ID   MYOA_PLAFB              Reviewed;         818 AA.
AC   Q9UAR6; P90624;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Myosin-A;
DE   AltName: Full=PfM-A;
GN   Name=MyoA {ECO:0000305};
OS   Plasmodium falciparum (isolate FCBR / Columbia).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=33631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10749937; DOI=10.1091/mbc.11.4.1385;
RA   Hettmann C., Herm A., Geiter A., Frank B., Schwarz E., Soldati T.,
RA   Soldati D.;
RT   "A dibasic motif in the tail of a class XIV apicomplexan myosin is an
RT   essential determinant of plasma membrane localization.";
RL   Mol. Biol. Cell 11:1385-1400(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 183-670.
RA   Pinder J.C.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
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; AF105117; AAD21242.1; -; mRNA.
DR   EMBL; Y09693; CAA70869.1; -; mRNA.
DR   PIR; A59291; A59291.
DR   AlphaFoldDB; Q9UAR6; -.
DR   SMR; Q9UAR6; -.
DR   PRIDE; Q9UAR6; -.
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   2: Evidence at transcript level;
KW   Actin-binding; ATP-binding; Cell membrane; Membrane; Motor protein; Myosin;
KW   Nucleotide-binding; Phosphoprotein.
FT   CHAIN           1..818
FT                   /note="Myosin-A"
FT                   /id="PRO_0000123375"
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..818
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"
SQ   SEQUENCE   818 AA;  92277 MW;  F397875C52B3B19E CRC64;
     MAVTNEEIKT ASKIVRRVSN VEAFDKSGSV FKGYQIWTDI SPTIENDPNI MFVKCVVQQG
     SKKEKLTVVQ IDPPGTGTPY DIDPTHAWNC NSQVDPMSFG DIGLLNHTNI PCVLDFLKHR
     YLKNQIYTTA VPLIVAINPY KDLGNTTNEW IRRYRDTADH TKLPPHVFTC AREALSNLHG
     VNKSQTIIVS GESGAGKTEA TKQIMRYFAS SKSGNMDLRI QTAIMAANPV LEAFGNAKTI
     RNNNSSRFGR FMQLVISHEG GIRYGSVVAF LLEKSRIITQ DDNERSYHIF YQFLKGANST
     MKSKFGLKGV TEYKLLNPNS TEVSGVDDVK DFEEVIESLK NMELSESDIE VIFSIVAGIL
     TLGNVRLIEK QEAGLSDAAA IMDEDMGVFN KACELMYLDP ELIKREILIK VTVAGGTKIE
     GRWNKNDAEV LKSSLCKAMY EKLFLWIIRH LNSRIEPEGG FKTFMGMLDI FGFEVFKNNS
     LEQLFINITN EMLQKNFVDI VFERESKLYK DEGISTAELK YTSNKEVINV LCEKGKSVLS
     YLEDQCLAPG GTDEKFVSSC ATNLKENNKF TPAKVASNKN FIIQHTIGPI QYCAESFLLK
     NKDVLRGDLV EVIKDSPNPI VQQLFEGQVI EKGKIAKGSL IGSQFLNQLT SLMNLINSTE
     PHFIRCIKPN ENKKPLEWCE PKILIQLHAL SILEALVLRQ LGYSYRRTFE EFLYQYKFVD
     IAAAEDSSVE NQNKCVNILK LSGLSESMYK IGKSMVFLKQ EGAKILTKIQ REKLVEWENC
     VSVIEAAILK HKYKQKVNKN IPSLLRVQAH IRKKMVAQ