ID Q9V405_DROME Unreviewed; 413 AA. AC Q9V405; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 14-DEC-2022, entry version 201. DE SubName: Full=26S proteasome regulatory complex subunit p48A {ECO:0000313|EMBL:AAF08387.1}; DE SubName: Full=CG16916 protein {ECO:0000313|EMBL:CBA35179.1}; DE SubName: Full=GH06151p {ECO:0000313|EMBL:ACI46532.1}; DE SubName: Full=Regulatory particle triple-A ATPase 3, isoform A {ECO:0000313|EMBL:AAF48001.1}; DE SubName: Full=Regulatory particle triple-A ATPase 3, isoform B {ECO:0000313|EMBL:AHN59578.1}; DE EC=3.6.1.3 {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|EMBL:AHN59578.1}; GN Name=Rpt3 {ECO:0000313|EMBL:AAF48001.1, GN ECO:0000313|FlyBase:FBgn0028686}; GN Synonyms=16916 {ECO:0000313|EMBL:AAF48001.1}, Dm_Rpt3a GN {ECO:0000313|EMBL:AAF48001.1}, Dmel\CG16916 GN {ECO:0000313|EMBL:AAF48001.1}, Dmp48A {ECO:0000313|EMBL:AAF48001.1}, GN l(1)G0052 {ECO:0000313|EMBL:AAF48001.1}, p48A GN {ECO:0000313|EMBL:AAF48001.1}, rpt3 {ECO:0000313|EMBL:AAF48001.1}, GN Rpt3-RA {ECO:0000313|EMBL:ACI46532.1}, S6 GN {ECO:0000313|EMBL:AAF48001.1}, S6B {ECO:0000313|EMBL:AAF48001.1}, TBP7 GN {ECO:0000313|EMBL:AAF48001.1}; GN ORFNames=CG16916 {ECO:0000313|EMBL:AAF48001.1, GN ECO:0000313|FlyBase:FBgn0028686}, Dmel_CG16916 GN {ECO:0000313|EMBL:AAF48001.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF08387.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Ovary {ECO:0000313|EMBL:AAF08387.1}; RA Hoelzl H.; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAF08387.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Ovary {ECO:0000313|EMBL:AAF08387.1}; RX PubMed=10893261; DOI=10.1083/jcb.150.1.119; RA Hoelzl H., Kapelari B., Kellermann J., Seemueller E., Suemegi M., RA Udvardy A., Medalia O., Sperling J., Mueller S.A., Engel A., Baumeister W.; RT "The regulatory complex of Drosophila melanogaster 26S proteasomes. Subunit RT composition and localization of a deubiquitylating enzyme."; RL J. Cell Biol. 150:119-130(2000). RN [3] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [5] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L., RA Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., RA Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [7] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [8] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [9] {ECO:0000313|EMBL:AAF48001.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [11] {ECO:0000313|EMBL:AAF48001.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [12] {ECO:0000313|EMBL:ACI46532.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley {ECO:0000313|EMBL:ACI46532.1}; RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [13] {ECO:0000313|EMBL:CBA35179.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ZBMEL131 {ECO:0000313|EMBL:CBA35181.1}, ZBMEL145 RC {ECO:0000313|EMBL:CBA35182.1}, ZBMEL157 {ECO:0000313|EMBL:CBA35183.1}, RC ZBMEL186 {ECO:0000313|EMBL:CBA35184.1}, ZBMEL191 RC {ECO:0000313|EMBL:CBA35185.1}, ZBMEL229 {ECO:0000313|EMBL:CBA35186.1}, RC ZBMEL377 {ECO:0000313|EMBL:CBA35187.1}, ZBMEL398 RC {ECO:0000313|EMBL:CBA35189.1}, ZBMEL82 {ECO:0000313|EMBL:CBA35179.1}, RC and ZBMEL84 {ECO:0000313|EMBL:CBA35180.1}; RX PubMed=20150340; DOI=10.1093/molbev/msq046; RA Parsch J., Novozhilov S., Saminadin-Peter S.S., Wong K.M., Andolfatto P.; RT "On the utility of short intron sequences as a reference for the detection RT of positive and negative selection in Drosophila."; RL Mol. Biol. Evol. 27:1226-1234(2010). RN [14] {ECO:0000313|EMBL:AAF48001.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109357; DOI=.1534/g3.115.018929; RG FlyBase Consortium; RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E., RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M., RA Gelbart W.M., null; RT "Gene Model Annotations for Drosophila melanogaster: Impact of High- RT Throughput Data."; RL G3 (Bethesda) 5:1721-1736(2015). RN [15] {ECO:0000313|EMBL:AAF48001.