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P08799 (MYS2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin-2 heavy chain
Alternative name(s):
Myosin II heavy chain
Gene names
Name:mhcA
ORF Names:DDB_G0286355
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length2116 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasmcell 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

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

Contains 1 IQ domain.

Contains 1 myosin motor domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainCoiled coil
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMMethylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 16982629PubMed 18067324PubMed 19955408PubMed 4278009. Source: GOC

actin-myosin filament sliding

Inferred from direct assay PubMed 16901894PubMed 19955408. Source: dictyBase

bleb assembly

Inferred from mutant phenotype PubMed 16624291PubMed 16926192. Source: dictyBase

cellular component movement

Inferred from mutant phenotype PubMed 15259052. Source: dictyBase

chemotaxis

Inferred from mutant phenotype PubMed 16926192. Source: dictyBase

contractile actin filament bundle assembly

Inferred from mutant phenotype PubMed 15894626. Source: dictyBase

contractile vacuole organization

Inferred from mutant phenotype PubMed 19843280. 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

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

hypotonic response

Inferred from mutant phenotype PubMed 19843280. Source: dictyBase

metabolic process

Inferred from direct assay PubMed 15910751PubMed 16982629PubMed 19955408. Source: GOC

mitotic cytokinesis

Inferred from mutant phenotype PubMed 10588668PubMed 2721503PubMed 3576222. 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_componentactomyosin

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

cell cortex

Inferred from direct assay PubMed 16461463. Source: dictyBase

cell trailing edge

Inferred from direct assay PubMed 22114350. Source: dictyBase

cytoskeleton

Inferred from direct assay PubMed 2578450. 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

phagocytic cup base

Inferred from direct assay PubMed 12952073. Source: dictyBase

uropod

Inferred from direct assay PubMed 17126332. Source: dictyBase

   Molecular_function14-3-3 protein binding

Inferred from physical interaction PubMed 20951045. Source: dictyBase

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

adenyl nucleotide binding

Inferred from direct assay PubMed 14620745. Source: dictyBase

microfilament motor activity

Inferred from direct assay PubMed 16982629PubMed 19955408. Source: dictyBase

motor activity

Inferred from direct assay PubMed 15910751. Source: dictyBase

protein binding

Inferred from physical interaction Ref.7. Source: IntAct

protein homodimerization activity

Inferred from direct assay PubMed 2745547. Source: dictyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

elmoAQ54YW12EBI-2928504,EBI-2928498

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21162116Myosin-2 heavy chain
PRO_0000123373

Regions

Domain86 – 759674Myosin motor
Domain762 – 79130IQ
Nucleotide binding179 – 1868ATP
Region638 – 66023Actin-binding
Region738 – 75215Actin-binding
Coiled coil817 – 21161300 Potential

Amino acid modifications

Modified residue1301N6,N6-dimethyllysine Potential
Modified residue18231Phosphothreonine; by MHCK Ref.4 Ref.5
Modified residue18331Phosphothreonine; by MHCK Ref.4 Ref.5
Modified residue20291Phosphothreonine; by MHCK Ref.4 Ref.5

Experimental info

Sequence conflict2491S → N in AAA33227. Ref.1
Sequence conflict3121C → Y in AAA33227. Ref.1

Secondary structure

................................................................................................................................................ 2116
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08799 [UniParc].

Last modified March 20, 2007. Version 3.
Checksum: 97DE4FB422AD3D56

FASTA2,116243,786
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
PIRA26655.
RefSeqXP_637740.1. XM_632648.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D0XX-ray2.00A1-759[»]
1D0YX-ray2.00A1-759[»]
1D0ZX-ray2.00A1-759[»]
1D1AX-ray2.00A1-759[»]
1D1BX-ray2.00A1-759[»]
1D1CX-ray2.30A1-759[»]
1FMVX-ray2.10A1-759[»]
1FMWX-ray2.15A1-759[»]
1G8XX-ray2.80A/B1-761[»]
1JWYX-ray2.30A3-765[»]
1JX2X-ray2.30A3-765[»]
1LVKX-ray1.90A1-759[»]
1MMAX-ray2.10A1-759[»]
1MMDX-ray2.00A1-759[»]
1MMGX-ray2.10A1-759[»]
1MMNX-ray2.10A1-759[»]
1MNDX-ray2.60A1-759[»]
1MNEX-ray2.70A1-759[»]
1Q5Gmodel-A2-765[»]
1VOMX-ray1.90A1-759[»]
1W9IX-ray1.75A1-754[»]
1W9JX-ray2.00A1-758[»]
1W9KX-ray2.05A1-759[»]
1W9LX-ray1.95A1-759[»]
1YV3X-ray2.00A1-762[»]
2AKAX-ray1.90A2-765[»]
2JHRX-ray2.80A2-761[»]
2JJ9X-ray2.30A2-761[»]
2X9HX-ray2.70A3-696[»]
2XELX-ray2.50A2-761[»]
2XO8X-ray2.40A3-761[»]
2Y0RX-ray2.85X2-759[»]
2Y8IX-ray3.13X2-759[»]
2Y9EX-ray3.40X2-759[»]
3BZ7X-ray2.00A2-759[»]
3BZ8X-ray2.20A2-759[»]
3BZ9X-ray2.10A2-759[»]
3MJXX-ray2.20A2-761[»]
3MKDX-ray2.40A2-693[»]
3MNQX-ray2.20A3-761[»]
3MYHX-ray2.01X2-759[»]
3MYKX-ray1.84X2-759[»]
3MYLX-ray2.00X2-759[»]
4AE3X-ray2.50A2-761[»]
ProteinModelPortalP08799.
SMRP08799. Positions 2-821.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46078N.
IntActP08799. 1 interaction.
STRING44689.DDB_0191444.

Proteomic databases

PRIDEP08799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0191444; DDB0191444; DDB_G0286355.
GeneID8625606.
KEGGddi:DDB_G0286355.

Organism-specific databases

dictyBaseDDB_G0286355. mhcA.

Phylogenomic databases

eggNOGCOG5022.
OMARNEANES.
PhylomeDBP08799.

Family and domain databases

Gene3D4.10.270.10. 1 hit.
InterProIPR000048. 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]
PfamPF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 3 hits.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 2 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08799.

Entry information

Entry nameMYS2_DICDI
AccessionPrimary (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: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase