Inferred from mutant phenotype PubMed 16624291PubMed 16926192. Source: dictyBase chemotaxis Inferred from mutant phenotype PubMed 16926192. Source: dictyBase contractile actin filament bundle assembly Inferred from mutant phenotype PubMed 15894626. Source: dictyBase cortical actin cytoskeleton organization Inferred from direct assay PubMed 16461463. Source: dictyBase culmination involved in sorocarp development Inferred from mutant phenotype PubMed 2721503PubMed 3576222. Source: dictyBase cytokinesis Inferred from mutant phenotype PubMed 10588668PubMed 2721503PubMed 3576222. Source: dictyBase cytoplasmic actin-based contraction involved in forward cell motility Inferred from mutant phenotype PubMed 18388319. Source: dictyBase filopodium assembly Inferred from mutant phenotype PubMed 15855234. Source: dictyBase myosin filament assembly Inferred from direct assay PubMed 4278009. Source: dictyBase negative regulation of actin filament polymerization Inferred from mutant phenotype PubMed 15894626. Source: dictyBase protein localization Inferred from mutant phenotype PubMed 16339076. Source: dictyBase pseudopodium retraction Inferred from mutant phenotype PubMed 18388319. Source: dictyBase uropod retraction Inferred from mutant phenotype PubMed 18388319. Source: dictyBase
Cellular_component	actomyosin Inferred from direct assay PubMed 4278009. Source: dictyBase actomyosin contractile ring Inferred from direct assay PubMed 9238018. Source: dictyBase apical cortex Inferred from direct assay PubMed 22902739. Source: dictyBase cytosol Inferred from direct assay PubMed 23132928. Source: dictyBase early phagosome Inferred from direct assay PubMed 20200225. Source: dictyBase myosin II complex Inferred from direct assay PubMed 4278009. Source: dictyBase myosin filament Inferred from direct assay PubMed 4278009. Source: dictyBase uropod Inferred from direct assay PubMed 17126332. Source: dictyBase
Molecular_function	ATP binding Inferred from direct assay PubMed 16982629PubMed 4278009. Source: dictyBase actin filament binding Inferred from direct assay PubMed 16982629PubMed 18067324. Source: dictyBase actin-dependent ATPase activity Inferred from direct assay PubMed 16982629PubMed 18067324PubMed 19955408PubMed 4278009. Source: dictyBase microfilament motor activity Inferred from direct assay PubMed 16982629PubMed 19955408. Source: dictyBase protein homodimerization activity Inferred from direct assay PubMed 2745547. Source: dictyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
elmoA	Q54YW1	2	EBI-2928504,EBI-2928498

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2116

2116

Myosin-2 heavy chain

PRO_0000123373

Regions

Domain

1 – 761

761

Myosin head-like

Domain

762 – 791

30

IQ

Nucleotide binding

179 – 186

8

ATP

Region

638 – 660

23

Actin-binding

Region

738 – 752

15

Actin-binding

Coiled coil

817 – 2116

1300

Potential

Amino acid modifications

Modified residue

130

1

N6,N6-dimethyllysine Potential

Modified residue

1823

1

Phosphothreonine; by MHCK Ref.4 Ref.5

Modified residue

1833

1

Phosphothreonine; by MHCK Ref.4 Ref.5

Modified residue

2029

1

Phosphothreonine; by MHCK Ref.4 Ref.5

Experimental info

Sequence conflict

249

1

S → N in AAA33227. Ref.1

Sequence conflict

312

1

C → Y in AAA33227. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2116

Helix Strand Turn

Details...

