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Database: UniProt
Entry: A0A3Q2D0I9_CYPVA
LinkDB: A0A3Q2D0I9_CYPVA
Original site: A0A3Q2D0I9_CYPVA 
ID   A0A3Q2D0I9_CYPVA        Unreviewed;      1933 AA.
AC   A0A3Q2D0I9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Myosin heavy chain, fast skeletal muscle-like {ECO:0000313|Ensembl:ENSCVAP00000011813.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000011813.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000011813.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   STRING; 28743.ENSCVAP00000011813; -.
DR   Ensembl; ENSCVAT00000018896.1; ENSCVAP00000011813.1; ENSCVAG00000014231.1.
DR   GeneTree; ENSGT00940000162888; -.
DR   OMA; TKNEEHM; -.
DR   Proteomes; UP000265020; Unplaced.
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; -; 5.
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; 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:UP000265020}.
FT   DOMAIN          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          86..779
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          656..678
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1879..1933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          843..1277
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1933 AA;  221743 MW;  C2F8E79363F58304 CRC64;
     MSSDPEMECF GPAAVYLRKP ERERIEAQNT PFDAKTAYFV TEQAEMYLKG KLVKKEGGKA
     TVEVQGGKTL TVKEDEIFPM NPPKFDKIED MAMMTHLSEP AVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYDAVVV AGYRGKKRIE APPHIFSISD NAYQFMLQDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA VASSGKKAEP IPGKMQGSLE DQIIAANPLL EAYGNAKTVR
     NDNSSRFGKF IRIHFGTSGK LASADIETYL LEKSRVTFQL SAERSYHIFY QLTTGHKPEL
     IEALLITTNP YDFPMISQGE ITVKSINDVE EFMATDTAID ILGFTAEEKV SIYKLTGAVM
     HHGNMKFKQK QREEQAEPDG TEVADKIAYL MGLNSADMLK ALCYPRVKVG NEMVVKGQTV
     PQVHNAVSAL CKSVYEKMFL WMVVRINEML DTKQPRSFFI GVLDIAGFEI FDFNSLEQLC
     INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP LGIFSILEEE
     CIVPKATDMT FKSKLYDQHV GKSAPFQKPK PAKGKAEAHF SLVHYAGTVD YNVNGWLDKN
     KDPLNDSVVQ LYQKSANKLL AHLYASHAGT DGGKKGGGKK KGGSFQTVSA LFRENLGKLM
     TNLRSTHPHF VRCLIPNESK TPGLMENFLV IHQLRCNGVL EGIRICRKGF PSRILYGDFK
     QRYKVLNASV IPEGQFIDNK KASEKLLGSI NIDHTQYRFG HTKVFFKAGL LGTLEEMRDE
     KLVQLVTMTQ ALCRGYVMRK EFVKMMERRE SIFTIQYNIR AFMNVKTWPW MKLYFKIKPL
     LKSAETEKEM AQMKEDFEKT KEELAKALAK KKELEEKMVS LLQEKNDLQL QVQSEGETLA
     DAEERCEQLI KAKIQLEAKV KETSERLEDE EEINAELTAK KRKLEDECSE LKKDIDDLEL
     TLAKVEKEKH ATENKVKNLV EEMASQDETI AKLTKEKKAL QEAHQQILDD LQAEEDKVNT
     LTKAKTKLEQ QVDDLEGSLE QEKKLRMDLE RAKRKLEGDL KLAQETIMDL ENDKQQSDEK
     IKKRDFEISQ LLGKIEDEQT IGVQLNKKIK ELQARIEELE EEIEAERAAR AKVEKQRSDL
     SRELEEISER LEEAGGATSV QIEMNKKREA EFQKLRRDLE EATLQHEATA AALRKKQADS
     VAELGEQIDN LQRVKQKLEK EKSEYKMEID DLSSNMEATA KAKANMEKMC RSLEDQLSEL
     KTKNDEHIRQ LNDTNSHKAR LVSENGEISR QLEEKESLVS QLTRGKQAFM HQIEELKRHL
     EEEIKAKNAL AHAVQSARHD CDLLREQYEE EQEAKGELQR AMSKANSEVA QWRAKYETDA
     IQRTEELEEA KKKLAQRLQD AEESIEAVNA KCGSLEKTKQ RLQGEVEDLM IDVERANALA
     ANLDKKQRNF DKVLAEWKQK YEESQAELEG AQKEARALNT EMFKMKNSYE EALDHLETLK
     RENKNLQQEI SDLTEHISES GKTIHELEKG KKMAENEKAE IQTALEEAEA TLEHEESKIL
     RVQLELTQVK GEIDRKIAEK DEEIEQIKRN SQRVMESMQS TLDAEVRSRN DALRVKKKME
     GDLNEMEIQL SHANRQAAEA QKQLRNVQGQ LKDAQLHLDE AVRAQDDMRE QVAIVERRNS
     LMVAEIEELR AALEQTERSR KVAEQELVDA SERVTLLHSQ NTSLINTKKK LEADFVQIQG
     EVEDAIQEAR NAEEKAKKAI TDAAMMAEEL KKEQDTSSHL ERMKKNLEVT VKDLQHRLEE
     AENLAMKGGK KQLQKLEARV RELEGEVEAE QRRGAEAIKG VRKYERRVKE LTYQTEEDKK
     NITRLQDLVD KLQLKVKSYK RQSEEAEEQA NTHLSRYRKV QHELEEAQER ADIAESQVNK
     LRAKSREMTR VQS
//
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