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Database: UniProt
Entry: A0A3B4YPF2_SERLL
LinkDB: A0A3B4YPF2_SERLL
Original site: A0A3B4YPF2_SERLL 
ID   A0A3B4YPF2_SERLL        Unreviewed;      1935 AA.
AC   A0A3B4YPF2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Myosin heavy chain, fast skeletal muscle {ECO:0000313|Ensembl:ENSSLDP00000031572.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000031572.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000031572.1}
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; 1841481.ENSSLDP00000031572; -.
DR   Ensembl; ENSSLDT00000032477.1; ENSSLDP00000031572.1; ENSSLDG00000024220.1.
DR   GeneTree; ENSGT00940000162888; -.
DR   Proteomes; UP000261360; 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; SM00015; IQ; 1.
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   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..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   COILED          843..1833
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1862..1924
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   1935 AA;  221921 MW;  B427A0E5BAF4A4FB CRC64;
     MGDSEMECFG PAAIYLRKPE RERIEAQNTP FDAKTAYFVS EPAEMYLKGK LVKREGGKAT
     VETLCGKSIT VKDDAIFPMN PPKFDKIEDM AMMTHLSEPS VLYNLKERYA AWMIYTYSGL
     FCVTVNPYKW LPVYDSVVVA GYRGKKRVEA PPHIFSISDN AYQFMLTDRE NQSILITGES
     GAGKTVNTKR VIQYFATIAV ASGKKATESA GKMQGSLEDQ IIAANPLLEA YGNAKTVRND
     NSSRFGKFIR IHFGTTGKLA SADIETYLLE KSRVTFQLSA ERSYHIFYQL MTGHKPELIE
     ALLITTNPYD YSMISQGEIT VKSINDIEEF IATDTAIDIL GFTAEEKASM YKLTGAVIHH
     GNMKFKQKQR EEQAEPDGTE VADKIAYLMG LNSADLLKAL CYPRVKVGNE YVTKGQTVPQ
     VNNSVMALCK SVYEKMFLWM VVRINEMLDT RQPRSYFIGV LDIAGFEIFD FNSLEQLCIN
     FTNEKLQQFF NHHMFVLEQE EYKKEGIEWE FIDFGMDLAA CIELIEKPMG IFSILEEECM
     FPKATDMTFK NKLYDQHLGK NKSFEKPKPA KGKAEAHFSL VHYAGTVDYN ICGWLDKNKD
     PLNDSVVQLY QKSSVKLLGH LYAAHAGAEA EGGGKKAGKK KGGSFQTVSA LFRENLGKLM
     TNLRSTHPHF VRCLIPNESK TPGLMENFLV IHQLRCNGVL EGIRICRKGF PSRILYGDFK
     QRYKVLNASV IPEGQFIDNK KASEKLLGSI DVDHTQYKFG HTKVFFKAGL LGTLEEMRDE
     KLAALVTMTQ ALCRGYLMRR EFVKMMERRE AIFSIQYNIR SFMNVKTWPW MKLYFKIKPL
     LKSAETEKEM AQMKEDFEKT KEDLTKALAK KKELEEKMVS LLQEKNDLLL QVQSEGENLT
     DAEERCEGLI KAKIQLEAKL KETTERLEDE EEMNAELTAK KRKLEDECSE LKKDIDDLEL
     TLAKVEKEKH ATENKVKNLV EEMASQDETI AKLTKEKKAL QEAHQQVLDD LQAEEDKVNT
     LTKAKTKLEQ QVDDLEGSLE QEKKLRMDLE RAKRKLEGDL KLAQESIMDL ENDKQQSEEK
     IKKKDFEISQ LLGKIEDEQS LGIQLQKKIK ELQARIEELE EEIEAERAAR AKVEKQRSDL
     SRELEEISER LEEAGGATAA QIEMNKKREA EFQKLRRDLE ESTLQHEATS AALRKKQADS
     VAELGEQIDN LQRVKQKLEK EKSEFKMEID DLSSNMESIA KSKGNLEKLC RTLEDQLSEL
     KSKNDENVRQ LNDFSVQKAR LQTENGEIVR QLEEKEALVS QLTRGKQAFT QQIEELKRHI
     EEEVKAKNAL AHAVQSARHD CDLLREQYEE EQEAKAELQR ALSKANSEVA QWRTKYETDA
     IQRTEELEDA KKKLAQRLQD AEESIEAVNA KCASLEKTKQ RLQGEVEDLM IDVERANALA
     ANLDKKQRNF DKVLAEWKQK YEESQAELEG SQKEARSLST EMFKLKNSYE ESLDHLETIK
     RENKNLQQEI SDLTEQIGES GKTIHELEKA KKTAETEKTE LQTSLEEAEA TLEHEESKIL
     RIQLELTQVK SEIDRKLAEK DEEIEQIKRN SQRVIESMQT TLDAEVRSRN DALRIKKKME
     GDLNEMEIQL SHANRQAAEA QKQLRNVQGQ LKDAQLHLDE AIRGHEEMKE QVAMVERRNN
     LMLAEIEELR VALEQTERGR KVAEQELVDA SERVGLLHSQ NTSLINTKKK LEADLIQIQG
     EVEDSVQEAR NAEEKAKKAI TDAAMMAEEL KKEQDTSGHL ERMKKNLEVT VKDLQHRLDE
     AENLAMKGGK KQLQKLEARV RELEAEVDAE QRRGADAIKG VRKYERRVKE LTYQTEEDRK
     NIGRLQDLVD KLQLKVKSYK RQAEEAEEQA NSHLSRYRRV QHEMEEAQER ADIAESQVNK
     LRAKSREIVK VKITT
//
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