Turn

3 – 5

3

Beta strand

6 – 9

4

Helix

10 – 15

6

Helix

22 – 28

7

Beta strand

34 – 37

4

Beta strand

39 – 43

5

Beta strand

44 – 46

3

Beta strand

48 – 55

8

Beta strand

57 – 63

7

Beta strand

65 – 67

3

Beta strand

69 – 73

5

Turn

74 – 76

3

Beta strand

77 – 79

3

Helix

83 – 85

3

Helix

91 – 93

3

Helix

99 – 111

13

Beta strand

116 – 119

4

Beta strand

122 – 126

5

Helix

137 – 143

7

Helix

148 – 150

3

Helix

155 – 169

15

Beta strand

173 – 178

6

Helix

185 – 200

16

Beta strand

204 – 206

3

Helix

207 – 209

3

Helix

210 – 226

17

Beta strand

227 – 230

4

Beta strand

236 – 247

12

Beta strand

249 – 251

3

Beta strand

253 – 261

9

Helix

265 – 268

4

Helix

279 – 287

9

Helix

290 – 296

7

Helix

301 – 303

3

Turn

305 – 307

3

Beta strand

308 – 311

4

Helix

320 – 334

15

Helix

338 – 355

18

Beta strand

359 – 361

3

Beta strand

363 – 368

6

Helix

373 – 382

10

Helix

386 – 394

9

Beta strand

397 – 400

4

Beta strand

403 – 406

4

Helix

411 – 441

31

Beta strand

447 – 454

8

Beta strand

462 – 464

3

Helix

466 – 495

30

Turn

496 – 498

3

Helix

506 – 510

5

Helix

511 – 518

8

Turn

520 – 523

4

Helix

525 – 533

9

Beta strand

534 – 537

4

Helix

540 – 551

12

Turn

552 – 554

3

Beta strand

556 – 559

4

Beta strand

565 – 572

8

Beta strand

575 – 580

6

Helix

584 – 589

6

Helix

594 – 601

8

Helix

608 – 613

6

Helix

615 – 618

4

Beta strand

624 – 626

3

Helix

630 – 646

17

Beta strand

648 – 656

9

Helix

669 – 678

10

Helix

681 – 687

7

Helix

688 – 690

3

Beta strand

694 – 698

5

Helix

699 – 701

3

Turn

702 – 704

3

Helix

706 – 708

3

Beta strand

709 – 711

3

Helix

719 – 730

12

Helix

734 – 736

3

Beta strand

737 – 739

3

Beta strand

741 – 746

6

Turn

748 – 752

5

Beta strand

754 – 756

3

Beta strand

757 – 760

4

Sequences

	Sequence		Length	Mass (Da)
	P08799 [UniParc]. Last modified March 20, 2007. Version 3. Checksum: 97DE4FB422AD3D56	FASTA	2,116	243,786
	10 20 30 40 50 60 MNPIHDRTSD YHKYLKVKQG DSDLFKLTVS DKRYIWYNPD PKERDSYECG EIVSETSDSF 70 80 90 100 110 120 TFKTVDGQDR QVKKDDANQR NPIKFDGVED MSELSYLNEP AVFHNLRVRY NQDLIYTYSG 130 140 150 160 170 180 LFLVAVNPFK RIPIYTQEMV DIFKGRRRNE VAPHIFAISD VAYRSMLDDR QNQSLLITGE 190 200 210 220 230 240 SGAGKTENTK KVIQYLASVA GRNQANGSGV LEQQILQANP ILEAFGNAKT TRNNNSSRFG 250 260 270 280 290 300 KFIEIQFNSA GFISGASIQS YLLEKSRVVF QSETERNYHI FYQLLAGATA EEKKALHLAG 310 320 330 340 350 360 PESFNYLNQS GCVDIKGVSD SEEFKITRQA MDIVGFSQEE QMSIFKIIAG ILHLGNIKFE 370 380 390 400 410 420 KGAGEGAVLK DKTALNAAST VFGVNPSVLE KALMEPRILA GRDLVAQHLN VEKSSSSRDA 430 440 450 460 470 480 LVKALYGRLF LWLVKKINNV LCQERKAYFI GVLDISGFEI FKVNSFEQLC INYTNEKLQQ 490 500 510 520 530 540 