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109356; DOI=.1534/g3.115.018937; RG FlyBase Consortium; RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E., RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M., RA null; RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders."; RL G3 (Bethesda) 5:1737-1749(2015). RN [16] {ECO:0000313|EMBL:AAF48001.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25589440; RA Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E., RA Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M., RA Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M., RA de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M., RA Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M., RA Karpen G.H., Celniker S.E.; RT "The Release 6 reference sequence of the Drosophila melanogaster genome."; RL Genome Res. 25:445-458(2015). RN [17] {ECO:0000313|EMBL:AAF48001.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., RA Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [18] {ECO:0000313|EMBL:AAF48001.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF145306; AAF08387.1; -; mRNA. DR EMBL; AE014298; AAF48001.1; -; Genomic_DNA. DR EMBL; BT046144; ACI46532.1; -; mRNA. DR EMBL; AE014298; AHN59578.1; -; Genomic_DNA. DR EMBL; FN544098; CBA35179.1; -; Genomic_DNA. DR EMBL; FN544099; CBA35180.1; -; Genomic_DNA. DR EMBL; FN544100; CBA35181.1; -; Genomic_DNA. DR EMBL; FN544101; CBA35182.1; -; Genomic_DNA. DR EMBL; FN544102; CBA35183.1; -; Genomic_DNA. DR EMBL; FN544103; CBA35184.1; -; Genomic_DNA. DR EMBL; FN544104; CBA35185.1; -; Genomic_DNA. DR EMBL; FN544105; CBA35186.1; -; Genomic_DNA. DR EMBL; FN544106; CBA35187.1; -; Genomic_DNA. DR EMBL; FN544108; CBA35189.1; -; Genomic_DNA. DR RefSeq; NP_001285108.1; NM_001298179.1. DR RefSeq; NP_572686.1; NM_132458.3. DR AlphaFoldDB; Q9V405; -. DR SMR; Q9V405; -. DR IntAct; Q9V405; 17. DR STRING; 7227.FBpp0073292; -. DR DNASU; 32047; -. DR EnsemblMetazoa; FBtr0073436; FBpp0073292; FBgn0028686. DR EnsemblMetazoa; FBtr0346274; FBpp0312031; FBgn0028686. DR GeneID; 32047; -. DR KEGG; dme:Dmel_CG16916; -. DR UCSC; CG16916-RA; d. melanogaster. DR AGR; FB:FBgn0028686; -. DR CTD; 32047; -. DR FlyBase; FBgn0028686; Rpt3. DR VEuPathDB; VectorBase:FBgn0028686; -. DR eggNOG; KOG0727; Eukaryota. DR GeneTree; ENSGT01020000230346; -. DR HOGENOM; CLU_000688_2_0_1; -. DR OMA; AYAAQVK; -. DR OrthoDB; 571919at2759; -. DR BRENDA; 3.4.25.1; 1994. DR Reactome; R-DME-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-DME-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-DME-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-DME-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-DME-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-DME-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-DME-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-DME-187577; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-DME-202424; Downstream TCR signaling. DR Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI. DR Reactome; R-DME-209406; Degradation of NF-kappa-B inhibitor, CACT. DR Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM. DR Reactome; R-DME-216167; Nuclear CI is degraded. DR Reactome; R-DME-2467813; Separation of Sister Chromatids. DR Reactome; R-DME-2871837; FCERI mediated NF-kB activation. DR Reactome; R-DME-350562; Regulation of ornithine decarboxylase (ODC). DR Reactome; R-DME-382556; ABC-family proteins mediated transport. DR Reactome; R-DME-432395; Degradation of TIM. DR Reactome; R-DME-432524; Degradation of PER. DR Reactome; R-DME-432626; Circadian