MYOA_TOXGO
ID MYOA_TOXGO Reviewed; 831 AA.
AC O00934;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Myosin-A;
DE Short=MyoA;
DE AltName: Full=TgM-A;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9300060; DOI=10.1006/jmbi.1997.1167;
RA Heintzelman M.B., Schwartzman J.D.;
RT "A novel class of unconventional myosins from Toxoplasma gondii.";
RL J. Mol. Biol. 271:139-146(1997).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 814-ARG-ARG-815.
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 {ECO:0000269|PubMed:10749937};
CC Peripheral membrane protein {ECO:0000269|PubMed:10749937}; Cytoplasmic
CC side {ECO:0000269|PubMed:10749937}. Note=Tightly associated with the
CC plasma membrane.
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; AF006626; AAC47724.1; -; mRNA.
DR PIR; A59283; A59283.
DR PDB; 5VT9; X-ray; 1.85 A; C/D=801-831.
DR PDB; 6TJ5; X-ray; 2.39 A; C=777-818.
DR PDB; 6TJ6; X-ray; 2.00 A; C=777-818.
DR PDB; 6TJ7; X-ray; 2.30 A; C=777-818.
DR PDBsum; 5VT9; -.
DR PDBsum; 6TJ5; -.
DR PDBsum; 6TJ6; -.
DR PDBsum; 6TJ7; -.
DR AlphaFoldDB; O00934; -.
DR SMR; O00934; -.
DR SwissPalm; O00934; -.
DR VEuPathDB; ToxoDB:TGARI_235470A; -.
DR VEuPathDB; ToxoDB:TGARI_235470B; -.
DR VEuPathDB; ToxoDB:TGCAST_235470A; -.
DR VEuPathDB; ToxoDB:TGCAST_235470B; -.
DR VEuPathDB; ToxoDB:TGCOUG_235470; -.
DR VEuPathDB; ToxoDB:TGDOM2_235470; -.
DR VEuPathDB; ToxoDB:TGFOU_235470A; -.
DR VEuPathDB; ToxoDB:TGFOU_235470B; -.
DR VEuPathDB; ToxoDB:TGFOU_235470C; -.
DR VEuPathDB; ToxoDB:TGGT1_235470; -.
DR VEuPathDB; ToxoDB:TGMAS_235470A; -.
DR VEuPathDB; ToxoDB:TGMAS_235470B; -.
DR VEuPathDB; ToxoDB:TGME49_235470; -.
DR VEuPathDB; ToxoDB:TGP89_235470A; -.
DR VEuPathDB; ToxoDB:TGP89_235470B; -.
DR VEuPathDB; ToxoDB:TGPRC2_235470A; -.
DR VEuPathDB; ToxoDB:TGPRC2_235470B; -.
DR VEuPathDB; ToxoDB:TGRH88_041990; -.
DR VEuPathDB; ToxoDB:TGRUB_235470; -.
DR VEuPathDB; ToxoDB:TGVAND_235470A; -.
DR VEuPathDB; ToxoDB:TGVAND_235470B; -.
DR VEuPathDB; ToxoDB:TGVEG_235470; -.
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.
FT CHAIN 1..831
FT /note="Myosin-A"
FT /id="PRO_0000123377"
FT DOMAIN 99..773
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 663..673
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 775..831
FT /note="Tail"
FT BINDING 193..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 814..815
FT /note="RR->AA: Complete loss of membrane localization."
FT /evidence="ECO:0000269|PubMed:10749937"
FT HELIX 803..816
FT /evidence="ECO:0007829|PDB:5VT9"
FT HELIX 818..820
FT /evidence="ECO:0007829|PDB:5VT9"
SQ SEQUENCE 831 AA; 93334 MW; 56C4ED1D50C2FB74 CRC64;
MASKTTSEEL KTATALKKRS SDVHAVDHSG NVYKGFQIWT DLAPSVKEEP DLMFAKCIVQ
AGTDKGNLTC VQIDPPGFDE PFEVPQANAW NVNSLIDPMT YGDIGMLPHT NIPCVLDFLK
VRFMKNQIYT TADPLVVAIN PFRDLGNTTL DWIVRYRDTF DLSKLAPHVF YTARRALDNL
HAVNKSQTII VSGESGAGKT EATKQIMRYF AAAKTGSMDL RIQNAIMAAN PVLEAFGNAK
TIRNNNSSRF GRFMQLDVGR EGGIKFGSVV AFLLEKSRVL TQDEQERSYH IFYQMCKGAD
AAMKERFHIL PLSEYKYINP LCLDAPGIDD VAEFHEVCES FRSMNLTEDE VASVWSIVSG
VLLLGNVEVT ATKDGGIDDA AAIEGKNLEV FKKACGLLFL DAERIREELT VKVSYAGNQE
IRGRWKQEDG DMLKSSLAKA MYDKLFMWII AVLNRSIKPP GGFKIFMGML DIFGFEVFKN
NSLEQFFINI TNEMLQKNFV DIVFDRESKL YRDEGVSSKE LIFTSNAEVI KILTAKNNSV
LAALEDQCLA PGGSDEKFLS TCKNALKGTT KFKPAKVSPN INFLISHTVG DIQYNAEGFL
FKNKDVLRAE IMEIVQQSKN PVVAQLFAGI VMEKGKMAKG QLIGSQFLSQ LQSLMELINS
TEPHFIRCIK PNDTKKPLDW VPSKMLIQLH ALSVLEALQL RQLGYSYRRP FKEFLFQFKF
IDLSASENPN LDPKEAALRL LKSSKLPSEE YQLGKTMVFL KQTGAKELTQ IQRECLSSWE
PLVSVLEAYY AGRRHKKQLL KKTPFIIRAQ AHIRRHLVDN NVSPATVQPA F
