MYOA_PLAYO
ID MYOA_PLAYO Reviewed; 817 AA.
AC Q7RQ71;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Myosin-A;
GN Name=MyoA {ECO:0000305}; ORFNames=PY01232;
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL;
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D.,
RA Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W.,
RA Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails are presumed to bind to membranous compartments, which
CC would be moved relative to actin filaments (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Tightly
CC associated with the plasma membrane. {ECO:0000250}.
CC -!- DOMAIN: This protein differs from the typical myosin heavy chain
CC structure in having head and tail domains but no discernible neck
CC domain.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AABL01000322; EAA20523.1; -; Genomic_DNA.
DR PDB; 2AUC; X-ray; 2.60 A; D=803-817.
DR PDB; 2QAC; X-ray; 1.70 A; T=803-817.
DR PDB; 4GGN; X-ray; 2.29 A; D/E/F=803-817.
DR PDBsum; 2AUC; -.
DR PDBsum; 2QAC; -.
DR PDBsum; 4GGN; -.
DR AlphaFoldDB; Q7RQ71; -.
DR SMR; Q7RQ71; -.
DR DIP; DIP-61139N; -.
DR IntAct; Q7RQ71; 2.
DR STRING; 73239.Q7RQ71; -.
DR EnsemblProtists; EAA20523; EAA20523; EAA20523.
DR InParanoid; Q7RQ71; -.
DR OMA; NGIMEAR; -.
DR EvolutionaryTrace; Q7RQ71; -.
DR Proteomes; UP000008553; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR CDD; cd14876; MYSc_Myo14; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036044; MYSc_Myo14.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ATP-binding; Cell membrane; Membrane;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..817
FT /note="Myosin-A"
FT /id="PRO_0000123376"
FT DOMAIN 97..771
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 661..671
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 773..817
FT /note="Tail"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IDR3"
FT HELIX 804..816
FT /evidence="ECO:0007829|PDB:2QAC"
SQ SEQUENCE 817 AA; 92192 MW; 5B1BF409873134FC CRC64;
MAVTNEELKT AHKIVRRVSN IEAFDKSGVV FKGYQIWTNI SPTIEEDPNV MFVKCVVQHG
SNQDKLNVVQ IDPPGSGTPY EIDVKSAWNC NSQVDPMSFG DIGLLNHTNT PCVLDFLKHR
YLKNQIYTTA CPLIVAINPY KDLGNTTDEW IRKYRDASDH TRLPPHIFSC AREALSNLHG
VNKSQTIIVS GESGAGKTEA TKQIMKYFAS SKNGNMDLYI QTAIMAANPV LEAFGNAKTI
RNNNSSRFGR FMQLAISHEG GIRNGSVVAF LLEKSRIITQ DDNERSYHIF YQFLKGADSN
MKSKFGLKGI KDYKLLNPNS PDVDGIDDVK DFQEVITSLK NMQLNDEQIE VIFSIIAGIL
TLGNVRIVEK TEAGLSDAAG IHNDDMETFK KACELMFLDP ELVKRELLIK VTIAGGNRIE
GRWNKNDAEV LKLSLCKAMY EKLFLWIIKN LNSRIEPEGG FKAFMGMLDI FGFEVFKNNS
LEQLFINITN EMLQKNFVDI VFERESKLYR DEGISTAELN YTSNKEVISV LCERGKSVLS
YLEDQCLAPG GSDEKFVNAC VVNLKSNEKF IPAKVASNKN FIIQHTIGPI QYCSDNFLLK
NKDVLRGELV EIILGSGNKV VSGLFEGQVI EKGKMAKGSL IGSQFLNQLT SLMTLINSTE
PHFIRCIKPN ENKKPLEWCE PKILIQLHAL SILEALVLRQ LGYSYRRTFD EFLYQFKFVD
INTSENSSLD SREKCNKILK LSGLSDDMLK IGKTMVFLKQ DGAKMLSKIQ REKLVEWENC
VSVIEAAIMK YKHKQNVENN VSSLMRVQAH IRKRMVA