ID A0A096LSV8_POEFO Unreviewed; 1829 AA.
AC A0A096LSV8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Myosin heavy chain, fast skeletal muscle-like {ECO:0000313|Ensembl:ENSPFOP00000022249.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000022249.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000022249.1}
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 EMBL; AYCK01000446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 48698.ENSPFOP00000022249; -.
DR Ensembl; ENSPFOT00000028128.1; ENSPFOP00000022249.1; ENSPFOG00000018505.2.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000162888; -.
DR OMA; RDAIYVI; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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; 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; 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; 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 PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-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}; Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT DOMAIN 1..672
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 549..571
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1796..1829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1829 AA; 209691 MW; AA0219BD6DF440FC CRC64;
MSHCLTQTYS GLFCVTVNPY KWLPVYDAMV VAAYRGKKRI EAPPHIFSIS DNAYQFMLQD
RENQSILITG ESGAGKTVNT KRVIQYFATI AVAGGKKSEP IPGKMQGSLE DQIIAANPLL
EAYGNAKTVR NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL SAERSYHIFY
QLATGHKPEL IEGLLITTNP YDFPMISQGE ITVKSINDVE EFIATDTAID ILGFTAEEKA
NIYKLTGAVM HHGNMKFKQK QREEQAEPDG TEVADKIAYL MGLNSADMLK ALCYPRVKVG
NEMVVKGQTV PQVNNAVSAL CKSVYEKMFL WMVVRINEML DTKQPRSYFI GVLDIAGFEI
FDFNSLEQLC INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP
LGIFSMLEEE CIVPKATDMT FKSKLYDQHL GKSAPFQKPK PAKGKAEAHF SLVHYAGTVD
YNVVGWLDKN KDPLNDSVVQ LYQKSSSKLL AHLYASHAGA DDAKGGKKGG GKKKGGSFQT
VSALFRENLG KLMTNLRSTH PHFVRCLIPN ESKTPGLMEN FLVIHQLRCN GVLEGIRICR
KGFPSRILYG DFKQRYKVLN ASVIPEGQFI DNKKASEKLL GSIDVDHTQY KFGHTKVFFK
AGLLGVLEEM RDEKLAELVT MTQAVCRGFL MRREFVKMME RRDAIFTIQY NIRAFMNVKT
WPWMKLYFKI KPLLKSAETE KEMAQMKEDF AKTKEDLTKA LAKKKELEEK MVSLLQEKND
LLLQVQSESE NLTDAEERCE GLIKAKIQLE AKLKETNERL EDEEEINAEL TAKKRKLEDE
CSELKKDIDD LELTLAKVEK EKHATENKVK NLTEEMASQD ETIAKLTKEK KALQEAHQQT
LDDLQAEEDK VNTLTKAKTK LEQQVDDLEG SLEQEKKLRM DLERAKRKLE GDLKLAQESI
MDLENDKQQS EEKIKKKDFE ISQLLNKIED EQSLGVQLQK KIKELQARIE ELEEEIEAER
AARAKVEKQR ADLSRELEEI SERLEEAGGA TAAQIEMNKK REAEFQKLRR DLEEATLQHE
ATAAALRKKQ ADSVAELGEQ IDNLQRVKQK LEKEKSEYKM EIDDLSSNME SIAKAKGNLE
KMCRTLEDQL SELKAKYDEN IRQLNDIGAQ RARLQTENGE FARQLDEKEA LVSQLTRGKQ
AYTQQIEELK RHIEEEVKAK NALAHAVQSS RHDCDLLREQ YEEEQEAKAE LQRAMSKANS
EVAQWRTKYE TDAIQRTEEL EEAKKKLAQR LQDAEESIEA VNAKCASLEK TKQRLQGEVE
DLMIDVERAN ALAANLDKKQ RNFDKILAEW KQKYEESQAE LEGAQKEARS MSTELFKMKN
SYEEALDHLE TLKRENKNLQ QEISDLTEQL GETGKTIHEL EKGKKTVESE KSEIQTALEE
AEATLEHEES KILRIQLELT QVKSEIDRKL AEKDEEIEQI KRNSQRVMES MQSTLDAEVR
SRNDALRIKK KMEGDLNEME IQLSHANRQA AEAQKQLRNI QGQLKDAQLH LDEAVRGQED
MREQVAMVER RNNLMVAEIE ELRAALEQTE RSRKVAEQEL VDASERVTLL HSQNTSLINT
KKKLESDFVQ IQGEVEDSVQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNL
EVTVKDLQHR LDEAENLAMK GGKKQLQKLE ARVRELEGEV ESEQRRGVEA IKGVRKYERR
VKELTYQTEE DKKNIVRLQD LVDKLQLKVK AYKRQAEEAE EQANAHLTRY RKVQHEMEEA
QERADIAESQ VNKLRAKSRE IGKAKESEE
//
