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Database: UniProt
Entry: A0A060X4S9_ONCMY
LinkDB: A0A060X4S9_ONCMY
Original site: A0A060X4S9_ONCMY 
ID   A0A060X4S9_ONCMY        Unreviewed;      1938 AA.
AC   A0A060X4S9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Myosin heavy chain, fast skeletal muscle-like {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GSONMT00032573001 {ECO:0000313|EMBL:CDQ72324.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ72324.1, ECO:0000313|Proteomes:UP000193380};
RN   [1] {ECO:0000313|EMBL:CDQ72324.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24755649; DOI=10.1038/ncomms4657;
RA   Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA   Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA   Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA   Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA   Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA   Guiguen Y.;
RT   "The rainbow trout genome provides novel insights into evolution after
RT   whole-genome duplication in vertebrates.";
RL   Nat. Commun. 5:3657-3657(2014).
RN   [2] {ECO:0000313|EMBL:CDQ72324.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC       chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC       regulatory light chain subunits (MLC-2).
CC       {ECO:0000256|ARBA:ARBA00038612}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC       {ECO:0000256|ARBA:ARBA00004657}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; FR904825; CDQ72324.1; -; Genomic_DNA.
DR   STRING; 8022.A0A060X4S9; -.
DR   PaxDb; 8022-A0A060X4S9; -.
DR   Proteomes; UP000193380; Unassembled WGS sequence.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 4.
DR   Gene3D; 1.20.5.370; -; 4.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.10.250.2420; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF44; MYOSIN-4; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 5.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000193380}.
FT   DOMAIN          32..81
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          85..794
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          671..693
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1581..1602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1883..1938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          858..1271
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1883..1930
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         178..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1938 AA;  221888 MW;  97D8116E1D93C7DF CRC64;
     MGDSEMQCFG AAAIYLRKPE RERITAQAAP FDAKSAFFVV EPKEMYLKGV LQSREGGKAT
     VKTLCGQTIT VKEDDIHPMN PPKYDKIEDM AMMTHLNEAT VLYNLKERYA AWMIYTYSGL
     FCVTVNPYKW LPVYDQSVVN AYRGKKRIEA PPHIFSISDN AYQHMLTDRE NQSILITGES
     GAGKTVNTKR VIQYFATIAV AGGKKEQAAA AASGKIKGSL EDQIIAANPL LEAYGNAKTV
     RNDNSSRFGK FIRIHFGTTG KLASADIETY LLEKSRVTFQ LSAERSYHIF YQLMTGHQPQ
     LLDALLITTN PYDYPMLSQG EITVKSICDV DEFIATDATH LYFKSQEAID ILGFTADEKI
     GIFKLTGSVM HHGAMKFKQK QREEQAEPDG TEVADKISYL MGLNSADLLK ALCYPRVKVG
     NEMVTKGQTV PQVGNSVMAL CKSVYEKMFL WMVVRINEML DTKQARQFFI GVLDIAGFEI
     FDYNSLEQLC INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WAFIDFGMDL AACIELIEKP
     MGIFSILEEE CMFPKASDTT FKTKLNEQHL GKTAAFQKPK PTKGKEAGKE AHFALVHYAG
     IVEYSITGWL DKNKDPLNDS VVQLYQKSTV KLLAYLYVTP AADGSAASKK GGAKKKGGSF
     QTVSALFREN LGKLMTNLRS THPHFVRCLI PNESKTPGLM ENFLVIHQLR CNGVLEGIRI
     CRKGFPSRIQ YGDFKQRYKV LNAKVIPEGQ FMDNKKASEK LLGSIDVDHT QYKFGHTKVF
     FKAGLLGTLE EMRDEKLASL VTMTQALCRG FLMRREYMKM IERRESTFAI QYNIRSFMNV
     KTWPWMKLYF KIKPLLKSAE TEKEMAQMKE TFEKTKEDLT KALSKKKELE EKMVAILNER
     NALALQVASE GESLNDAEER CEGLIKSKIQ LEAKLKETTE RLEDEEELNA EVTAKKRKLE
     DECSELKKDI DDLELTLAKV EKEKHATENK VKNLVEEMAS QDETIAKLTK EKKALQEAHQ
     QVLDDLQAEE DKVNTLTKAK TKLEQQVDDL EGSLEQEKKV RMDLERAKRK LEGDLKLSQE
     SVMDLENDRQ QSEEKIKKKD FELSQFLNKV EDEQTLGLQL QKKIKELQAR VEELEEEIEA
     ERAARAKVEK QRSDLSRELE EISERLEEAG GATSVQIEMS KKREAEFQKL RRDLEEKQAD
     TVAELGEQID NLQRVKQKLE KEKSEFKMEI DDLSSNLESV SKSKGIYEKM CRSLEDQMSE
     LKSKNDEHVR QLNDIGVLRA RLLTENGEYG RQLEEKEALV SQLTRGKQAF TQQVEELKRH
     IEEEVKSKNA LAHSVQSARH DCDLLREQYE EEQEAKAELQ RGLSKANGEV AQWRTKYETD
     AIQRTEELED AKKKLAQRLQ DAQETIEATN SKCASLEKTK QRLLGEVEDL MIDVERANAS
     AAQLDKKQRN FDKVLAEWKQ KYEEGQAELE GSLKEARSLS TELFKMKNSY EECLDHLETL
     KRENKNLQQE IADLTEHIGE SGKTIHELEK GKKTVELEKS EFQTALEEAE ATLEHEESKI
     LHVQLELTQV KSEVDRKLAE KDEETEQIKR NSQRMMDSMQ STLDTEIRSR NDALRIKKKM
     EGDLNEMEIQ LSHANRQAAE SQKQLRNIQG ALKDAQLHLD DAVRASDDMK EQVAIVERRN
     NLMLAEIEEL RAALEQTERG RKVAEQELVD ASERVGLLHS QNTSLINTKK KLEVDLTQIQ
     GEMEDTVQEA RNADEKAKKA ITDAAMMAEE LKKEQDTSSH LERMKKNLEV TVKDLQHRLD
     EAENLAMKGG KKQLQKLEAR VRELESEVDA EQRRSADAIK GVRKYERRVK ELSYQTEEDK
     KNANRLQDLV DKLQLKVKAY KRQSEEAEEQ SNTHLSRYRK VQHELEEAQE RADIAESQVS
     KMRAKSREIG GKVRSTLY
//
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