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Protein

Myosin-2 heavy chain

Gene

mhcA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi179 – 186ATP8

GO - Molecular functioni

  • 14-3-3 protein binding Source: dictyBase
  • actin-dependent ATPase activity Source: dictyBase
  • actin filament binding Source: dictyBase
  • adenyl nucleotide binding Source: dictyBase
  • ATP binding Source: dictyBase
  • microfilament motor activity Source: dictyBase
  • motor activity Source: dictyBase
  • protein homodimerization activity Source: dictyBase

GO - Biological processi

  • actin-myosin filament sliding Source: dictyBase
  • aggregation involved in sorocarp development Source: dictyBase
  • bleb assembly Source: dictyBase
  • cell motility Source: dictyBase
  • chemotaxis Source: dictyBase
  • contractile actin filament bundle assembly Source: dictyBase
  • contractile vacuole organization Source: dictyBase
  • cortical actin cytoskeleton organization Source: dictyBase
  • culmination involved in sorocarp development Source: dictyBase
  • cytoplasmic actin-based contraction involved in forward cell motility Source: dictyBase
  • filopodium assembly Source: dictyBase
  • hypotonic response Source: dictyBase
  • mitotic cytokinesis Source: dictyBase
  • myosin filament assembly Source: dictyBase
  • negative regulation of actin filament polymerization Source: dictyBase
  • protein localization Source: dictyBase
  • pseudopodium retraction Source: dictyBase
  • regulation of cell shape Source: dictyBase
  • response to hydrogen peroxide Source: dictyBase
  • response to mechanical stimulus Source: dictyBase
  • uropod retraction Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.1. 1939.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-2 heavy chain
Alternative name(s):
Myosin II heavy chain
Gene namesi
Name:mhcA
ORF Names:DDB_G0286355
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0286355. mhcA.

Subcellular locationi

GO - Cellular componenti

  • actomyosin Source: dictyBase
  • actomyosin contractile ring Source: dictyBase
  • apical cortex Source: dictyBase
  • cell cortex Source: dictyBase
  • cell trailing edge Source: dictyBase
  • cytoskeleton Source: dictyBase
  • cytosol Source: dictyBase
  • early phagosome Source: dictyBase
  • equatorial cell cortex Source: dictyBase
  • myosin filament Source: dictyBase
  • myosin II complex Source: dictyBase
  • phagocytic cup base Source: dictyBase
  • uropod Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001233731 – 2116Myosin-2 heavy chainAdd BLAST2116

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei130N6,N6-dimethyllysineSequence analysis1
Modified residuei1823Phosphothreonine; by MHCK2 Publications1
Modified residuei1833Phosphothreonine; by MHCK2 Publications1
Modified residuei2029Phosphothreonine; by MHCK2 Publications1

Post-translational modificationi

Phosphorylation inhibits thick filament formation and reduces the actin-activated ATPase activity.2 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiP08799.
PRIDEiP08799.

PTM databases

iPTMnetiP08799.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
elmoAQ54YW12EBI-2928504,EBI-2928498

GO - Molecular functioni

  • 14-3-3 protein binding Source: dictyBase
  • actin filament binding Source: dictyBase
  • protein homodimerization activity Source: dictyBase

Protein-protein interaction databases

DIPiDIP-46078N.
IntActiP08799. 1 interactor.
STRINGi44689.DDB0191444.

