ID CD48A_ARATH Reviewed; 809 AA. AC P54609; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 187. DE RecName: Full=Cell division control protein 48 homolog A {ECO:0000303|PubMed:12427991}; DE Short=AtCDC48a {ECO:0000303|PubMed:12427991}; GN Name=CDC48A {ECO:0000303|PubMed:12427991}; GN Synonyms=CDC48 {ECO:0000303|PubMed:8521820}; GN OrderedLocusNames=At3g09840 {ECO:0000312|Araport:AT3G09840}; GN ORFNames=F8A24.11 {ECO:0000312|EMBL:AAF23260.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX PubMed=8521820; DOI=10.1002/j.1460-2075.1995.tb00250.x; RA Feiler H.S., Desprez T., Santoni V., Kronenberger J., Caboche M., Traas J.; RT "The higher plant Arabidopsis thaliana encodes a functional CDC48 homologue RT which is highly expressed in dividing and expanding cells."; RL EMBO J. 14:5626-5637(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP SUBCELLULAR LOCATION, INTERACTION WITH SYP31 AND KNOLLE, AND SUBUNIT. RX PubMed=12427991; DOI=10.1104/pp.011742; RA Rancour D.M., Dickey C.E., Park S., Bednarek S.Y.; RT "Characterization of AtCDC48. Evidence for multiple membrane fusion RT mechanisms at the plane of cell division in plants."; RL Plant Physiol. 130:1241-1253(2002). RN [7] RP INTERACTION WITH PUX1, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=cv. Columbia; RX PubMed=15498773; DOI=10.1074/jbc.m405498200; RA Rancour D.M., Park S., Knight S.D., Bednarek S.Y.; RT "Plant UBX domain-containing protein 1, PUX1, regulates the oligomeric RT structure and activity of arabidopsis CDC48."; RL J. Biol. Chem. 279:54264-54274(2004). RN [8] RP INTERACTION WITH PUX1; PUX2; PUX3; PUX4 AND PUX11. RA Posthuma R., Rancour D., Park S., Bates B., Bednarek S.; RT "The plant UBX-domain containing (PUX) protein family regulates the RT function of Arabidopsis CDC48, a conserved essential AAA-ATPase."; RL (In) Proceedings of the 16th international conference on Arabidopsis RL research, abstract#116, Madison (2005). RN [9] RP INTERACTION WITH SERK1; GRF6 AND KAPP, SUBUNIT, AND IDENTIFICATION IN THE RP SERK1 COMPLEX. RX PubMed=15592873; DOI=10.1007/s00425-004-1447-7; RA Rienties I.M., Vink J., Borst J.W., Russinova E., de Vries S.C.; RT "The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the RT 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP."; RL Planta 221:394-405(2005). RN [10] RP SUBCELLULAR LOCATION, AND INTERACTION WITH SERK1. RX PubMed=16621602; DOI=10.1016/j.jsb.2006.03.004; RA Aker J., Borst J.W., Karlova R., de Vries S.C.; RT "The Arabidopsis thaliana AAA protein CDC48A interacts in vivo with the RT somatic embryogenesis receptor-like kinase 1 receptor at the plasma RT membrane."; RL J. Struct. Biol. 156:62-71(2006). RN [11] RP INTERACTION WITH PUX1; PUX4 AND PUX5, MUTAGENESIS OF LYS-254; GLU-308; RP LYS-527 AND GLU-581, AND SUBUNIT. RX PubMed=17190830; DOI=10.1074/jbc.m609042200; RA Park S., Rancour D.M., Bednarek S.Y.; RT "Protein domain-domain interactions and requirements for the negative RT regulation of Arabidopsis CDC48/p97 by the plant ubiquitin regulatory X RT (UBX) domain-containing protein, PUX1."; RL J. Biol. Chem. 282:5217-5224(2007). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=cv. Landsberg erecta; RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200; RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.; RT "Multidimensional protein identification technology (MudPIT) analysis of RT ubiquitinated proteins in plants."; RL Mol. Cell. Proteomics 6:601-610(2007). RN [13] RP SUBUNIT, INTERACTION WITH SERK1, AND PHOSPHORYLATION AT SER-41. RX PubMed=17693538; DOI=10.1104/pp.107.103986; RA Aker J., Hesselink R., Engel R., Karlova R., Borst J.W., Visser A.J.W.G., RA de Vries S.C.; RT "In vivo hexamerization and characterization of the Arabidopsis AAA ATPase RT CDC48A complex using forster resonance energy transfer-fluorescence RT lifetime imaging microscopy and fluorescence correlation spectroscopy."; RL Plant Physiol. 