Clock pathway. DR Reactome; R-DME-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-DME-4608870; Asymmetric localization of PCP proteins. DR Reactome; R-DME-4641257; Degradation of AXIN. DR Reactome; R-DME-4641258; Degradation of DVL. DR Reactome; R-DME-5358346; Hedgehog ligand biogenesis. DR Reactome; R-DME-538864; Degradation of CRY. DR Reactome; R-DME-5607761; Dectin-1 mediated noncanonical NF-kB signaling. DR Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-DME-5610780; Degradation of GLI1 by the proteasome. DR Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome. DR Reactome; R-DME-5632684; Hedgehog 'on' state. DR Reactome; R-DME-5658442; Regulation of RAS by GAPs. DR Reactome; R-DME-5676590; NIK-->noncanonical NF-kB signaling. DR Reactome; R-DME-5689603; UCH proteinases. DR Reactome; R-DME-5689880; Ub-specific processing proteases. DR Reactome; R-DME-68867; Assembly of the pre-replicative complex. DR Reactome; R-DME-68949; Orc1 removal from chromatin. DR Reactome; R-DME-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-DME-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-DME-75815; Ubiquitin-dependent degradation of Cyclin D. DR Reactome; R-DME-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR Reactome; R-DME-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-DME-8939902; Regulation of RUNX2 expression and activity. DR Reactome; R-DME-8941858; Regulation of RUNX3 expression and activity. DR Reactome; R-DME-8948751; Regulation of PTEN stability and activity. DR Reactome; R-DME-8951664; Neddylation. DR Reactome; R-DME-9020702; Interleukin-1 signaling. DR Reactome; R-DME-9755511; KEAP1-NFE2L2 pathway. DR Reactome; R-DME-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2. DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR BioGRID-ORCS; 32047; 1 hit in 1 CRISPR screen. DR GenomeRNAi; 32047; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0028686; Expressed in secondary oocyte and 24 other tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0001673; C:male germ cell nucleus; IDA:FlyBase. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005838; C:proteasome regulatory particle; IDA:FlyBase. DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0036402; F:proteasome-activating activity; ISM:FlyBase. DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR005937; 26S_Psome_P45-like. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR032501; Prot_ATP_ID_OB_C. DR InterPro; IPR035256; PSMC4. DR PANTHER; PTHR23073:SF120; 26S PROTEASOME REGULATORY SUBUNIT 6B HOMOLOG; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF17862; AAA_lid_3; 1. DR Pfam; PF16450; Prot_ATP_ID_OB; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR01242; 26Sp45; 1. DR PROSITE; PS00674; AAA; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|RuleBase:RU003651}; KW Hydrolase {ECO:0000313|EMBL:AAF48001.1}; KW Meiosis {ECO:0000256|ARBA:ARBA00023254}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651}; KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:AAF08387.1}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9V405}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}. FT DOMAIN 193..332 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" SQ SEQUENCE 413 AA; 46999 MW; 34E7518BE593A0E3 CRC64; MPYNMDVLIP EKDELSDLKL KDAHSSLDEL DMEDLYVRYK KLQKTLEFIE VQEEYIKDEQ RNLKKEYLHA QEEVKRIQSV PLVIGQFLEA VDQNTGIVGS TTGSNYYVRI LSTIDRELLK PSASVALHKH SNALVDVLPP EADSSISMLQ PDEKPDVSYA DIGGMDMQKQ EIREAVELPL THFELYKQIG IDPPRGVLMY GPPGCGKTML AKAVAHHTTA SFIRVVGSEF VQKYLGEGPR MVRDVFRLAK ENAPAIIFID EIDAIATKRF DAQTGADREV QRILLELLNQ MDGFDQTTNV KVIMATNRAD TLDPALLRPG RLDRKIEFPL PDRRQKRLVF STITSKMNLS EDVDLEEFVA RPDKISGADI NAICQEAGMH AVRENRYIVL AKDFEKGYKN NIKKDEQEHE FYK //