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Database: UniProt
Entry: A0A087YKL5_POEFO
LinkDB: A0A087YKL5_POEFO
Original site: A0A087YKL5_POEFO 
ID   A0A087YKL5_POEFO        Unreviewed;      1939 AA.
AC   A0A087YKL5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Myosin heavy chain, fast skeletal muscle-like {ECO:0000313|Ensembl:ENSPFOP00000018568.1};
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:ENSPFOP00000018568.1, 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:ENSPFOP00000018568.1}
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   Ensembl; ENSPFOT00000018590.2; ENSPFOP00000018568.1; ENSPFOG00000018505.2.
DR   GeneTree; ENSGT00940000162888; -.
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: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; -; 4.
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}; Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT   DOMAIN          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          86..782
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          659..681
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1911..1939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          846..1280
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1939 AA;  222248 MW;  8D6925C44D9C6721 CRC64;
     MSGDSEMECF GPAAVYLRKP ERERIEAQNT PFDAKTAYFV TEPTEMYLKG KLVKKEGGKA
     TVEVKGGKSI TVKEDEIFPM NPPKFDKIED MAMMTHLSEP SVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYDAMVV AAYRGKKRIE APPHIFSISD NAYQFMLQDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA VAGGKKSEPI PGKMQGSLED QIIAANPLLE AYGNAKTVRN
     DNSSRFGKFI RIHFGTTGKL ASADIETYLL EKSRVTFQLS AERSYHIFYQ LATGHKPELI
     AEGLLITTNP 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 GSINIDHTQY RFGHTKVFFK AGLLGTLEEM
     RDEKLAELVT MTQALCRGYV MRREFVKMME RREAIFTIQY NIRSFMNVKT WPWMKLYFKI
     KPLLKSAETE KEMAQMKEDF AKTKEDLTKA LAKKKELEEK MVSLLQEKND LQLQIQSEGE
     TLADAEERCE GLIKAKIQLE AKLKETNERL EDEEEINAEL TAKKRKLEDE CSELKKDIDD
     LELTLAKVEK EKHATENKVK NLTEEMASQD ETIAKLTKEK KALQEAHQQT LDDLQAEEDK
     VNTLTKAKTK LEQQVDDLEG SLEQEKKLRM DLERAKRKLE GDLKLAQETT MDLENDKQQS
     EEKIKKRDFE ISQLLSKIED EQTIGSQLQK KIKELQARIE ELEEEIEAER AARAKVEKQR
     ADLSRELEEI SERLEEAGGA TAVQIEMNKK REAEFQKLRR DLEEATLQHE ATAASLRKKQ
     ADSVAELGEQ IDNLQRVKQK LEKEKSEYKM EIDDLSSNME STAKAKVNME KMCRSLEDQL
     SELKTKNDEH IRQLNEINSH KARLVSENGE ISRQLEEKES LVSQLTRGKQ AFMHQIEELK
     RHLEEEVKAK NALAHAVQSS RHDCDLLREQ YEEEQEAKAE LQRAMSKANS EVAQWRTKYE
     TDAIQRTEEL EEAKKKLAQR LQDAEESIEA VNAKCASLEK TKQRLQGEVE DLMIDVERAN
     ALAANLDKKQ RNFDKVLAEW KQKYEESQAE LEGAQKEARS LSTEMFKMKN SYEEALDHLE
     TLKRENKNLQ QEISDLTEHI SETGKTIHEL EKGKKTAENE KVEIQTALEE AEATLEHEES
     KILRVQLELT QVKSEIDRKL AEKDEEIEQI KRNSQRVMES MQSTLDAEVR SRNDALRIKK
     KMEGDLNEME IQLSHANRQA AEAQKQLRNV QGQLKDAQLH LDEAVRAQDD MKEQVAMVER
     RNTLMVAEIE ELRAALEQTE RSRKVAEQEL VDASERVTLL HSQNTSLINT KKKLEADFVQ
     VQGEVEDAIQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNL EVTVKDLQHR
     LEEAENLALK GGKKQLQKLE ARVRELEGEV EAEQRRGAEA IKGVRKYERR VKELTYQTEE
     DKKNIARLQD LVDKLQLKVK SYKRQSEDAE EQANAHLSRY RKVQHELEEA QERADIAESQ
     VNKLRAKSRE MGRGKEAEE
//
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