145:339-350(2007). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [15] RP INTERACTION WITH PUX7. RX PubMed=23747397; DOI=10.1016/j.gene.2013.05.056; RA Gallois J.L., Drouaud J., Lecureuil A., Guyon-Debast A., Bonhomme S., RA Guerche P.; RT "Functional characterization of the plant ubiquitin regulatory X (UBX) RT domain-containing protein AtPUX7 in Arabidopsis thaliana."; RL Gene 526:299-308(2013). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-254 AND LYS-527, RP INTERACTION WITH TOC159; SP1 AND SP2/OEP39, AND SUBUNIT. RC STRAIN=cv. Columbia; RX PubMed=30792274; DOI=10.1126/science.aav4467; RA Ling Q., Broad W., Troesch R., Toepel M., Demiral Sert T., RA Lymperopoulos P., Baldwin A., Jarvis R.P.; RT "Ubiquitin-dependent chloroplast-associated protein degradation in RT plants."; RL Science 363:0-0(2019). RN [17] RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, SUBUNIT, AND RP INDUCTION BY METHYL VIOLOGEN. RC STRAIN=cv. Columbia; RX PubMed=35417702; DOI=10.1016/j.celrep.2022.110664; RA Li J., Yuan J., Li Y., Sun H., Ma T., Huai J., Yang W., Zhang W., Lin R.; RT "The CDC48 complex mediates ubiquitin-dependent degradation of intra- RT chloroplast proteins in plants."; RL Cell Rep. 39:110664-110664(2022). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-481 IN COMPLEX WITH ADP. RA Heinemann U., Roske Y., Banchenko S., Arumughan A., Wanker E., Petrovic S.; RT "Common mode of remodeling AAA ATPases p97/CDC48 by their disassembly RT cofactors ASPL/PUX1."; RL Submitted (AUG-2018) to the PDB data bank. CC -!- FUNCTION: Probably functions in cell division and growth processes CC (Probable). Interacts with certain SNAREs as part of specialized CC membrane fusion events where vesicles from the same organelle fuse CC (homotypic fusion) (Probable). In collaboration with SP1/DIAL1 and CC P39/SP2, mediates translocalization of ubiquitinated proteins from the CC chloroplast outer envelope membrane (OEM) for degradation by the 26S CC proteasome in the cytosol, thus contributing to chloroplast-associated CC protein degradation (CHLORAD) (PubMed:30792274). CDC48 complex CC component required for plant tolerance to reactive oxygen species (ROS) CC by modulating ubiquitin-dependent degradation, by the 26S proteasome, CC of intra-chloroplast proteins (e.g. RbcL and AtpB) in response to CC oxidative stress (PubMed:35417702). {ECO:0000250, CC ECO:0000269|PubMed:30792274, ECO:0000269|PubMed:35417702, ECO:0000305}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=40.5 uM for ATP (at 22 degrees Celsius) CC {ECO:0000269|PubMed:15498773}; CC Vmax=3.47 umol/min/ug enzyme with ATP as substrate (at 22 degrees CC Celsius) {ECO:0000269|PubMed:15498773}; CC -!- SUBUNIT: Homohexamer (PubMed:15498773, PubMed:17190830, CC PubMed:30792274). Interacts with SERK1, GRF6, KAPP and SYP31, but not CC with KNOLLE. Component of the SERK1 signaling complex, composed of CC KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1 CC (PubMed:12427991, PubMed:15592873, PubMed:16621602, PubMed:17693538, CC PubMed:23747397). Interacts with PUX1, PUX2, PUX3, PUX4, PUX5, PUX7 and CC PUX11 via its N-terminus (PubMed:15498773, PubMed:17190830, Ref.8). CC Component of the CDC48 complex made of a CDC48 homohexamer attached to CC UFD1B/UFD1C and NPL4A/NPL4B (PubMed:35417702). Interacts with SP1 and CC SP2/OEP39 (PubMed:30792274). Binds to Toc159 at the chloroplast CC envelope (PubMed:30792274). {ECO:0000269|PubMed:12427991, CC ECO:0000269|PubMed:15498773, ECO:0000269|PubMed:15592873, CC ECO:0000269|PubMed:16621602, ECO:0000269|PubMed:17190830, CC ECO:0000269|PubMed:17693538, ECO:0000269|PubMed:23747397, CC ECO:0000269|PubMed:30792274, ECO:0000269|PubMed:35417702, CC ECO:0000269|Ref.8}. CC -!