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Database: UniProt
Entry: A0A154P7I5_DUFNO
LinkDB: A0A154P7I5_DUFNO
Original site: A0A154P7I5_DUFNO 
ID   A0A154P7I5_DUFNO        Unreviewed;      1568 AA.
AC   A0A154P7I5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Unconventional myosin-Va {ECO:0000313|EMBL:KZC07080.1};
DE   Flags: Fragment;
GN   ORFNames=WN55_08462 {ECO:0000313|EMBL:KZC07080.1};
OS   Dufourea novaeangliae (Sweat bee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Halictidae; Rophitinae; Dufourea.
OX   NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC07080.1, ECO:0000313|Proteomes:UP000076502};
RN   [1] {ECO:0000313|EMBL:KZC07080.1, ECO:0000313|Proteomes:UP000076502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0120121106 {ECO:0000313|EMBL:KZC07080.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KZC07080.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Dufourea novaeangliae.";
RL   Submitted (JUL-2015) 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; KQ434822; KZC07080.1; -; Genomic_DNA.
DR   STRING; 178035.A0A154P7I5; -.
DR   Proteomes; UP000076502; 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; 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; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
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; 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:UP000076502}.
FT   DOMAIN          60..751
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1523..1568
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          630..652
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1116..1165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1407..1454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          903..1078
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1172..1263
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1309..1395
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1116..1135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1407..1425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1431..1451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         153..160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KZC07080.1"
FT   NON_TER         1568
FT                   /evidence="ECO:0000313|EMBL:KZC07080.1"
SQ   SEQUENCE   1568 AA;  181217 MW;  FD5BD8BC5C414341 CRC64;
     GGRVWVPHLE KVWEGAVLLE DYKLNQPTLK VHTDDSNQTK TLEIKSDTDL PPLRNPDILI
     GENNLTSLSF LHEPAVLYNL QIRFSRHCIY TYCGIVLVAF NPYNELPIYG NDTIWAYRGQ
     AMGDLEPHIF AVAEEAYTKL EREGHDQSII VSGESGAGKT VSAKYTMRYF ATVGGSTTET
     QVEKKVLASL PIMEAIGNAK TTRNDNSSRF GKFIEIQFNR HYHITGASMR TYLLEKSRVV
     FQANEERNYH IFYQMCAATS RLPHLHLGHQ NQFHYLNQGY NPVIDGVDDL ACFDETITAL
     TMLGFTSKQQ DDMLRILAAI MHLGNVNIKS SETQNSSDEN DTEASYISPS DKHLLTICEL
     LGTDMNAMRK WLCHRKIVSM REVFLKPMHV EQAIGARDAL AKHIYAELFN WIVTGINRSL
     QSQNKPQCFI GVLDIYGFET FEINSFEQFC INYANEKLQQ QFNQHVFKLE QEEYLREEIE
     WTFIDFYDNQ PCIDLIETKL GILDLLDEEC RMPKGSDSSW AEKLYAKCGK SKHFEKPRFG
     TSAFLIHHFA DLVRYETTGF LEKNRDTVIE EQVDALRNGD NKLLKKLLSE EDPKLMVPPN
     VRVKVSAQKP MSVTPKQNKK TVGSQFRDSL NMLMATLNAT TPHYVRCIKP NDTKEAFEYN
     PVRAVQQLRA CGVLETIRIS AAGFPSQRTY NDFFLRYRSL CRFKDIRRDD LKETCRRILA
     RYIKDEDKFK FGKSKVLFRA GQVAYLEKLR AERQRDACVI IQKTVRGLIC RNRYRKIRRA
     VLGLQRYGRG YIARQKAQAV REERAAIKIQ ARVKGWLKRR RYLQIKRTVM GIQMYGRGKM
     ARERYKVMKD NAAAITIQRF CRGYLVRMAC KKKVENIVIV QACVRRYMAK KVFRRLKAEA
     RSVEHVKSLN KGLEKKIITL QQKNTELSKE NQTLKNVQNE MVDLKHKLEG LKSVEVENRK
     LNITLLEKEK ELEKMQDVIK IERDEKMDIL QEKERSTQEK TQENKKLEEE IEKLRKDLSV
     ASEKLKNNQR GAEENLKHRL EQEKDLLLLD QDQDRGAYQR LLKEYHELEQ HAELLEQKLA
     MHAPAHSRSL SNASSSSGQI VSTELAQDDQ NLDLGYGSVR STASSSAPYS RVETIDWSQH
     RSDSPPDGEV QTHKSPPETN GPAHAPVDIG LVLKLQQRLK DVEKEKGRLI RMVEDLERDN
     PEETSRTQDT FRLQELEMEN AQLKKDLGSL RKNVSSAGLT GAQQSLMGQF DALQEELERR
     REECIQLHSV LADNTRRMKS LGSNYGRDVD IINEDGELVL AFETQKKINR QLEDELQTKE
     KGWREQRNEW RAEIDRLQEE IEKQQKLLSV NVSKSPQTQT EAFMQHEIAR VTTENLELQE
     KHDKVAEECR RFKKQCRILA KRLRDAGYEG DDSKEHKDRP RVPKGAVPDT TEPASDSTIM
     SSTSHSGENG SNMPAIRKKE RDYEGMFEFR KEDINVVMRH LVIDLNPRIA VTLLPGLPAY
     ILFMCIRHTD CINDDEKVRL LLTAYLNAVK RVVKKREDFD SGVLWLSNTL RLLHSMKQYS
     GDKPFQIE
//
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