Structurei

Secondary structure

12116
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 5Combined sources3
Beta strandi6 – 9Combined sources4
Helixi10 – 15Combined sources6
Helixi22 – 28Combined sources7
Beta strandi34 – 37Combined sources4
Beta strandi39 – 43Combined sources5
Beta strandi44 – 46Combined sources3
Beta strandi48 – 55Combined sources8
Beta strandi57 – 63Combined sources7
Beta strandi65 – 67Combined sources3
Beta strandi69 – 73Combined sources5
Turni74 – 76Combined sources3
Beta strandi77 – 79Combined sources3
Helixi83 – 85Combined sources3
Helixi91 – 93Combined sources3
Helixi99 – 111Combined sources13
Beta strandi116 – 119Combined sources4
Beta strandi122 – 126Combined sources5
Helixi137 – 143Combined sources7
Helixi148 – 150Combined sources3
Helixi155 – 169Combined sources15
Beta strandi173 – 178Combined sources6
Helixi185 – 200Combined sources16
Beta strandi204 – 206Combined sources3
Helixi207 – 209Combined sources3
Helixi210 – 226Combined sources17
Beta strandi227 – 230Combined sources4
Beta strandi236 – 247Combined sources12
Beta strandi249 – 251Combined sources3
Beta strandi253 – 261Combined sources9
Helixi265 – 268Combined sources4
Helixi279 – 287Combined sources9
Helixi290 – 296Combined sources7
Helixi301 – 303Combined sources3
Turni305 – 307Combined sources3
Beta strandi308 – 311Combined sources4
Helixi320 – 334Combined sources15
Helixi338 – 355Combined sources18
Beta strandi359 – 361Combined sources3
Beta strandi363 – 368Combined sources6
Helixi373 – 382Combined sources10
Helixi386 – 394Combined sources9
Beta strandi397 – 400Combined sources4
Beta strandi403 – 406Combined sources4
Helixi411 – 441Combined sources31
Beta strandi447 – 454Combined sources8
Beta strandi462 – 464Combined sources3
Helixi466 – 495Combined sources30
Turni496 – 498Combined sources3
Helixi506 – 510Combined sources5
Helixi511 – 518Combined sources8
Turni520 – 523Combined sources4
Helixi525 – 533Combined sources9
Beta strandi534 – 537Combined sources4
Helixi540 – 551Combined sources12
Turni552 – 554Combined sources3
Beta strandi556 – 559Combined sources4
Beta strandi565 – 572Combined sources8
Beta strandi575 – 580Combined sources6
Helixi584 – 589Combined sources6
Helixi594 – 601Combined sources8
Helixi608 – 613Combined sources6
Helixi615 – 618Combined sources4
Beta strandi624 – 626Combined sources3
Helixi630 – 646Combined sources17
Beta strandi648 – 656Combined sources9
Helixi669 – 678Combined sources10
Helixi681 – 687Combined sources7
Helixi688 – 690Combined sources3
Beta strandi694 – 698Combined sources5
Helixi699 – 701Combined sources3
Turni702 – 704Combined sources3
Helixi706 – 708Combined sources3
Beta strandi709 – 711Combined sources3
Helixi719 – 730Combined sources12
Helixi734 – 736Combined sources3
Beta strandi737 – 739Combined sources3
Beta strandi741 – 746Combined sources6
Turni748 – 752Combined sources5
Beta strandi754 – 756Combined sources3
Beta strandi757 – 760Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PJKX-ray2.15A1-761[»]
ProteinModelPortaliP08799.
SMRiP08799.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08799.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini86 – 759Myosin motorAdd BLAST674
Domaini762 – 791IQPROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni638 – 660Actin-bindingAdd BLAST23
Regioni738 – 752Actin-bindingAdd BLAST15

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili817 – 2116Sequence analysisAdd BLAST1300

Domaini

Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2).Curated
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.