- INTERACTION: CC P54609; P54609: CDC48A; NbExp=5; IntAct=EBI-1563238, EBI-1563238; CC P54609; Q94JZ8: PUX7; NbExp=3; IntAct=EBI-1563238, EBI-10684297; CC P54609; Q94AG2: SERK1; NbExp=12; IntAct=EBI-1563238, EBI-1555537; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, phragmoplast. CC Cell membrane; Peripheral membrane protein {ECO:0000305}. Plastid, CC chloroplast membrane {ECO:0000269|PubMed:30792274, CC ECO:0000269|PubMed:35417702}; Peripheral membrane protein CC {ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:30792274}. CC Note=Primarily localized to the nucleus and, during cytokinesis, to the CC phragmoplast, a site where membrane vesicles are targeted in the CC deposition of new cell wall materials. CC -!- DEVELOPMENTAL STAGE: Highly expressed in the proliferating cells of the CC vegetative shoot, root, floral inflorescence and flowers, and in CC rapidly growing cells. CC -!- INDUCTION: Induced by reactive oxygen species (ROS) produced in CC response to methyl viologen (MV). {ECO:0000269|PubMed:35417702}. CC -!- PTM: Phosphorylated on at least one threonine residue and on Ser-41 by CC SERK1. {ECO:0000269|PubMed:17693538}. CC -!- DISRUPTION PHENOTYPE: Accumulation of ubiquitinated chloroplast CC proteins, due to impaired RbcL and AtpB ubiquitination and subsequent CC degradation by the 26S proteasome pathway upon ROS stress. CC {ECO:0000269|PubMed:35417702}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}. 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; U37587; AAC49120.1; -; mRNA. DR EMBL; AC015985; AAF23260.1; -; Genomic_DNA. DR EMBL; CP002686; AEE74820.1; -; Genomic_DNA. DR EMBL; OZ408685; CAO7040273.1; -; Genomic_DNA. DR EMBL; AY065076; AAL38252.1; -; mRNA. DR EMBL; AY094434; AAM19807.1; -; mRNA. DR PIR; S60112; S60112. DR RefSeq; NP_187595.1; NM_111819.5. DR PDB; 6HD3; X-ray; 2.80 A; A/C=1-481. DR PDB; 9M3V; EM; 3.90 A; A/B/C/D/E/F=1-809. DR PDB; 9M3W; EM; 3.20 A; A/B/C/D/E/F=1-809. DR PDB; 9M3X; EM; 3.30 A; A/B/C/D/E/F=1-809. DR PDB; 9M3Y; EM; 3.00 A; A/B/C/D/E/F=1-809. DR PDB; 9M3Z; EM; 3.90 A; A/B/C/D/E/F=1-809. DR PDB; 9M4G; X-ray; 2.60 A; A/B=28-190. DR PDB; 9M4N; X-ray; 3.45 A; A=28-809. DR PDB; 9UW1; X-ray; 1.88 A; A/B/C=28-196. DR PDB; 9V9O; X-ray; 2.20 A; A/B/C/D=28-196. DR AlphaFoldDB; P54609; -. DR EMDB; EMD-63608; -. DR EMDB; EMD-63609; -. DR EMDB; EMD-63610; -. DR EMDB; EMD-63611; -. DR EMDB; EMD-63612; -. DR SMR; P54609; -. DR BioGRID; 5476; 79. DR FunCoup; P54609; 3957. DR IntAct; P54609; 4. DR STRING; 3702.P54609; -. DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family. DR iPTMnet; P54609; -. DR MetOSite; P54609; -. DR SwissPalm; P54609; -. DR PaxDb; 3702-P54609; -. DR ProteomicsDB; 223907; -. DR GeneID; 820142; -. DR KEGG; ath:AT3G09840; -. DR Araport; AT3G09840; -. DR TAIR; AT3G09840; CDC48A. DR eggNOG; KOG0730; Eukaryota. DR HOGENOM; CLU_000688_12_0_1; -. DR InParanoid; P54609; -. DR OMA; VEMRHFR; -. DR OrthoDB; 1051988at2759; -. DR PhylomeDB; P54609; -. DR CD-CODE; 4299E36E; Nucleolus. DR PRO; PR:P54609; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; P54609; baseline and differential. DR GO; GO:0031969; C:chloroplast membrane; IDA:UniProtKB. DR GO; GO:0009707; C:chloroplast outer membrane; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:TAIR. