MYOB_TOXGO
ID MYOB_TOXGO Reviewed; 1171 AA.
AC O00936; O00935; Q8WRF8; Q8WRF9; Q9U618;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 4.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Myosin-B/C;
DE Short=MyoB/C;
DE AltName: Full=TgM-B;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811 {ECO:0000312|EMBL:AAC47726.3};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MYOSIN B AND MYOSIN C), SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=11706051; DOI=10.1083/jcb.200012116;
RA Delbac F., Sanger A., Neuhaus E.M., Stratmann R., Ajioka J.W., Toursel C.,
RA Herm-Gotz A., Tomavo S., Soldati T., Soldati D.;
RT "Toxoplasma gondii myosins B/C: one gene, two tails, two localizations, and
RT a role in parasite division.";
RL J. Cell Biol. 155:613-623(2001).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-1171 (ISOFORMS MYOSIN B AND MYOSIN C).
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 [3] {ECO:0000305}
RP SEQUENCE REVISION TO 745-746.
RA Heintzelman M.B., Schwartzman J.D.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE OF 71-139.
RC STRAIN=RH;
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 [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE OF 1-139, AND SEQUENCE REVISION.
RA Delbac F., Soldati D.;
RL Submitted (OCT-2001) 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. Plays a role in proper
CC daughter cell budding and separation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11706051}.
CC Note=Isoform MyoB is cytoplasmic while isoform MyoC is concentrated at
CC the anterior and posterior polar rings of the inner membrane complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Myosin B; Synonyms=MyoB;
CC IsoId=O00936-1; Sequence=Displayed;
CC Name=Myosin C; Synonyms=Myoc;
CC IsoId=O00936-2; Sequence=VSP_050203, VSP_050204;
CC -!- DEVELOPMENTAL STAGE: Both isoforms are expressed at higher levels in
CC bradyzoites than in tachyzoites. Isoform MyoC is the predominant
CC isoform in tachyzoites. {ECO:0000269|PubMed:11706051}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AF438183; AAL30895.1; -; mRNA.
DR EMBL; AF438184; AAL30896.1; -; mRNA.
DR EMBL; AF006627; AAC47725.3; -; mRNA.
DR EMBL; AF006628; AAC47726.3; -; mRNA.
DR EMBL; AF202585; AAF09586.2; -; Genomic_DNA.
DR PIR; T29105; T29105.
DR PIR; T29106; T29106.
DR AlphaFoldDB; O00936; -.
DR SMR; O00936; -.
DR PRIDE; O00936; -.
DR VEuPathDB; ToxoDB:TGARI_255190; -.
DR VEuPathDB; ToxoDB:TGCAST_255190; -.
DR VEuPathDB; ToxoDB:TGCOUG_255190; -.
DR VEuPathDB; ToxoDB:TGDOM2_255190A; -.
DR VEuPathDB; ToxoDB:TGDOM2_255190B; -.
DR VEuPathDB; ToxoDB:TGFOU_255190; -.
DR VEuPathDB; ToxoDB:TGGT1_255190; -.
DR VEuPathDB; ToxoDB:TGMAS_255190A; -.
DR VEuPathDB; ToxoDB:TGMAS_255190B; -.
DR VEuPathDB; ToxoDB:TGME49_255190; -.
DR VEuPathDB; ToxoDB:TGP89_255190; -.
DR VEuPathDB; ToxoDB:TGPRC2_255190; -.
DR VEuPathDB; ToxoDB:TGRH88_073760; -.
DR VEuPathDB; ToxoDB:TGRUB_255190; -.
DR VEuPathDB; ToxoDB:TGVAND_255190; -.
DR VEuPathDB; ToxoDB:TGVEG_255190; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030286; C:dynein complex; IEA:InterPro.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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 GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd14876; MYSc_Myo14; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR037177; DLC_sf.
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 SUPFAM; SSF54648; SSF54648; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; ATP-binding; Cytoplasm; Motor protein;
KW Myosin; Nucleotide-binding.