FFNHHMFKLE QEEYLKEKIN WTFIDFGLDS QATIDLIDGR QPPGILALLD EQSVFPNATD 550 560 570 580 590 600 NTLITKLHSH FSKKNAKYEE PRFSKTEFGV THYAGQVMYE IQDWLEKNKD PLQQDLELCF 610 620 630 640 650 660 KDSSDNVVTK LFNDPNIASR AKKGANFITV AAQYKEQLAS LMATLETTNP HFVRCIIPNN 670 680 690 700 710 720 KQLPAKLEDK VVLDQLRCNG VLEGIRITRK GFPNRIIYAD FVKRYYLLAP NVPRDAEDSQ 730 740 750 760 770 780 KATDAVLKHL NIDPEQYRFG ITKIFFRAGQ LARIEEAREQ RISEIIKAIQ AATRGWIARK 790 800 810 820 830 840 VYKQAREHTV AARIIQQNLR AYIDFKSWPW WKLFSKARPL LKRRNFEKEI KEKEREILEL 850 860 870 880 890 900 KSNLTDSTTQ KDKLEKSLKD TESNVLDLQR QLKAEKETLK AMYDSKDALE AQKRELEIRV 910 920 930 940 950 960 EDMESELDEK KLALENLQNQ KRSVEEKVRD LEEELQEEQK LRNTLEKLKK KYEEELEEMK 970 980 990 1000 1010 1020 RVNDGQSDTI SRLEKIKDEL QKEVEELTES FSEESKDKGV LEKTRVRLQS ELDDLTVRLD 1030 1040 1050 1060 1070 1080 SETKDKSELL RQKKKLEEEL KQVQEALAAE TAAKLAQEAA NKKLQGEYTE LNEKFNSEVT 1090 1100 1110 1120 1130 1140 ARSNVEKSKK TLESQLVAVN NELDEEKKNR DALEKKKKAL DAMLEEMKDQ LESTGGEKKS 1150 1160 1170 1180 1190 1200 LYDLKVKQES DMEALRNQIS ELQSTIAKLE KIKSTLEGEV ARLQGELEAE QLAKSNVEKQ 1210 1220 1230 1240 1250 1260 KKKVELDLED KSAQLAEETA AKQALDKLKK KLEQELSEVQ TQLSEANNKN VNSDSTNKHL 1270 1280 1290 1300 1310 1320 ETSFNNLKLE LEAEQKAKQA LEKKRLGLES ELKHVNEQLE EEKKQKESNE KRKVDLEKEV 1330 1340 1350 1360 1370 1380 SELKDQIEEE VASKKAVTEA KNKKESELDE IKRQYADVVS SRDKSVEQLK TLQAKNEELR 1390 1400 1410 1420 1430 1440 NTAEEAEGQL DRAERSKKKA EFDLEEAVKN LEEETAKKVK AEKAMKKAET DYRSTKSELD 1450 1460 1470 1480 1490 1500 DAKNVSSEQY VQIKRLNEEL SELRSVLEEA DERCNSAIKA KKTAESALES LKDEIDAANN 1510 1520 1530 1540 1550 1560 AKAKAERKSK ELEVRVAELE ESLEDKSGTV NVEFIRKKDA EIDDLRARLD RETESRIKSD 1570 1580 1590 1600 1610 1620 EDKKNTRKQF ADLEAKVEEA QREVVTIDRL KKKLESDIID LSTQLDTETK SRIKIEKSKK 1630 1640 1650 1660 1670 1680 KLEQTLAERR AAEEGSSKAA DEEIRKQVWQ EVDELRAQLD SERAALNASE KKIKSLVAEV 1690 1700 1710 1720 1730 1740 DEVKEQLEDE ILAKDKLVKA KRALEVELEE VRDQLEEEED SRSELEDSKR RLTTEVEDIK 1750 1760 1770 1780 1790 1800 KKYDAEVEQN TKLDEAKKKL TDDVDTLKKQ LEDEKKKLNE SERAKKRLES ENEDFLAKLD 1810 1820 1830 1840 1850 1860 AEVKNRSRAE KDRKKYEKDL KDTKYKLNDE AATKTQTEIG AAKLEDQIDE LRSKLEQEQA 1870 1880 1890 1900 1910 1920 KATQADKSKK TLEGEIDNLR AQIEDEGKIK MRLEKEKRAL EGELEELRET VEEAEDSKSE 1930 1940 1950 1960 1970 1980 AEQSKRLVEL ELEDARRNLQ KEIDAKEIAE DAKSNLQREI VEAKGRLEEE SIARTNSDRS 1990 2000 2010 2020 2030 2040 RKRLEAEIDA LTAQVDAEQK AKNQQIKENK KIETELKEYR KKFGESEKTK TKEFLVVEKL 2050 2060 2070 2080 2090 2100 ETDYKRAKKE AADEQQQRLT VENDLRKHLS EISLLKDAID KLQRDHDKTK RELETETASK 2110 IEMQRKMADF FGGFKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conserved protein domains in a myosin heavy chain gene from Dictyostelium discoideum." Warrick H.M., de Lozanne A., Leinwand L.A., Spudich J.A. Proc. Natl. Acad. Sci. U.S.A. 83:9433-9437(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"Cloning and characterization of a nonmuscle myosin heavy chain cDNA." De Lozanne A., Lewis M., Spudich J.A., Leinwand L.A. Proc. Natl. Acad. Sci. U.S.A. 82:6807-6810(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2035-2116.