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR. DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR. DR GO; GO:0005811; C:lipid droplet; IDA:TAIR. DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR. DR GO; GO:0005730; C:nucleolus; IDA:TAIR. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0009524; C:phragmoplast; IDA:TAIR. DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0009506; C:plasmodesma; HDA:TAIR. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IDA:TAIR. DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central. DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central. DR GO; GO:0051301; P:cell division; IMP:TAIR. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEP:UniProtKB. DR GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central. DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR. DR GO; GO:0009846; P:pollen germination; IMP:TAIR. DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR. DR GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0031648; P:protein destabilization; IMP:TAIR. DR GO; GO:0030162; P:regulation of proteolysis; IMP:UniProtKB. DR GO; GO:1902882; P:regulation of response to oxidative stress; IMP:UniProtKB. DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR CDD; cd19519; RecA-like_CDC48_r1-like; 1. DR CDD; cd19528; RecA-like_CDC48_r2-like; 1. DR FunFam; 1.10.8.60:FF:000004; Cell division control 48; 1. DR FunFam; 3.10.330.10:FF:000001; Cell division control 48; 1. DR FunFam; 2.40.40.20:FF:000003; Transitional endoplasmic reticulum ATPase; 1. DR FunFam; 3.40.50.300:FF:000012; Transitional endoplasmic reticulum ATPase; 1. DR FunFam; 3.40.50.300:FF:000048; Transitional endoplasmic reticulum ATPase; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 3.10.330.10; -; 1. DR Gene3D; 6.10.20.150; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR005938; AAA_ATPase_CDC48. DR InterPro; IPR050168; AAA_ATPase_domain. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR009010; Asp_de-COase-like_dom_sf. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. 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 NCBIfam; TIGR01243; CDC48; 1. DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1. DR PANTHER; PTHR23077:SF138; CELL DIVISION CONTROL PROTEIN 48 HOMOLOG A; 1. DR Pfam; PF00004; AAA; 2. DR Pfam; PF17862; AAA_lid_3; 2. 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. DR PROSITE; PS00674; AAA; 2. DR PDBsum; 6HD3; -. DR PDBsum; 9M3V; -. DR PDBsum; 9M3W; -. DR PDBsum; 9M3X; -. DR PDBsum; 9M3Y; -. DR PDBsum; 9M3Z; -. DR PDBsum; 9M4G; -. DR PDBsum; 9M4N; -. DR PDBsum; 9UW1; -. DR PDBsum; 9V9O; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division; KW Cell membrane; Chloroplast; Cytoplasm; Cytoskeleton; Membrane; KW Nucleotide-binding; Nucleus; Phosphoprotein; Plastid; Protein transport; KW Reference proteome; Repeat; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..809 FT /note="Cell division control protein 48 homolog A" FT /id="PRO_0000084579" FT REGION 782..809 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 791..801 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 210 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:6HD3" FT BINDING 248..256 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:6HD3" FT BINDING 387 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:6HD3" FT BINDING 521..529 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 41 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:17693538" FT MUTAGEN 254 FT /note="K->A: Decreases ATPase activity. Chlorosis due to FT defective chloroplast biogenesis and reactive oxygen FT species (ROS) accumulation, as a result of TOC proteins, FT outer envelope membrane (OEM) proteins and SP1/DIAL1 FT overaccumulation; when associated with