ID Q9V405_DROME Unreviewed; 413 AA. AC Q9V405; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 28-MAR-2018, entry version 168. 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.-.-.- {ECO:0000313|EMBL:AAF48001.1, 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-RA {ECO:0000313|EMBL:ACI46532.1}, GN S6 {ECO:0000313|EMBL:AAF48001.1}, S6B {ECO:0000313|EMBL:AAF48001.1}, GN TBP7 {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; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; 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., RA Baumeister W.; RT "The regulatory complex of Drosophila melanogaster 26S proteasomes. RT Subunit 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., RA Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., RA Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA 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., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., RA Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA 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 RT melanogaster 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., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic 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., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a 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 RT 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. 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., RA Yu C., Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [10] {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 [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=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 RT heterochromatin."; RL Science 316:1586-1591(2007). RN [12] {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 [13] {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 [14] {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., RA Andolfatto P.; RT "On the utility of short intron sequences as a reference for the RT detection of positive and negative selection in Drosophila."; RL Mol. Biol. Evol. 27:1226-1234(2010). RN [15] {ECO:0000313|EMBL:AAF48001.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the AAA ATPase family. CC {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 UniGene; Dm.8238; -. DR SMR; Q9V405; -. DR IntAct; Q9V405; 17. DR STRING; 7227.FBpp0073292; -. 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 CTD; 32047; -. DR FlyBase; FBgn0028686; Rpt3. DR eggNOG; KOG0727; Eukaryota. DR eggNOG; COG1222; LUCA. DR GeneTree; ENSGT00550000074962; -. DR KO; K03063; -. DR OMA; LIIRNDP; -. DR OrthoDB; EOG091G07NC; -. 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-174113; SCF-beta-TrCP mediated degradation of Emi1. 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-2871837; FCERI mediated NF-kB activation. DR Reactome; R-DME-432395; Degradation of TIM. DR Reactome; R-DME-432524; Degradation of PER. 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-538848; Degradation of CLK. 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-68949; Orc1 removal from chromatin. DR Reactome; R-DME-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-DME-69229; Ubiquitin-dependent degradation of Cyclin D1. DR Reactome; R-DME-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-DME-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. 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-9020702; Interleukin-1 signaling. DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR GenomeRNAi; 32047; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0028686; -. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central. DR GO; GO:0001673; C:male germ cell nucleus; IDA:FlyBase. DR GO; GO:0031595; C:nuclear proteasome complex; IBA:GO_Central. 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:ATPase activity; ISM:FlyBase. DR GO; GO:0036402; F:proteasome-activating ATPase activity; IBA:GO_Central. DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central. DR GO; GO:0007623; P:circadian rhythm; TAS:Reactome. DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IBA:GO_Central. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:FlyBase. DR GO; GO:0008063; P:Toll signaling pathway; TAS:Reactome. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central. DR InterPro; IPR005937; 26S_Psome_P45-like. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR035256; PSMC4. DR PANTHER; PTHR23073:SF8; PTHR23073:SF8; 1. DR Pfam; PF00004; AAA; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Hydrolase {ECO:0000313|EMBL:AAF48001.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651}; KW Proteasome {ECO:0000313|EMBL:AAF08387.1}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q9V405}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}. FT DOMAIN 193 332 AAA. {ECO:0000259|SMART:SM00382}. FT COILED 32 52 {ECO:0000256|SAM:Coils}. 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 //