GenomeNet

Database: UniProt
Entry: B3MJH5_DROAN
LinkDB: B3MJH5_DROAN
Original site: B3MJH5_DROAN 
ID   B3MJH5_DROAN            Unreviewed;       332 AA.
AC   B3MJH5;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   Name=Dana\GF15785 {ECO:0000313|EMBL:EDV32343.1};
GN   Synonyms=dana_GLEANR_16549 {ECO:0000313|EMBL:EDV32343.1};
GN   ORFNames=GF15785 {ECO:0000313|EMBL:EDV32343.1};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV32343.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV32343.1, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000256|ARBA:ARBA00005378}.
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DR   EMBL; CH902620; EDV32343.1; -; Genomic_DNA.
DR   RefSeq; XP_001963122.1; XM_001963086.2.
DR   AlphaFoldDB; B3MJH5; -.
DR   SMR; B3MJH5; -.
DR   STRING; 7217.B3MJH5; -.
DR   EnsemblMetazoa; FBtr0120485; FBpp0118977; FBgn0092809.
DR   GeneID; 6498590; -.
DR   KEGG; dan:6498590; -.
DR   eggNOG; KOG0990; Eukaryota.
DR   HOGENOM; CLU_042324_2_0_1; -.
DR   InParanoid; B3MJH5; -.
DR   OMA; AEDNLPW; -.
DR   OrthoDB; 275853at2759; -.
DR   PhylomeDB; B3MJH5; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0031391; C:Elg1 RFC-like complex; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18140; HLD_clamp_RFC; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013748; Rep_factorC_C.
DR   InterPro; IPR047854; RFC_lid.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   PANTHER; PTHR11669:SF9; REPLICATION FACTOR C SUBUNIT 5; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801}.
FT   DOMAIN          43..171
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   332 AA;  37443 MW;  2012F9AB619F5E7C CRC64;
     MTEHNGPAVR MPWVEKYRPS GLDDLISHEE IISTISRFIS RKQLPHLLFY GPPGTGKTST
     ILACARQLYS PQQFKSMVLE LNASDDRGIG IVRGQILNFA STRTIFCDTF KLIILDEADA
     MTNDAQNALR RIIEKYTDNV RFCVICNYLS KIIPALQSRC TRFRFAPLSP DQMMPRLEKI
     IDAEAVQITE DGKRALLTLA KGDMRKVLNV LQSTVMAFDK VNEDNVYTCV GYPLRQDIEQ
     ILKALLSGNS VEDSFKTVEN AKYARGLALE DILTELHLFV MRLELPMSVM NKLIVKLAQI
     EERLAKGCTE PAQTAALVAA FFICRDMVSL EK
//
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