Sequence similaritiesi

Contains 1 IQ domain.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
InParanoidiP08799.
KOiK10352.
OMAiGATRQGK.
PhylomeDBiP08799.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. 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]
PfamiPF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 2 hits.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08799-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPIHDRTSD YHKYLKVKQG DSDLFKLTVS DKRYIWYNPD PKERDSYECG
60 70 80 90 100
EIVSETSDSF TFKTVDGQDR QVKKDDANQR NPIKFDGVED MSELSYLNEP
110 120 130 140 150
AVFHNLRVRY NQDLIYTYSG LFLVAVNPFK RIPIYTQEMV DIFKGRRRNE
160 170 180 190 200
VAPHIFAISD VAYRSMLDDR QNQSLLITGE SGAGKTENTK KVIQYLASVA
210 220 230 240 250
GRNQANGSGV LEQQILQANP ILEAFGNAKT TRNNNSSRFG KFIEIQFNSA
260 270 280 290 300
GFISGASIQS YLLEKSRVVF QSETERNYHI FYQLLAGATA EEKKALHLAG
310 320 330 340 350
PESFNYLNQS GCVDIKGVSD SEEFKITRQA MDIVGFSQEE QMSIFKIIAG
360 370 380 390 400
ILHLGNIKFE KGAGEGAVLK DKTALNAAST VFGVNPSVLE KALMEPRILA
410 420 430 440 450
GRDLVAQHLN VEKSSSSRDA LVKALYGRLF LWLVKKINNV LCQERKAYFI
460 470 480 490 500
GVLDISGFEI FKVNSFEQLC INYTNEKLQQ FFNHHMFKLE QEEYLKEKIN
510 520 530 540 550
WTFIDFGLDS QATIDLIDGR QPPGILALLD EQSVFPNATD NTLITKLHSH
560 570 580 590 600
FSKKNAKYEE PRFSKTEFGV THYAGQVMYE IQDWLEKNKD PLQQDLELCF
610 620 630 640 650
KDSSDNVVTK LFNDPNIASR AKKGANFITV AAQYKEQLAS LMATLETTNP
660 670 680 690 700
HFVRCIIPNN KQLPAKLEDK VVLDQLRCNG VLEGIRITRK GFPNRIIYAD
710 720 730 740 750
FVKRYYLLAP NVPRDAEDSQ KATDAVLKHL NIDPEQYRFG ITKIFFRAGQ
760 770 780 790 800
LARIEEAREQ RISEIIKAIQ AATRGWIARK VYKQAREHTV AARIIQQNLR
810 820 830 840 850
AYIDFKSWPW WKLFSKARPL LKRRNFEKEI KEKEREILEL KSNLTDSTTQ
860 870 880 890 900
KDKLEKSLKD TESNVLDLQR QLKAEKETLK AMYDSKDALE AQKRELEIRV
910 920 930 940 950
EDMESELDEK KLALENLQNQ KRSVEEKVRD LEEELQEEQK LRNTLEKLKK
960 970 980 990 1000
KYEEELEEMK RVNDGQSDTI SRLEKIKDEL QKEVEELTES FSEESKDKGV
1010 1020 1030 1040 1050
LEKTRVRLQS ELDDLTVRLD SETKDKSELL RQKKKLEEEL KQVQEALAAE
1060 1070 1080 1090 1100
TAAKLAQEAA NKKLQGEYTE LNEKFNSEVT ARSNVEKSKK TLESQLVAVN
1110 1120 1130 1140 1150
NELDEEKKNR DALEKKKKAL DAMLEEMKDQ LESTGGEKKS LYDLKVKQES
1160 1170 1180 1190 1200
DMEALRNQIS ELQSTIAKLE KIKSTLEGEV ARLQGELEAE QLAKSNVEKQ
1210 1220 1230 1240 1250
KKKVELDLED KSAQLAEETA AKQALDKLKK KLEQELSEVQ TQLSEANNKN
1260 1270 1280 1290 1300
VNSDSTNKHL ETSFNNLKLE LEAEQKAKQA LEKKRLGLES ELKHVNEQLE
1310 1320 1330 1340 1350
EEKKQKESNE KRKVDLEKEV SELKDQIEEE VASKKAVTEA KNKKESELDE
1360 1370 1380 1390 1400
IKRQYADVVS SRDKSVEQLK TLQAKNEELR NTAEEAEGQL DRAERSKKKA
1410 1420 1430 1440 1450
EFDLEEAVKN LEEETAKKVK AEKAMKKAET DYRSTKSELD DAKNVSSEQY
1460 1470 1480 1490 1500
VQIKRLNEEL SELRSVLEEA DERCNSAIKA KKTAESALES LKDEIDAANN
1510 1520 1530 1540 1550
AKAKAERKSK ELEVRVAELE ESLEDKSGTV NVEFIRKKDA EIDDLRARLD
1560 1570 1580 1590 1600
RETESRIKSD EDKKNTRKQF ADLEAKVEEA QREVVTIDRL KKKLESDIID
1610 1620 1630 1640 1650
LSTQLDTETK SRIKIEKSKK KLEQTLAERR AAEEGSSKAA DEEIRKQVWQ
1660 1670 1680 1690 1700
EVDELRAQLD SERAALNASE KKIKSLVAEV DEVKEQLEDE ILAKDKLVKA
1710 1720 1730 1740 1750
KRALEVELEE VRDQLEEEED SRSELEDSKR RLTTEVEDIK KKYDAEVEQN
1760 1770 1780 1790 1800
TKLDEAKKKL TDDVDTLKKQ LEDEKKKLNE SERAKKRLES ENEDFLAKLD
1810 1820 1830 1840 1850
AEVKNRSRAE KDRKKYEKDL KDTKYKLNDE AATKTQTEIG AAKLEDQIDE
1860 1870 1880 1890 1900
LRSKLEQEQA KATQADKSKK TLEGEIDNLR AQIEDEGKIK MRLEKEKRAL
1910 1920 1930 1940 1950
EGELEELRET VEEAEDSKSE AEQSKRLVEL ELEDARRNLQ KEIDAKEIAE
1960 1970 1980 1990 2000
DAKSNLQREI VEAKGRLEEE SIARTNSDRS RKRLEAEIDA LTAQVDAEQK
2010 2020 2030 2040 2050
AKNQQIKENK KIETELKEYR KKFGESEKTK TKEFLVVEKL ETDYKRAKKE
2060 2070 2080 2090 2100
AADEQQQRLT VENDLRKHLS EISLLKDAID KLQRDHDKTK RELETETASK
2110
IEMQRKMADF FGGFKA
Length:2,116
Mass (Da):243,786
Last modified:March 20, 2007 - v3
Checksum:i97DE4FB422AD3D56
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti249S → N in AAA33227 (PubMed:3540939).Curated1
Sequence conflicti312C → Y in AAA33227 (PubMed:3540939).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14628 Genomic DNA. Translation: AAA33227.1.
AAFI02000085 Genomic DNA. Translation: EAL64202.1.
PIRiA26655.
RefSeqiXP_637740.1. XM_632648.1.

