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
//