ID E9H736_DAPPU Unreviewed; 1820 AA.
AC E9H736;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Unconventional myosin-Va {ECO:0008006|Google:ProtNLM};
GN ORFNames=DAPPUDRAFT_308269 {ECO:0000313|EMBL:EFX72449.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX72449.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX72449.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; GL732599; EFX72449.1; -; Genomic_DNA.
DR STRING; 6669.E9H736; -.
DR EnsemblMetazoa; EFX72449; EFX72449; DAPPUDRAFT_308269.
DR KEGG; dpx:DAPPUDRAFT_308269; -.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_9_1_1; -.
DR InParanoid; E9H736; -.
DR OMA; GKSKHFE; -.
DR PhylomeDB; E9H736; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd15470; Myo5_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 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; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 6.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
DR PROSITE; PS51456; MYOSIN_MOTOR; 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|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:UP000000305}.
FT DOMAIN 66..781
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1484..1772
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 655..677
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1096..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1590..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 933..960
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1166..1235
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1305..1405
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1096..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1820 AA; 209569 MW; 5A9FE1138BE40BEE CRC64;
MSTAVLYTKG AKVWLPDAID VWKIGEILED FKSDSLKLLL DTRETIELNV KESKDLPPLR
NPEFLIGGND LTSLSYLHEP AVLHTLKVRF MNYNAIYTYC GIVLVAINPY QELSIYSQDT
VLAYRNRNQY GSLDPHIFAV AEEAFTKMER ESQDQSIIVS GESGAGKTVS AKYAMRYFAT
AGGSATETQV ERKVLASSPI MEAIGNAKTT RNDNSSRFGK YIELGFNKDY HIQGAGMRTY
LLEKSRVVFQ SAEERNYHIF YQLCAASSLP EMAYLQLQHQ DHFSYTRKGN CPTIDGVDDL
AEFQETRRAL TLLGFSEDQQ ADMFRVFAGL LHLGNVTIVD ADHEGSNIPK TDTYLASFCS
LMGLDVASSE ELRKWLCFRQ IVSMKEVFTK PMTKAEASFA RDALAKHIYS LLFQKIVTMI
NKSLASSSRP HRFIGVLDIY GFETFEWNSF EQFCINYANE KLQQQFNQHV FKLEQEEYVR
EKIDWTFIDF YDNQPCIDLI EKPLGILDLL DEECRVPKGA DNAWVEKLYT QCKKYEQFVK
PRLSNTGFII VHFADRVEYQ CAGFVEKNRD TVLEEQVQVL RSSSNGIVRQ LIVDEESIVG
ARSPAAAAAG SRSVVGTVPR GGGSLLVPGG GPGRQTNTMT KQNRRTVGSQ FRESLTLLMN
TLNATTPHYV RCIKPNDSKE SFVFEPRRAV QQLRACGVLE TVRISAAGFP SRLTYEEFIV
RYRVLFHSRQ CQRKLRDLSV QRESCETVLA TLITEDDKFK FGASKIFFRA GQVAYLEKRR
TDKLRACGIL IQRMIRGWFY RKRYVKLRMA VVGVQRFCRG YLARCKAQRL RETRSAIVIQ
KHVRGFLKRR SYTRLRENVL RLQTYGRGFL ARKRYLQLVC NAKAVMIQKM VRGFLARRRY
LRARKSIVLL QCCWRRWLAR RQYKALRLEA RSIEHVKNLN KGLENKIISM QQRIEEMNKE
LIPLRQKQND YVELKTQCEA NRGLANELKV SVGRIGELEL LVKQLQIQLD RERDEKMDLV
QERERVEKQN EELNARIENI QKELVESTEI NQTRSQEAEE SILRRLDQER AMLAQEYDQE
RAAYQKLLQD YHELEERMEE AERERLHEEP GKSSKSETIR GHSRNASNVS TLSNTSELIA
DPEDDGGYGS VRHVPNRSDS EDVGLVLKLQ QRLKTVEKDK ASLATRVEEL ECESPTADVR
RAQDMIRLQE LEMENAKIKD DLKNLRRQAA TENEVQLPRS LDMLMSQFDA MSDELDRRRE
ECIQLRTVLA NTTLGGDIGE QSTLNASRLN GGEPFAEDNE ILMAFESQKR IIRHLENELQ
EEKASSQRKI QIEREEVERL RLDNEQQAKL LAGALHRTPQ GQTDAVMQHE ISRLTADNLD
LQEKNDLLSE QLKKYRSQMK LAKKVKQEGV PAENQEASPE ETNYLGMFDF NMGDEKQIAR
NLVYELKPRV ASTLLPGLPA YIIFMCVRHA DYINNDEKIR SFLTLIINAI RRLIKKRYED
LDTSVVWLVN TCRLLHSLKQ YSGEKAFQEE NTPKQNEQCL RNFDLSEYRQ VLSDIAVWIY
QAVIKFMEER VQQLIVTAVL EHEAISGLSS HKQPVGQSGR ARSGSTRDTT SPVDPQEAIA
HLLRELTIFH QVLQLYGVDP TLIAQAFRQV FYYICACALN NLLLRKEMCH WSKGIQIRYN
ISHLEQWVRD QHIHGQDTMS ATIVDTLQPI IQAAQLLQAR KSDDDVSNIC TMCSRLTSAQ
IIKILNLYTP ADELEDRIPI SFIRKVQEEL QKRTDHQSQS KLLMDTKHAF TVRFPYSPSS
IKLEDIDIPA VLNLPMLKKV
//