[4]	"Replacement of threonine residues by serine and alanine in a phosphorylatable heavy chain fragment of Dictyostelium myosin II." Lueck-Vielmeter D., Schleicher M., Grabatin B., Wippler J., Gerisch G. FEBS Lett. 269:239-243(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-1823; THR-1833 AND THR-2029, MUTAGENESIS. Strain: AX2.
[5]	"Phosphorylation of threonine residues on cloned fragments of the Dictyostelium myosin heavy chain." Wagle G., Noegel A., Scheel J., Gerisch G. FEBS Lett. 227:71-75(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-1823; THR-1833 AND THR-2029.
[6]	"Thirteen is enough: the myosins of Dictyostelium discoideum and their light chains." Kollmar M. BMC Genomics 7:183-183(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
[7]	"An Elmo-like protein associated with myosin II restricts spurious F-actin events to coordinate phagocytosis and chemotaxis." Isik N., Brzostowski J.A., Jin T. Dev. Cell 15:590-602(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ELMOA.
[8]	"X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-." Fisher A.J., Smith C.A., Thoden J.B., Smith R., Sutoh K., Holden H.M., Rayment I. Biochemistry 34:8960-8972(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-762.
[9]	"X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7-A resolution." Smith C.A., Rayment I. Biochemistry 34:8973-8981(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-762.
[10]	"X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9-A resolution." Smith C.A., Rayment I. Biochemistry 35:5404-5417(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-762.
[11]	"X-ray structures of the MgADP, MgATPgammaS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain." Gulick A.M., Bauer C.B., Thoden J.B., Rayment I. Biochemistry 36:11619-11628(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-762.
[12]	"X-ray crystal structure and solution fluorescence characterization of Mg.2'(3')-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain." Bauer C.B., Kuhlman P.A., Bagshaw C.R., Rayment I. J. Mol. Biol. 274:394-407(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-762.
[13]	"Structure of a genetically engineered molecular motor." Kliche W., Fujita-Becker S., Kollmar M., Manstein D.J., Kull F.J. EMBO J. 20:40-46(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-761.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14628 Genomic DNA. Translation: AAA33227.1.
AAFI02000085 Genomic DNA. Translation: EAL64202.1.

