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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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