ID L5LVS0_MYODS Unreviewed; 1696 AA.
AC L5LVS0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Myosin-14 {ECO:0000313|EMBL:ELK30162.1};
GN ORFNames=MDA_GLEAN10005292 {ECO:0000313|EMBL:ELK30162.1};
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:ELK30162.1, 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; KB107319; ELK30162.1; -; Genomic_DNA.
DR eggNOG; KOG0161; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0060473; C:cortical granule; 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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 2.
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; 3.
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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF31; MYOSIN-14; 1.
DR Pfam; PF00063; Myosin_head; 3.
DR Pfam; PF01576; Myosin_tail_1; 3.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 3.
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:UP000010556}.
FT DOMAIN 7..607
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 485..507
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1068..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1605..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1662..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1696 AA; 193641 MW; AB4DFFA232E060AC CRC64;
MNPPKFSKAE DMAELTCLNE ASVLHNLRER YYSGLIYTYS GLFCVVINPY KQLPIYTEAI
VEMYRGKKRH EVPPHVYAVT EGAYRSMLQD REDQSILCTG ESGAGKTENT KKVIQYLAHV
ASSPKGRKEP GVPGKFIRIN FDVAGYIVGA NIETYLLEKS RAIRQAKDEC SFHIFYQLLG
GAGEQLKADL LLEPCSQYRF LTNGPASSPG QERELFQETL ESLRVLGFTH EEITSMLRMV
SAVLQFGNIV LKRERNNDQA SMPDNTAAQK LCRLLGLGVT DFSRALLTPR IKVGRDYVQK
AQTKEQADFA LEALAKATYE RLFRWLAPVP SHAPPPPLLD EECWFPKATD KSFVEKVAQE
QGGHPKFQRP RQLRDQADFS VLHYAGKVDY KANEWLMKNM DPLNDNVAAL LHQSTDRLTA
EIWKDGQQIG PRLQGPEKPG MMRSPKLMEG IVGLEQVSSL GDGPPGGRPR RGMFRTVGQL
YKESLSRLMA TLSNTNPSFV RCIVPNHEKR AGKLEPRLVL DQLRCNGVLE GIRICRQGFP
NRILFQEFRQ RYEILTPNAI PKGFMDGKQA CEKMIQALEL DPNLYRVGQS KIFFRAGVLA
QLEEERDLKV TDIIVSFQAA ARGYLARRAF QKRQQQQSAL RVMQRNCAAY LKLRHWQWWR
LFTKVKPLLQ VTRQDEVLQA RAQELQKVQE LQQQSAREVG ELQSRLTQLE EERTRLAEQL
RAEAELCAEA EETRGRLAAR KQELELVVSE LEARVGEEEE CSRQLQHEKK RLQQHIQELE
THLEAEEGAR QKLQLEKVTT EAKLKKFEED LLLLEDQNTK LSKERRLLEE RLAEFSSQAA
EEEEKVKSLN KLRLKYEATI ADMEDRLRKE EKGRQELEKL KRRLDGESSE LQEQMVEQQQ
RVEELRAQLG RKEEELQAAL ARVEEEGGAR ALLLKSLREA QAGLSEAQED LEAERLARAK
AEKQRRDLGE ELEALRGELE DTLDSTNAQQ ELRSKREQEV TELKKALEEE TRIHEIAVQE
LRQRHGQALG ELAEQLEQAR RGKGVWDKTR LALETEVSEL RAELSNLQAS RQEGEQRRRR
LESQLQEVQG RAGDGERARA EAAEKLQRAQ VELENVSGAL SEAESRAIRL SKELSSTEAQ
LHDAQELLQE ETRAKLALGS RVRALEADVS GLREQLEEEA AARGRAGREL QTAQVQLSEW
RRRQEEEAGA LEGRAELVCH LNPSTSLLCL CLCLSVCLSL SLAAPYSPPP CTLISALLAE
EKAAVLRAVE ERERVEAEGR EREARTLSLT RALEEEQEAR EELERQNRAL RAELEALLSS
KDDVGKSVHE LERARRAAEQ AASDLRTQVT ELEDELTAAE DTKLRLEAQM KELWREVEET
RTSREEIFAQ NRESDKRLKG LEAEVLRLQE ELAASDRARR QAQQERDEMA DDFLGKGSLS
KAAILDEKRQ LEGRLGQMEE ELEEEQSNAE LLGDRYRKLL LQVESLTTEL SAERSFSAKA
ESGRQQLERQ IQELRERLGE EDAGARARQK MTIAALESKL AQAEEQLEQE SRERILSGKL
VRRAEKRLKE VVLQVEEERR VADQLRDQLE KGNLRVKQLK RQLEEAEEEA SRAQAGRRRL
QRELEDVTES AESMNREVTT LRNRLRRGPL TFTTRTVRQV FRLEEGVASD EEAEEAEPGS
GPQPQESDGP QDVQPQ
//