PIR

A26655.

RefSeq

XP_637740.1. XM_632648.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D0X	X-ray	2.00	A	1-759	[»]
1D0Y	X-ray	2.00	A	1-759	[»]
1D0Z	X-ray	2.00	A	1-759	[»]
1D1A	X-ray	2.00	A	1-759	[»]
1D1B	X-ray	2.00	A	1-759	[»]
1D1C	X-ray	2.30	A	1-759	[»]
1FMV	X-ray	2.10	A	1-759	[»]
1FMW	X-ray	2.15	A	1-759	[»]
1G8X	X-ray	2.80	A/B	1-761	[»]
1JWY	X-ray	2.30	A	3-765	[»]
1JX2	X-ray	2.30	A	3-765	[»]
1LVK	X-ray	1.90	A	1-759	[»]
1MMA	X-ray	2.10	A	1-759	[»]
1MMD	X-ray	2.00	A	1-759	[»]
1MMG	X-ray	2.10	A	1-759	[»]
1MMN	X-ray	2.10	A	1-759	[»]
1MND	X-ray	2.60	A	1-759	[»]
1MNE	X-ray	2.70	A	1-759	[»]
1Q5G	model	-	A	2-765	[»]
1VOM	X-ray	1.90	A	1-759	[»]
1W9I	X-ray	1.75	A	1-759	[»]
1W9J	X-ray	2.00	A	1-759	[»]
1W9K	X-ray	2.05	A	3-759	[»]
1W9L	X-ray	1.95	A	1-759	[»]
1YV3	X-ray	2.00	A	2-759	[»]
2AKA	X-ray	1.90	A	2-765	[»]
2JHR	X-ray	2.80	A	2-761	[»]
2JJ9	X-ray	2.30	A	2-761	[»]
2X9H	X-ray	2.70	A	3-696	[»]
2XEL	X-ray	2.50	A	2-761	[»]
2XO8	X-ray	2.40	A	3-761	[»]
2Y0R	X-ray	2.85	X	2-759	[»]
2Y8I	X-ray	3.13	X	2-759	[»]
2Y9E	X-ray	3.40	X	2-759	[»]
3BZ7	X-ray	2.00	A	2-759	[»]
3BZ8	X-ray	2.20	A	2-759	[»]
3BZ9	X-ray	2.10	A	2-759	[»]
3MJX	X-ray	2.20	A	2-761	[»]
3MKD	X-ray	2.40	A	2-693	[»]
3MNQ	X-ray	2.20	A	3-761	[»]
3MYH	X-ray	2.01	X	2-759	[»]
3MYK	X-ray	1.84	X	2-759	[»]
3MYL	X-ray	2.00	X	2-759	[»]
4AE3	X-ray	2.50	A	2-761	[»]

ProteinModelPortal

P08799.

SMR

P08799. Positions 2-821.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46078N.

IntAct

P08799. 1 interaction.

STRING

44689.DDB_0191444.

Proteomic databases

PRIDE

P08799.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblProtists

DDB0191444; DDB0191444; DDB_G0286355.

GeneID

8625606.

KEGG

ddi:DDB_G0286355.

Organism-specific databases

dictyBase

DDB_G0286355. mhcA.

Phylogenomic databases

eggNOG

COG5022.

KO

K10352.

OMA

NTMFILE.

ProtClustDB

CLSZ2430102.

Family and domain databases

Gene3D

4.10.270.10. 1 hit.

InterPro

IPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR008989. Myosin_S1_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]

Pfam

PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 3 hits.
[Graphical view]

PRINTS

PR00193. MYOSINHEAVY.

SMART

SM00015. IQ. 2 hits.
SM00242. MYSc. 1 hit.
[Graphical view]

SUPFAM

SSF50084. Myosin_S1_N. 1 hit.
SSF52540. SSF52540. 1 hit.

PROSITE

PS50096. IQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P08799.

Entry information

Entry name

MYS2_DICDI

Accession

Primary (citable) accession number: P08799
Secondary accession number(s): Q54LU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	March 20, 2007
Last modified:	May 29, 2013
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)