ID Q5NTZ3_CYPCA Unreviewed; 1931 AA.
AC Q5NTZ3;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Myosin heavy chain {ECO:0000313|EMBL:BAD82813.1};
GN Name=MYH {ECO:0000313|EMBL:BAD82813.1};
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:BAD82813.1};
RN [1] {ECO:0000313|EMBL:BAD82813.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15777658; DOI=10.1016/j.gene.2004.11.040;
RA Muramatsu-Uno M., Kikuchi K., Suetake H., Ikeda D., Watabe S.;
RT "The complete genomic sequence of the carp fast skeletal myosin heavy chain
RT gene.";
RL Gene 349:143-151(2005).
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; AB182405; BAD82813.1; -; Genomic_DNA.
DR SMR; Q5NTZ3; -.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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-13; 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}.
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 1878..1931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 840..1154
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; 220988 MW; 8F8322F65A26AC77 CRC64;
MGDGEMECFG PAAIYLRKPE KERIEAQTAP FDAKTAFFVT DAAEMYLKST LVSREGGKAT
VKTHCGKTVT VKEDEIFQMN PPKFDKMEDM AMMTHLNEPS VLFNLKERYA AWMIYTYSGL
FCATVNPYKW LPVFDAIVVA GYRGKKKIEA PPHIFSISDN AYHSMLTDRE NQSILITGES
GAGKTVNTKR VIQYFATVAM SGPKKTEAVP GKMQGSLEDQ IIAANPLLEA YGNAKTIRND
NSSRFGKFIR IHFGTTGKLA KADIETYLLE KSRVTFQLSA ERSYHIFYQL MTGHKPELLE
ALLITTNPYD YPMISQGEIT VKSIDDVEEF IATDTAIDIL GFTADEKISI YKLTGAVMHH
GAMKFKQKQR EEQAEPDGNE AADKIAYLIG INSADMLKAL CYPKMKVGNE MVTKGQTVPQ
VNNAVSALCK SIYEKMFLWM VVRINEMLNT TNPREFYIGV LDIAGFEIFD YNSLEQLCIN
FTNEKLQQFF NHTMFVLEQE EYKKEGIEWA FIDFGMDLAA CIELIEKPMG IFSILEEECM
FPKATDTSFK NKLHDQHLGK SAAFQKPKPA KGKPEAHFSL VHYAGTVDYN IAGWLEKNKD
PLNDSVVQLY QKSALKVLAL LYVAVPEEGG GKKAGKKKGG SFQTVSALFR ENLAKLMSNL
RSTHPHFVRC LIPNESKTPG LMENFLVIHQ LRCNGVLEGI RICRKGFPSR IHYGDFKQRY
KILNASVIPE GQFIDNKKAT EKLLGSIDVD HTQYKFGHTK VFFKAGLLGA LEEMRDEKLV
NLVTMTQALA RGYVMRKEFV KMMERREAIF SIQYNIRSFM NVKHWPWMKV YFKIKPLLKS
AESEKEMASM KENFEKMKED LTKALAKKKE LEDKMVSLVQ EKNDLLQQVT SESENLCDAE
ERCEGLIKSK IHLEGKLKET NERLEDEEEI NAELTAKKRK LEDECSELKK DIDDLELTLA
KVEKEKHATE NKVKNLTEEM ASQDESIAKL TKEKKALQEA HQQTLDDLQA EEDKVNTLTK
AKAKLEQQVD ELEGSLEQEK KLRMDLERVK RKLEGDLKLA QESIMDLENE KQQSDEKIKK
KDFEISQFLS KIEDEQSLGA QLQKKIKELQ ARIEELEEEI EAERAARAKV EKQRADLSRE
LEEISERLEE AGGATAAQIE MNKKREADFQ KMRRDLEEST LQHEATAAAL RKKQADTVAE
LGEQIDNLQR VKQKLEKEKS EYKMEIDDLT SNMEAVAKAK GNLEKMCRTL EDQLSEIKAK
SDENSRQLND MNAQRARLQT ENGEFSRQLE EKEALVSQLT RGKQAFTQQI EDLKRHVEEE
VKAKNALAHA VQSARHDCDL LREQYEEEQE AKTELQRGMS KANSEVAQWR AKYETDAIQR
TEELEEAKKK LAQRLQDAEE SIEAVSSKCA SLEKTKQRLQ GEVEDLMIDG ERANALAANL
DKKQRNFDKV LAEWKQKYEE SHAELEAAQK EARSLSTELF KMKNSYEEAL DHLETLKREN
KNLQQEISDL SEQLGETGKS IHELEKAKKI VESEKAEIQT ALEEAESTLE HEESKILRVQ
LELNQVKSEI DRKLAEKDEE IEQIKRNSQR VMDSMQSTLD SEIRSRNDAL RVKKKMEGDL
NEMEVQLSHA NRQAAEAQKQ LRNVQGQLKD AQLHLDEAVR GQENMKEQVA MVERRNTLMQ
AEIEELRAAL EQTERGRKVA EQELVDASER VGLLHSQNTS LINTKKKLET DLLQVQGEVD
DAVQEARNAE EKAKKAITDA AMMAEELKKE QDTSAHLERM KKNMEVTVKD LQHRLDEAES
LAMKGGKKQL QKLESRVHEL EAEVEAEQRR GADAVKGVRK YERRVKELTY QTEEDKKNVT
RLQDLVDKLQ LKVKAYKRQA EEAEEQANTH LSRYRKVQHE LEESHERADI AESQVNKLRA
KSREAGKTKD E
//