A-527." FT /evidence="ECO:0000269|PubMed:17190830, FT ECO:0000269|PubMed:30792274" FT MUTAGEN 308 FT /note="E->Q: Decreases ATPase activity." FT /evidence="ECO:0000269|PubMed:17190830" FT MUTAGEN 527 FT /note="K->A: Abolishes ATPase activity. Chlorosis due to FT defective chloroplast biogenesis and reactive oxygen FT species (ROS) accumulation, as a result of TOC proteins, FT outer envelope membrane (OEM) proteins and SP1/DIAL1 FT overaccumulation; when associated with A-527." FT /evidence="ECO:0000269|PubMed:17190830, FT ECO:0000269|PubMed:30792274" FT MUTAGEN 581 FT /note="E->Q: Abolishes ATPase activity." FT /evidence="ECO:0000269|PubMed:17190830" FT HELIX 16..22 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 47..52 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 70..77 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 90..94 FT /evidence="ECO:0007829|PDB:6HD3" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 103..108 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 116..123 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 135..139 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 140..143 FT /evidence="ECO:0007829|PDB:6HD3" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 155..160 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 163..180 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 213..228 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 232..235 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 243..247 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 254..265 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 268..273 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 274..278 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 284..298 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 301..307 FT /evidence="ECO:0007829|PDB:6HD3" FT TURN 308..311 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 312..314 FT /evidence="ECO:0007829|PDB:6HD3" FT TURN 316..318 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 322..337 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 340..342 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 344..351 FT /evidence="ECO:0007829|PDB:6HD3" FT TURN 353..355 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 358..361 FT /evidence="ECO:0007829|PDB:6HD3" FT STRAND 368..371 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 377..386 FT /evidence="ECO:0007829|PDB:6HD3" FT TURN 387..390 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 399..405 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 411..429 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 442..445 FT /evidence="ECO:0007829|PDB:6HD3" FT HELIX 452..460 FT /evidence="ECO:0007829|PDB:6HD3" SQ SEQUENCE 809 AA; 89393 MW; 93222D637EA193B0 CRC64; MSTPAESSDS KSKKDFSTAI LERKKSPNRL VVDEAINDDN SVVSLHPATM EKLQLFRGDT ILIKGKKRKD TVCIALADET CEEPKIRMNK VVRSNLRVRL GDVISVHQCP DVKYGKRVHI LPVDDTVEGV TGNLFDAYLK PYFLEAYRPV RKGDLFLVRG GMRSVEFKVI ETDPAEYCVV APDTEIFCEG EPVKREDEER LDDVGYDDVG GVRKQMAQIR ELVELPLRHP QLFKSIGVKP PKGILLYGPP GSGKTLIARA VANETGAFFF CINGPEIMSK LAGESESNLR KAFEEAEKNA PSIIFIDEID SIAPKREKTN GEVERRIVSQ LLTLMDGLKS RAHVIVMGAT NRPNSIDPAL RRFGRFDREI DIGVPDEIGR LEVLRIHTKN MKLAEDVDLE RISKDTHGYV GADLAALCTE AALQCIREKM DVIDLEDDSI DAEILNSMAV TNEHFHTALG NSNPSALRET VVEVPNVSWN DIGGLENVKR ELQETVQYPV EHPEKFEKFG MSPSKGVLFY GPPGCGKTLL AKAIANECQA NFISVKGPEL LTMWFGESEA NVREIFDKAR QSAPCVLFFD ELDSIATQRG GGSGGDGGGA ADRVLNQLLT EMDGMNAKKT VFIIGATNRP DIIDSALLRP GRLDQLIYIP LPDEDSRLNI FKAALRKSPI AKDVDIGALA KYTQGFSGAD ITEICQRACK YAIRENIEKD IEKEKRRSEN PEAMEEDGVD EVSEIKAAHF EESMKYARRS VSDADIRKYQ AFAQTLQQSR GFGSEFRFEN SAGSGATTGV ADPFATSAAA AGDDDDLYN //