ID A0A3B0J2M3_DROGU Unreviewed; 1793 AA.
AC A0A3B0J2M3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Blast:Unconventional myosin-Va {ECO:0000313|EMBL:SPP75704.1};
GN ORFNames=DGUA_6G003563 {ECO:0000313|EMBL:SPP75704.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP75704.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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; OUUW01000001; SPP75704.1; -; Genomic_DNA.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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; 3.
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; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 5.
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}.
FT DOMAIN 70..771
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1467..1743
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 650..672
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1102..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 916..957
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 992..1099
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1151..1235
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1265..1317
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1388..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1793 AA; 206924 MW; 801305A7E3D54F5A CRC64;
MSSEEMLYAK GAKIWVTHAE KVWESATLEE NYRKGAGFLK ICTESGSLKE FKLKPDGSNL
PPLRNPAILV GQNDLTTLSY LHEPGVLYNL RVRFCERQII YTYCGIILVA INPYAEMPLY
GPSIIRAYRG QSMGDLEPHI FALAEEAYTK LERENCNLSI IVSGESGAGK TVSAKYAMRY
FAAVGGSESE TQVERKVLAS SPIMEAFGNA KTTRNDNSSR FGKFTKLLFK NQMGVMYLQG
ATVHTYLLEK SRVVYQAQGE RNYHIFYQLC AARAKYPELL LDHQDKFQFL NMGGAPDIER
VSDADQFNET AQAMTVLGFS FQQIAEIVKI LAGILHLGNI EVAKKYTEGS EEEDTDSCEI
SHNDIHLQIT GDLLRVKTED LRRWLVMRQI ESVNEHVLIP NSVEAGQAAR DALAKHIYAK
LFQYIGGVLN KSLNNGSKQC SFIGVLDIYG FETFEVNSFE QFCINYANEK LQQQFNQHVF
KLEQEEYLKE GITWTMIDFY DNQPCIDLIE SRLGVLDLLD EECRMPKGSD ESWAGKLIGK
CSKFPHFEKP RFGSTSFFIK HFSDTVEYDV NGFLEKNRDT VSKELTSVMA MSSMSLVKQV
MALEDIDTLG VDANTTSTLG GRVVISAGRK QVVPSKQHRK TVGSQFQESL ASLISTLHAT
TPHYVRCIKP NDEKIAFKWE TAKIVQQLRA CGVLETVRIS AAGFPSRWLY PDFYMRYQLL
AHRSKIDKND LNQSCRNIVY KWIEDEDKSR FGNTQIFFRA GQVAFLEQVR ANLRKKYITI
VQSVVRRFIY RRRYLRLQMV IRGIQRYARG YMARERVQKM REARAALILS KYAKGWLCRR
RYLRLRHSIA GIQTYARGML ARRKFYALRD NYRAVQIQRF VRGVLARRAY HHKRRNIIIC
QAAVRRFLAR RKFKRMKAEA KTISHMENKY MGLENKIISM QQRIDELNRD NSNLKHKTSE
ISVLKMKLEM KKNLEGEFKN VKAACMDKDM LIAALNKQLE AERDEKMQLL QENGHAQEEW
LTQKQSYCLA NEELRNQVDQ MIEMAKNAEA TQRDQNVRML AEIDNDELNE AYQRAIKDKE
VIENENYQLK EELSRFQQNG VYSQRNRSAS NASSQNEEDV GYASAKNTLD INRSSDLHSK
SHTFVDCTSL VVKLRSILEE EKSKHKVLQD QYIKLASRYK PTEDSFRVSE LEVENEKLRS
EHDQLRTSIK HGVEINELNA QHAALQEEVR RRRDECIQLK AVLLQQNQAL RSFEPESMHL
RGSDVNELLE AFQSQKLVNR QLEDELKAIT EEHNSKLVEM TQEIERLHNE QDELQKVIFE
SIDASEDASV DTLKQNDRYL RRELQKAVAQ FLLVQEELKL ANAKLQAYRQ NGGQLEHKLE
EEMSRSKGSG LSNDVGANVT KQKSQNPQGL MKFHSNDLDK ILQRLLSTMT PRTVVGLLPG
FPAYLIFMCI RYTDLTNADD DVRELLSKFV IQIKKMHRTP HPIENRVIWL VNSITLLNLL
KQYGDVEEYV KLNTEKQNQQ QLKNFNLFEY RRVILDLIVN LYQALIMQIQ GLLDPKIVPA
ILKNDEIQRG RQPHGMRGRT TSIGAVSSPE HGGGPAWKQL IGQLEHFYKQ FQHFGLDNCY
SEQIFQQLLY FVCAVALNCL MLRGDICMWE TGMVIRYNIG CIEDWVHSKK MSNEVLAPLS
PLNQVSQLLQ SRKSEQDVQT ICDLCTSLST AQVLKVMKSY KLDDYENEIT NVFLEKLTKE
LNARQTQKSN SDEFTMDQKF IQPFKVVFRY SDIKLEDIEL PSHLNLDEFL EKI
//
