ID   MYOD_TOXGO              Reviewed;         822 AA.
AC   Q9XYF6;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Myosin-D;
DE            Short=MyoD;
DE   AltName: Full=TgM-D;
OS   Toxoplasma gondii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=5811;
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).
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; Peripheral membrane protein.
CC       Cytoplasm.
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; AF105118; AAD21243.1; -; mRNA.
DR   AlphaFoldDB; Q9XYF6; -.
DR   SMR; Q9XYF6; -.
DR   VEuPathDB; ToxoDB:TGARI_263180; -.
DR   VEuPathDB; ToxoDB:TGCAST_263180; -.
DR   VEuPathDB; ToxoDB:TGCOUG_263180; -.
DR   VEuPathDB; ToxoDB:TGDOM2_263180; -.
DR   VEuPathDB; ToxoDB:TGFOU_263180A; -.
DR   VEuPathDB; ToxoDB:TGFOU_263180B; -.
DR   VEuPathDB; ToxoDB:TGGT1_263180; -.
DR   VEuPathDB; ToxoDB:TGMAS_263180; -.
DR   VEuPathDB; ToxoDB:TGME49_263180; -.
DR   VEuPathDB; ToxoDB:TGP89_263180A; -.
DR   VEuPathDB; ToxoDB:TGP89_263180B; -.
DR   VEuPathDB; ToxoDB:TGPRC2_263180A; -.
DR   VEuPathDB; ToxoDB:TGPRC2_263180B; -.
DR   VEuPathDB; ToxoDB:TGRH88_067840; -.
DR   VEuPathDB; ToxoDB:TGRUB_257470; -.
DR   VEuPathDB; ToxoDB:TGRUB_263180; -.
DR   VEuPathDB; ToxoDB:TGVAND_263180; -.
DR   VEuPathDB; ToxoDB:TGVEG_263180; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Cytoplasm; Membrane;
KW   Motor protein; Myosin; Nucleotide-binding.
FT   CHAIN           1..822
FT                   /note="Myosin-D"
FT                   /id="PRO_0000123379"
FT   DOMAIN          95..770
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   REGION          660..670
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          772..822
FT                   /note="Tail"
FT   BINDING         189..196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   822 AA;  91063 MW;  4308CE770EDE6F15 CRC64;
     MAAKPEQDCK TAAALIRAGS LIEGVESAGK DFLVWTTQGP AVKKDPDLLF SLCRVLPGST
     QQTLKLQQVE PTADSQELTV QAKEVWQANP GIDPLTYGDI GGLPHTNEPC VLDFLARRYQ
     SKVIYTTAEP LIVAVNPFQD LKNAGPDTIA LYRDAPDVDK LPPHVFYASR RAMTNMHQLK
     KPQTIIVSGE SGAGKTETTK MLMKYLATSA GGNLDLKIQT AIMAANPVLE AFGNAKTVRN
     NNSSRFGRFM LLDVAREGGI QHGKVVAFLL EKSRIVCQDK DERNYHIFYQ FLKGAPGHMR
     QRYMLQPLEA YTFINPHCLD APGIVDTEDF EQTVKSLESM NMTETETCTI WSIVSGVLLM
     GNAKPTGKTE AGVENAACFV GESEAALRNA CSLLFLDYPS ILHELTVKTT YAGSNKIESR
     WTVPDSEMLR ASLAKGMFEQ LFLWIIRKLN ADIEPKGGSF DVFMGLLDIF GFEVFQNNSL
     EQLFINITNE VLQRNFTDIV FEKELQLYSK EGISSKKIEY TTNEKLIETL LGKGTSVLAA
     LEDQCISPSG TDEKFVSSLA SKLAGNKCFI PSKNTKSLEF TVVHTIGKVI YNADGFAFKN
     KDVLRPEIIE ITRASTNDVV RGLFEGVKVE KGKMAKGMLI GSQFMTQLKG LMEVIQKTES
     HFIRCIKPND DKVPLKWVNS KVLIQLHALS ILEALHLRQL AFSYRRTFEE FAAQFRFINL
     GVSNKPGADA KTICVELLKS TSISADEYAL GKTMVFLKPQ AAKMLVRLQR EALSAWEPLV
     GVFEGMTVLK RAKQLSTGRA VPATRICANV RRKLVQAGIK VC