GenomeNet

Database: UniProt
Entry: B4R0K6_DROSI
LinkDB: B4R0K6_DROSI
Original site: B4R0K6_DROSI 
ID   B4R0K6_DROSI            Unreviewed;       669 AA.
AC   B4R0K6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Vesicle-fusing ATPase {ECO:0000256|ARBA:ARBA00012674, ECO:0000256|RuleBase:RU367045};
DE            EC=3.6.4.6 {ECO:0000256|ARBA:ARBA00012674, ECO:0000256|RuleBase:RU367045};
GN   Name=Dsim\GD20473 {ECO:0000313|EMBL:EDX13021.1};
GN   ORFNames=Dsim_GD20473 {ECO:0000313|EMBL:EDX13021.1};
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX13021.1, ECO:0000313|Proteomes:UP000000304};
RN   [1] {ECO:0000313|EMBL:EDX13021.1, ECO:0000313|Proteomes:UP000000304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mosaic {ECO:0000313|Proteomes:UP000000304};
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).
CC   -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion
CC       of transport vesicles within the Golgi cisternae. Is also required for
CC       transport from the endoplasmic reticulum to the Golgi stack. Seems to
CC       function as a fusion protein required for the delivery of cargo
CC       proteins to all compartments of the Golgi stack independent of vesicle
CC       origin. {ECO:0000256|RuleBase:RU367045}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000161,
CC         ECO:0000256|RuleBase:RU367045};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU367045};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU367045};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU367045}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU367045}.
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DR   EMBL; CM000364; EDX13021.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4R0K6; -.
DR   SMR; B4R0K6; -.
DR   STRING; 7240.B4R0K6; -.
DR   HOGENOM; CLU_008037_2_0_1; -.
DR   OMA; CFDNEIA; -.
DR   PhylomeDB; B4R0K6; -.
DR   Proteomes; UP000000304; Chromosome 3r.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:EnsemblMetazoa.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
DR   GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR   GO; GO:0060439; P:trachea morphogenesis; IEA:EnsemblMetazoa.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR004201; Cdc48_dom2.
DR   InterPro; IPR029067; CDC48_domain_2-like_sf.
DR   InterPro; IPR003338; CDC4_N-term_subdom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039812; Vesicle-fus_ATPase.
DR   PANTHER; PTHR23078:SF3; VESICLE-FUSING ATPASE; 1.
DR   PANTHER; PTHR23078; VESICULAR-FUSION PROTEIN NSF; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF02933; CDC48_2; 1.
DR   Pfam; PF02359; CDC48_N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01072; CDC48_2; 1.
DR   SMART; SM01073; CDC48_N; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU367045};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367045};
KW   ER-Golgi transport {ECO:0000256|RuleBase:RU367045};
KW   Hydrolase {ECO:0000256|RuleBase:RU367045};
KW   Magnesium {ECO:0000256|RuleBase:RU367045};
KW   Metal-binding {ECO:0000256|RuleBase:RU367045};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU367045};
KW   Protein transport {ECO:0000256|RuleBase:RU367045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000304};
KW   Transport {ECO:0000256|RuleBase:RU367045}.
FT   DOMAIN          8..92
FT                   /note="CDC48 N-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01073"
FT   DOMAIN          117..183
FT                   /note="CDC48"
FT                   /evidence="ECO:0000259|SMART:SM01072"
FT   DOMAIN          234..332
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          457..593
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   669 AA;  74423 MW;  8AE27FA2D8B2A334 CRC64;
     MSIEKAHRMR AIKCPTDELS LTNKAIVNVS DFTEEVKYVD ISPGPGLHYI FALEKISGPE
     LPLGHVGFSL VQRKWATLSI NQEIDVRPYR FDASADIITL VSFETDFLQK KTTTQEPYDS
     DEMAKEFLMQ FAGMPLTVGQ TLVFQFKDKK FLGLAVKTLE AVDPRTFEKA ENSVLNLQGR
     SKGKIVRQSI INPDWDFGKM GIGGLDKEFN AIFRRAFASR VFPPELVEQL GIKHVKGILL
     YGPPGTGKTL MARQIGTMLN AREPKIVNGP QILDKYVGES EANIRRLFAE AEEEEKRLGP
     NSGLHIIIST RSTPFARLAD PWLGRVQILN IHTKRMRDFN KIANDVDNNE IAARTKNFSG
     AELEGLVRAA QSTAMNRLIK ADSKVHVDPE AMEKLRVTRA DFLHALDNDI KPAFGAAQEM
     LDNLLARGII NWGPPVTELL EDGMLSVQQA KATESSGLVS VLIEGAPNSG KSALAANLAQ
     LSDFPFVKVC SPEDMVGFTE SAKCLHIRKI FDDAYRSTLS CIVVDNVERL LDYGPIGPRY
     SNLTLQALLV LLKKQPPKGR KLLILCTSSR RDVLEEMEML SAFTSVLHVS NLSTPEHVLA
     VLDDSDLFSP EELQSIARKM AGKRLCIGIK KLLSLIDMIR QSEPPQRVIK FLSKMEEEGG
     LEMDRVLGH
//
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