ID A0A3B3B3D9_ORYME Unreviewed; 1908 AA.
AC A0A3B3B3D9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Myosin heavy chain, fast skeletal muscle-like {ECO:0000313|Ensembl:ENSOMEP00000000096.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000000096.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000000096.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSOMET00000016428.1; ENSOMEP00000000096.1; ENSOMEG00000002870.1.
DR GeneTree; ENSGT00940000162888; -.
DR Proteomes; UP000261560; 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; -; 6.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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; 2.
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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 86..777
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 655..677
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1554..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1855..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1855..1891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1908 AA; 218560 MW; BE47261635C60F2D CRC64;
MSTDAEMEQY GPAAIYLRKP ERERIEAQTT PFDAKTAFFV VDADEMYVKC KLVKKEGGKA
TVETDGGKTV TVKEDDIHPR NPPKFDKMED MAMMTHLNEP SVLYNLKERY ASWMIYTYSG
LFCVVVNPYK WLPVYDAQCV QGYRGKKRIE APPHIFSISD NAYQFMLTDR ENQSVLITGE
SGAGKTVNTK RVIQYFATIA ALGGKKEQQS SGKIQGSLED QIVAANPLLE AYGNAKTVRN
DNSSRFGKFI RIHFGSSGKL ASADIETYLL EKSRVTFQLS AERSYHIFYQ LMTGHKPELL
EALLITTNPY DFPMISQGEI TVKSINDVEE FIATDTAIDI LGFNAEEKLG IYKLTGAVMH
HGNMKFKQKQ REEQAEPDGT EVADKIAYLM GMNSADMLKA LCYPRVKVGN EMVTKGQTVP
QVNNAVSALC KSVYEKMFLW MVIRINEMLD TKQPRQFFIG VLDIAGFEIF DFNSLEQLCI
NYTNEKLQQF FNHTMFVLEQ EEYKKEGIEW EFIDFGMDLA ACIELIEKPM GIFSILEEEC
MFPKASDTTF KNKLHDQHLG KNKAFEKPKP AKGKAEAHFS LVHYAGTVDY NITGWLDKNK
DPLNDSVVQL YQKSANKLLA FLYAAHASAG GGAKKGGKKK GGSFQTVSAL FRENLAKLMT
NLRSTHPHFV RCLIPNETKT PGLMENFLVI HQLRCNGVLE GIRICRKGFP SRILYGDFKQ
RLAITSLDTL RYPVFFKAGL LGTLEEMRDE KLASLVTMTQ ALCRGYVMRK QFVKMMERRE
SIYTIQYNVR SFMNVKNWPW LKLYFKIKPL LKSAETEKEL QEMKGNYEKM TTDLAAALAK
KKELEEKMVS LLQEKNDLQL QVAAEAENLG DAEERCEGLI KSKIQMEAKL KETTERLEDE
EEINAELTAK KRKLEDECSE LKKDIDDLEL TLAKVEKEKH ATENKVKNLT EEMASQDESI
AKLTKEKKAL QEAHQQTLDD LQAEEDKVNT LTKAKTKLEQ QVDDLEGSLE QEKKLRMDLE
RAKRKLEGDL KLAQESIMDL ENDKQQSDEK IKKKDFEISQ LLSKIEDEQS LGAQLQKKIK
ELQARIEELE EEIEAERAAR AKVEKQRADL SRELEEISER LEEAGGATAA QIEMNKKREA
EFQKLRRDLE ESTLQHESTA AALRKKQADS VAELGEQIDN LQRVKQKLEK EKSEYKMEID
DLSSNMEAVA KAKGNLEKMC RTLEDQLSEI KAKNDENVRQ LNDLNAQRAR LQTENGEFSR
QLEEKEALVS QLTRGKQAFT QQIEELKRLV EEEVKAKNAL AHGVQSARHD CDLLREQFEE
EQEAKAEMQR GMSKANSEVA QWRTKYETDA IQRTEELEEA KKKLAQRLQE AEESIEAVNS
KCASLEKTKQ RLQGEVEDLM IDVERANGLA ANLDKKQRNF DKVLAEWKQK YEESQAELEG
AQKEARSLST ELFKMKNSYE ESLDQLETMK RENKNLQQEI SDLTEQIGET GKSVHELEKA
KKTVETEKSE IQTALEEAEG TLEHEESKIL RVQLELNQVK GEIDRKLAEK DEEMEQIKRN
SQRVTESMQS TLDSEVRSRN DALRIKKKME GDLNEMEIQL SHSNRQAAEA QKQLRNVQGQ
LKDAQLHLDD ALRAQDDMKE QVAMVERRNG LMLAEIEELR AALEQTERGR KVAEQELVDA
SERVGLLHSQ NTSLINTKKK LESDLVQVQG EVDEAIQEAR NAEEKAKKAI TDAAMMSEEL
KKEQDTSAHL ERMKKNLEVT VKDLQHRLDE AENLAMKGGK KQLQKLESRV RELESEVEAE
QRRGAEAVKG VRKYERRVKE LTYQTEEDKK NVTRLQDLVD KLQLKVKAYK RQAEEAEEQA
NTHMSKLRKV QHELEEAQER ADIAEAQVNK LRRKPHHTRG EHADSTQK
//
