ID B3P784_DROER Unreviewed; 1288 AA.
AC B3P784;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=GG12368 {ECO:0000313|EMBL:EDV53904.1};
GN Name=Dere\GG12368 {ECO:0000313|EMBL:EDV53904.1};
GN ORFNames=Dere_GG12368 {ECO:0000313|EMBL:EDV53904.1};
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000313|EMBL:EDV53904.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53904.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [2] {ECO:0000313|EMBL:EDV53904.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53904.1};
RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT "Assembly reconciliation.";
RL Bioinformatics 24:42-45(2008).
RN [3] {ECO:0000313|EMBL:EDV53904.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV53904.1};
RG FlyBase;
RL Submitted (JUN-2008) 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; CH954182; EDV53904.1; -; Genomic_DNA.
DR RefSeq; XP_001982034.1; XM_001981998.2.
DR EnsemblMetazoa; FBtr0132422; FBpp0130914; FBgn0104657.
DR eggNOG; KOG0164; Eukaryota.
DR HOGENOM; CLU_000192_7_7_1; -.
DR OMA; AVIHIRA; -.
DR OrthoDB; 1094820at2759; -.
DR PhylomeDB; B3P784; -.
DR Proteomes; UP000008711; 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 Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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; IPR010926; Myosin_TH1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF802; UNCONVENTIONAL MYOSIN-IB ISOFORM X1; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 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 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 5..937
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1103..1288
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT REGION 170..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..835
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COMPBIAS 170..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1288 AA; 148179 MW; 8980A6D48890CAE1 CRC64;
MEQEIGTWDS VLLENLSEDS FINNIHQRYK RDHIYTYIGT SVVALNPYHH ISEHSLDNVR
NYGDKGIFQL PPHIYGLTNL AYQSLKDQSE DQCVLLTGES GAGKTETFKM IVNFLTHIQD
RSHCPPTPNV LRKQSSTSSA SGLVLHAHRR ASSSCSGTAN FIICKNRAEN PSASVSRRQS
PSPGPSQRSR TRAESIERQS RRHMREKIVD FDFSHHKSSE NISGLPESHA HHLHPTKSCF
KHQQTQVSAC TAMPAAAKGS PKYAVPTMYG GCRQCGHSKC VRAQSLEKEE RDDLRGSNCR
LSTIATATSN PVHPHRGSCS NLMRQHSTES QPERERDRSS LMGSTQRISL YDAHKLSKVL
GDLPPPPPSS VSPTPSASSS LHRRHKSPTQ RMRECVTCAD VFLEAMGNAC TLKNNNSSRY
GKLFDIEIDF KGDPMGVHIT HYMLEKTRIT DTIIGERNFH IFYQLLLGAD LQLLKSLKLY
RNVEKYELLR NTTAMEEDRM NFHYTKRSLD VLGLSCEESN SIFRVIAVVL KLGNFIFVPI
TNIDGTEGCQ VSNVYEVQET AQLLNMEAQI LINCLTRANS SNSAQEDVGC EMDARQAAIN
RNTLCRTLYS RLFTWLVNKI NESLKSTQRE KNLALLDFYG FEVLDHNSFE QFAINYSAEK
IHQNFVFHVL RSEQELYIRE GLEWSRIDYF DNESICELID KPSYGILSLI NEPHLNSNDA
LLLRVQQCCA GHPNFMTSGS NSMCFQIRHY ASVVNYSIHR FLEKNSDMLP KYISAAFYQS
KLSLVQSLFP EGNPRRQVTK KPSTLSSNIR TQLQTLLAIV KHRRSHYVFC IKPNEGKHPH
QFDMALVQHQ VRYMSLMPLV HLCRTGHCYH LLHVKFFHRY KLLNSLTWPH FHGGSQVEGI
ALIIRNLPLP SAEFTIGTKN VFVRSPRTVY ELEQFRRLRI SELAVLIQKM FRMYHARKRF
QRMRHSQMII SSAWRTWREC RFGIPFTGRR HLWSLYRVAR EEYRSLKYKR QVRWAIDIIG
RYYRQWKIRQ FLLTIPLRLP PNTLSPLSTE WPVAPVFLAD ASRHLRSIYH RWKCYIYRNS
FDQTARNRMR EKVTASIIFK DRKASYGRSV GHPFVGDYVR LRHNQQWKKI CAETNDQYVV
FADIINKIAR SSGKFVPILL VLSTSSLLLL DQRTLQIKYR VPASEIYRMS LSPYLDDIAV
FHVKASEFGR KKGDFVFQTG HVIEIVTKMF LVIQNATGKP PEIHISTEFE ANFGQQTVIF
SFKYGGMSDL AQGPPKVTRK ANRMEIIV
//