Genome annotation databases

EnsemblProtistsiEAL64202; EAL64202; DDB_G0286355.
GeneIDi8625606.
KEGGiddi:DDB_G0286355.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14628 Genomic DNA. Translation: AAA33227.1.
AAFI02000085 Genomic DNA. Translation: EAL64202.1.
PIRiA26655.
RefSeqiXP_637740.1. XM_632648.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PJKX-ray2.15A1-761[»]
ProteinModelPortaliP08799.
SMRiP08799.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46078N.
IntActiP08799. 1 interactor.
STRINGi44689.DDB0191444.

PTM databases

iPTMnetiP08799.

Proteomic databases

PaxDbiP08799.
PRIDEiP08799.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL64202; EAL64202; DDB_G0286355.
GeneIDi8625606.
KEGGiddi:DDB_G0286355.

Organism-specific databases

dictyBaseiDDB_G0286355. mhcA.

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
InParanoidiP08799.
KOiK10352.
OMAiGATRQGK.
PhylomeDBiP08799.

Enzyme and pathway databases

BRENDAi3.6.4.1. 1939.

Miscellaneous databases

EvolutionaryTraceiP08799.
PROiP08799.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. 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]
PfamiPF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 2 hits.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMYS2_DICDI
AccessioniPrimary (citable) accession number: P08799
Secondary accession number(s): Q54LU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: March 20, 2007
Last modified: November 2, 2016
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

Dictyostelium myosin-2 has no K2EDTA ATPase activity, perhaps correlated with the absence of a Cys at the SH-1 position (688).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.