FT CHAIN 1..1171
FT /note="Myosin-B/C"
FT /id="PRO_0000123378"
FT DOMAIN 105..780
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 671..681
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 810..1171
FT /note="Tail"
FT BINDING 199..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1054..1074
FT /note="IVRVMNSKVPPYMQKDVSYLI -> NAPTQEFVIFSLTWKHNQKHS (in
FT isoform Myosin C)"
FT /evidence="ECO:0000303|PubMed:11706051,
FT ECO:0000303|PubMed:9300060"
FT /id="VSP_050203"
FT VAR_SEQ 1075..1171
FT /note="Missing (in isoform Myosin C)"
FT /evidence="ECO:0000303|PubMed:11706051,
FT ECO:0000303|PubMed:9300060"
FT /id="VSP_050204"
FT CONFLICT 791
FT /note="A -> G (in Ref. 1; AAL30895/AAL30896)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1171 AA; 132672 MW; 2A5D98FA96C44D3A CRC64;
MERKQTQMIL GRRLAKDSPE VKHFQRKSSV VPFGRDGRAA TNFTCWTADC PAVKADPTLV
FAKCIVVGGS MDTQLELEQV DPPARGTFTV APTDVFNANE LIEPETVDDI GYLPHTNVAC
VLDVLKSRFL RSIIYTTAEP LLVAINPFKD LGNTTDAWIS TYRNASKPEM LPPHVFKTAR
AALEDLEGYK KNQSIIVSGE SGAGKTEATK QIMRFFASAS SEVRTTIQDT IMAGNPILEA
FGNAKTIRNN NSSRFGRFMM LDVSSHRGIQ HGSISNFLLE KVRVVSQEAN ERSYHIFYQL
LKGATSEMRA KYHLRSLKEY AYLNGKNGGC YDVPGIDDKA DFEEVLQSLD AMQITGSKRH
SVFSILSGLL LIGNVSIEGK DAQGVPDAAY ISPQSEEILE EACQLLSVDD AALKKEILVK
STKVGPQVIE GVRTKDEAKT SVLSLSKNVY DKLFDWLVRQ LNSLIDAPDG MPNFIGILDI
FGFEVLEVNS LEQVLINITN EYLQKHFIDV VFDMETKLYQ AEGVPTEALE YTDNLALVGA
LCGKNDSFFA LLEDACLGIR STDEGFCGTI LRRLEPSGFF LESRRDKRLK FIIRHTIADI
EYTCEGMLEK NKDFLRKEVM DVMKASTDPV TKALFEGIEI EAGKIGKGTL IASRFLKNLE
EMIGIVAQTE AHFIRCLKPN EEKKPLGWNG SKVLNQLFSL SILEALQLRQ VGYAYRRNFS
EFCSHFRWLD LGLVNSDRDR KEVAQLLLEQ SGIPESSWVI GKTMVFVKPD AAKELSILQR
EKLMCFQPLI AVLGPMWRKV LLRKKMARVI HFLTRLESNA RRHLEPDSIN ISPEEREALL
SGMERPRNPC VVVKKRVEPE RAPPTKVLSL SRARLSLSKE LPRNYAASNE ALDVDDTMSV
DTDAFLRLKM KRSPNENYLR QTALARLKER RPSHVCMEEA YHVWRSVELL FREPLSDKRL
QNICTVIRND MDQHYGFFWQ VIINRTPNFG MAATHIHGSL HVVEQEGMYR DGRQFLFHLI
MYKTRKPRKE EIRLHERAAE KTYGICRKRD FSGIVRVMNS KVPPYMQKDV SYLIGMLFQR
YQYTRDWTNF ATCIQSYLIG RYSEPFGGAW NVVAQEGAFF LSRLWTKHSR FLRVEIDFPA
LAEQASSEPC PGCPTPVLTV VCFEACAPDR P
