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Database: UniProt
Entry: O42352_CYPCA
LinkDB: O42352_CYPCA
Original site: O42352_CYPCA 
ID   O42352_CYPCA            Unreviewed;      1931 AA.
AC   O42352;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   SubName: Full=Myosin heavy chain {ECO:0000313|EMBL:BAA22068.1};
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962 {ECO:0000313|EMBL:BAA22068.1};
RN   [1] {ECO:0000313|EMBL:BAA22068.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Fast skeletal muscle {ECO:0000313|EMBL:BAA22068.1};
RX   PubMed=9208928; DOI=10.1111/j.1432-1033.1997.t01-2-00380.x;
RA   Hirayama Y., Watabe S.;
RT   "Structural differences in the crossbridge head of temperature-associated
RT   myosin subfragment-1 isoforms from carp fast skeletal muscle.";
RL   Eur. J. Biochem. 246:380-387(1997).
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; D89991; BAA22068.1; -; mRNA.
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; 6.
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   2: Evidence at transcript level;
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}.
FT   DOMAIN          32..81
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          85..776
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          653..675
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1877..1931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          840..1154
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1191..1830
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         178..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1931 AA;  221163 MW;  59466B7BD0872DDD CRC64;
     MGDGEMECFG PAAIYLRKPE RERIEAQTAP FDAKTAFFVT DAAEMYLKST LVSREGGKAT
     VKTHCGKTVT VKEDEIFQMN PPKFDKMEDM AMMTHLNEPS VLFNLKERYA AWMIYTYSGL
     FCATVNPYKW LPVYDAVVVA GYRGKKRIEA PPHIFSISDN AYQFMLTDRE NQSILITGES
     GAGKTVNTKR VIQYFATVAM SGPKKTEAVP GKMQGSLEDQ IIAANPLLEA YGNAKTIRND
     NSSRFGKFIR IHFGTTGKLA KADIETYLLE KSRVTFQLSA ERSYHIFYQL MTGHKPELLE
     ALLITTNPYD YPMISQGEIT VKSIDDVEEF IATDTAIDIL GFTADEKISI YKLTGAVMHH
     GSMKFKQKQR EEQAEPDGNE AADKIAYLLG INSADMLKAL CYPRVKVGNE MVTKGQTVPQ
     VNNAVSALCK SIYEKMFLWM VVRINEMLNT TNPREFYIGV LDIAGFEIFD YNSLEQLCIN
     FTNEKLQQFF NHTMFVLEQE EYKKEGIEWA FIDFGMDLAA CIELIEKPMG IFSILEEECM
     FPKATDTSFK NKLHDQHLGK SAAFQKPKPA KGKPEAHFSL LHYAGTVDYN IAGWLEKNKD
     PLNDSVVQLY QKSALKVLAL LYVAVPEEGG GKKAGKKKGG SFQTVSALFR ENLAKLMTNL
     RSTHPHFVRC LIPNESKTPG LMENFLVIHQ LRCNGVLEGI RICRKGFPSR IHYGDFKQRY
     KILNASVIPE GHFIDNKKAT EKLLGSIDVD HTQYKFGHTK VFFKAGLLGA LEEMRDEKLV
     NLVTMTQALA RGYVMRKEFV KMMERREAIF SIQYNIRSFM NVKHWPWMKV YFKIKPLLKT
     AESEKEMASM KENFEKMKED LTKALAKKKE LEEKMVSLVQ EKNDLLLQVT SESENLCDAE
     ERCEGLIKSK IQLEGKLKET NERLEDEEEI NAELTAKKRK LEDECSELKK DIDDLELTLA
     KVEKEKHATE NKVKNLTEEM ACQDESIAKL TKEKKALQEA HQQTLDDLQA EEDKVNTLTK
     AKTKLEQQVD DLEGSLEQEK KLRMDLERVK RKLEGDLKLA QESIMDLENE KQQSDEKIKK
     KDFEISQFLS KIEDEQSLGA QLQKKIKELQ ARIEELEEEI EAERSARAKV EKQRADLSRE
     LEEISERLEE AGGATAAQIE MNKKREADFQ KMRRDLEEST LQHEATAAAL RKKQADTVAE
     LGEQIDNLQR VKQKLEKEKS EYKMEIDDLT SNMEAVAKAK GNLEKMCRTL EDQLSEIKAK
     SDENSRQLND MNAQRARLQT ENGEFSRQLE EKEALVSQLT RGKQAFTQQI EDLQRHVEEE
     VKAKNALAHA VQSARHDCDL LREQYEEEQE AKTELQRGMS KANSEVAQWR AKYETDAIQR
     TEELEEAKKK LAQRLQDAEE SIEAVSSKCA SLEKTKQRLQ GEVEDLMIDG ERANALAANL
     DKKQRNFDKV LAEWKQKYEE SQAELEAAQK EARSLSTELF KMKNSYEEAL DHLETLKREN
     KNLQQEISDL SEQLGETGKS IHELEKAKKI VESEKAEIQT ALEEAESTLE HEESKILRVQ
     LELNQVKSEI DRKLAEKDEE IEQIKRNSQR VMDSMQSTLD SEIRSRNDAL RVKKKMEGDL
     NEMEVQLSHA NRQAAEAQKQ LRNVQGQLKD AQLHLDEAVR GQEDMKEQVA MVERRNTLMQ
     AEIEELRAAL EQTERGRKVA EQELVDASER VGLLHSQNTS LINTKKKLET DLLQVQGEVD
     DAVQEARNAE EKAKKAITDA AMMAEELKKE QDTSAHLERM KKNMEVTVKD LQHRLDEAES
     LAMKGGKKQL QKLESRVHEL EAEVEAEQRR GADAVKGVRK YERRVKELTY QTEEDKKSVT
     RLQDLVDKLQ LKVKAYKRQA EEAEEQANTH LSRYRKVQHE LEESHERADI AESQVNKLRA
     KSREAGKTKD E
//
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