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Database: UniProt
Entry: L5MCJ0_MYODS
LinkDB: L5MCJ0_MYODS
Original site: L5MCJ0_MYODS 
ID   L5MCJ0_MYODS            Unreviewed;      1821 AA.
AC   L5MCJ0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Myosin-Vc {ECO:0000313|EMBL:ELK36037.1};
GN   ORFNames=MDA_GLEAN10016327 {ECO:0000313|EMBL:ELK36037.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK36037.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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; KB101809; ELK36037.1; -; Genomic_DNA.
DR   eggNOG; KOG0160; Eukaryota.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
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   CDD; cd15476; Myo5c_CBD; 1.
DR   CDD; cd01380; MYSc_Myo5; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 2.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 6.10.220.10; -; 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; IPR002710; Dilute_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR037991; Myo5c_CBD.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR036103; MYSc_Myo5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 5.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 4.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 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:UP000010556}.
FT   DOMAIN          95..149
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          154..843
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1500..1776
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          722..744
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          974..1086
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1116..1188
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1301..1346
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1382..1430
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         248..255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1821 AA;  209920 MW;  506227C59E241142 CRC64;
     MCRGSHCLQP LFLLPDSSHP EASLIVALVS PRTAVLLLDS AAACPLLDRR ACLGTATQLP
     LFQGSKDPGS RTLGQQQSQS QWNVGLESLP EFGGQEYNRV WIPDPEDVWK SAEIAKDYRV
     GDKVLRLLLE DGTELDYSVD PESLPPLRNP DILVGENDLT ALSYLHEPAV LHNLRIRFAE
     SKLIYTYSGI ILVAMNPYKQ LPIYGDAIIH AYSGQNMGDM DPHIFAVAEE AYKQMARNNK
     NQSIIVSGES GAGKTVSARY AMRYFATVSK SNSNAHVEDK VLASNPITEA VGNAKTTRND
     NSSRFGKYTE ISFDERNQII GANMRTYLLE KSRVVFQSEN ERNYHIFYQL CASAQQSEFK
     HLKLGSAEEF NYTRMGGNTV IEGVSDSAGM EETRKTFTLL GFQEDFQMDV FKVLAAILHL
     GNVQITAVGN ERSAVSADDS HLQVFCELLG LERGSVAQWL CNRKIITTSE TVVKPMTRPQ
     AANARDALAK KVYAHLFDFI VERINQALQF SGKQHTFIGV LDIYGFETFD VNSFEQFCIN
     YANEKLQQQF NLHVFKLEQE EYMKEDIPWT LIDFYDNQSV IDLIEAKMGI LELLDEECLL
     PHGTDENWLQ KLYNNFINKN SLFEKPRMSN ASFIIQHFAD KVEYKCEGFL EKNRDTVYDM
     LVEILRASKF HLCAKFFQES PVPPSPFGSA ITMKSAKQVI KPNNKQFRTT VGSKVSGGLG
     SLSLLMETLN ATTPHYVRCI KPNDEKLPFE FDSKRIVQQL RACGVLETIR ISAQSYPSRW
     TYIEFYSRYG ILMTKQELSF GDKKEVCKVV LHRLIQDSNQ YQFGKTKIFF RAGQVAYLEK
     LRLDKLRQGC VVIQKHIRGW LQRKKFLRQR QAALTIQQYF RGQHTVRKAV TAAALKEAWA
     AIIIQKHCRG YLVRSLYQLI RVATITIQAY TRGCLARRRY RKMLEEHKAV ILQKYARAWL
     ARRRFQSIRR FVLNIQLTYR VQRLQKKLED QNRENHGLME KLTSLAAARA GDVEKVQKLE
     SELDRAAAHR RNYEERGQRY KATVEEKLAK LQKHNSELEV QKEQIQRKLQ EQTEELKGKM
     DDLTKQLFED VQKEEQQRIL LEKSFELKTQ DYEKQMCSLK EEVKALKDEK MQLQRQLEEE
     QATSGGLQGE VARLSQQAKT ISEFEKEIEL LQTQKIDVEK HVQSQKREMR EKMSEITKQL
     LESYDIADVR SRLSVEDLEH LNEDGELWFA YEGLKKATRV LESHFQSQKD CYEKEIEALN
     FKVVHLSQEI NHLQKLFREE NDINESIRHE VTRLTSENMM IPDFKQQISE LEKQKQDLEI
     RLNEQTESMR GKLEEFSNEL NHTREEEGIH PEEKEKLMDD IHAMPEVSKG LKKQVETEPK
     VESSLRQDAS RLTMENRDLE EELDMKDRVI KKLQDQVKSL TKTIGKANDV HLSSGPKEYL
     GMLEYKREDE AKLIQNLILD LKPRGVVVNM IPGLPAHILF MCVRYADSLN DASMLKSLMN
     SIINGIKQVV KEHLEDFEML SFWLSNTCHF LNCLKQYSGE EEFMKHNSPH QNKNCLNNFD
     LSEYRQILSD VAIRIYHQFI IVMENNIQPI IVPGMLEYES LQGISGLKPT GFRKRSSSID
     DTDAYTMTSV LQQLSYFYST MCQNGLDPEL VRQAVKQLFF LIGAVTLNSL FLRKDMCSCR
     KGMQIRCNIS YLEEWLKDKN LQNSLAKETL EPLSQAAWLL QVKKITDSDA KEIFERCTSL
     SAVQIIKILN LYTPIDDFEK RVTPSFVRKV QALLNSREDS SQLMLDASYL FQVVFPFTPS
     PHALEMIEIP SSFKLGFLNR L
//
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