ID A0A3Q3GBP9_9LABR Unreviewed; 1937 AA.
AC A0A3Q3GBP9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Myosin heavy chain, fast skeletal muscle {ECO:0000313|Ensembl:ENSLBEP00000029049.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000029049.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000029049.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; 56723.ENSLBEP00000029049; -.
DR Ensembl; ENSLBET00000030418.1; ENSLBEP00000029049.1; ENSLBEG00000021948.1.
DR GeneTree; ENSGT00940000162888; -.
DR InParanoid; A0A3Q3GBP9; -.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000261660; Unplaced.
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; -; 5.
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; 4.
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:UP000261660}.
FT DOMAIN 33..83
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 87..780
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 657..679
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1882..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..1658
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 180..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1937 AA; 222026 MW; CC3F3631080D3352 CRC64;
MSTDAEMQQY GPAAIYLRKP ERERIEAQNS PFDAKTAYFV VHPEEMYLKG KLTKKEGGKA
TVETLTGGKT ITVKEDDIHP MNPPKYDKIE DMAMMTHLNE PCVLYNLKER YASWMIYTYS
GLFCVVVNPY KWLPVYDSVV VNAYRGKKRI EAPPHIFSIS DNAYQFMLTD RENQSILITG
ESGAGKTVNT KRVIQYFATI AVAGAKKAET PGKMQGSLED QIIAANPLLE AYGNAKTVRN
DNSSRFGKFI RIHFGTSGKL ASADIETYLL EKSRVTFQLS AERSYHIFYQ LMTGHKPELL
EALLITTNPY DYHMISQGEI TVKSIDDVEE FIATDTAIDI LGFTAEEKMG IFKLTGAVMH
HGNMKFKQKQ REEQAEPDGT EVADKIAYLL GLNSADMLKA LCYPRVKVGN EMVTKGQTVP
QVNNSVSALC KSIYEKMFAW MVVRINEMLD TKQPRQFFIG VLDIAGFEIF DYNSLEQLCI
NFTNEKLQQF FNHHMFVLEQ EEYKKEGIDW EFIDFGMDLA ACIELIEKPM GIFSILEEEC
MFPKASDTTF KNKLHDQHLG KTKAFEKPKP GKGKAEAHFS LVHYAGTVDY NITGWLDKNK
DPLNDSVVQL YQKSSNKLLA LLYVAHAGAE EAAGGKKGGK KKGGSFQTVS ALFRENLGKL
MTNLRSTHPH FVRCLIPNET KTPGLMENFL VIHQLRCNGV LEGIRICRKG FPSRILYGDF
KQRYKVLNAS VIPEGQFIDN KKASEKLLGS IDVDHTQYKF GHTKVFFKAG LLGTLEEMRD
DKLAELVTMT QALARGYVMR KAFVKMMERR ESIFSIQYNI RSFMNVKNWP WLKLYFKIKP
LLKSAETEKE LHQMKENYDK MQSDLTTALA KKKELEEKMV SLLQEKNDLQ LQVASEFDNL
SDAEERCEGL IKSKIQLEAK LKETAERLED EEEINAELTA KKRKLEDECS ELKKDIDDLE
LTLAKVEKEK HATENKVKNL TEEMASQDES IAKLTKEKKA LQEAHQQTLD DLQAEEDKVN
TLTKAKTKLE QQVDDLEGSL EQEKKLRMDL ERAKRKLEGD LKLALESIMD LENDKQQSDE
KIKKKDFEIS QLLSKIEDEQ SLGAQLQKKI KELQARIEEL EEEIEAERAA RAKVEKQRAD
LSRELEEISE RLEEAGGATA AQIEMNKKRE AEFQKMRRDL EESTLQHEAT SAALRKKQAD
SVAELGEQID NLQRVKQKLE KEKSEFKMEI DDLSSNMEGV AKAKGNLEKM CRTLEDQLSE
LKTKNDENVR QLNDMNAQKA RLQTENGEYS RQLEEKEALV SQLTRGKQAF TQQIEELKRH
VEEEVKAKNA LAHAVQSARH DCDLLREQYE EEQEAKTELQ RGMSKANSEV AQWRSKYETD
AIQRTEELEE AKKKLAQRLQ DAEETIEAVN SKCASLEKTK QRLQGEVEDL MIDVERANAL
AANLDKKQRN FDKVLAEWKQ KYEESQAELE GALKESRSLS TELFKMKNSY EETLDHLETM
KRENKNLQQE VSDLTEQIGE TGKTIHELEK SKKITETEKA EIQSALEEAE GTLEHEEAKI
LRIQLELNQV KGEVDRKLAE KDEEMEQIKR NSQRVIDSMQ STLDAEIRSR NDALRIKKKM
EGDLNEMEIQ LSHANRQAAE SQKQLRNVQG QLKDAQLHLD DAIRGQEDMK EQVAMVERRN
GLMLAEIEEL RVALEQTERG RKVAEQELVD ASERVGLLHS QNTSLINTKK KLEADFVQVQ
SEVDDAVQEA RNAEDKAKKA ITDAAMMAEE LKKEQDTSAH LERMKKNLEV TVKDLQHRLD
EAENLAMKGG KKQLQKLESR VRELEAEVEA EQRRGSEAVK GVRKYERRVK ELTYQTEEDK
KNVGRLQDLV DKLQLKVKSY KRQAEDAEEQ ANTHMSRLRK VQHEMEESQE RADIAESQVN
KLRAKSRDLG KVTLLFE
//
