ID A0A3Q7H5U9_SOLLC Unreviewed; 484 AA.
AC A0A3Q7H5U9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc05g007470.3.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc05g007470.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc05g007470.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc05g007470.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc05g007470.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00049360};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC {ECO:0000256|ARBA:ARBA00007448}.
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DR AlphaFoldDB; A0A3Q7H5U9; -.
DR FunCoup; A0A3Q7H5U9; 1285.
DR STRING; 4081.A0A3Q7H5U9; -.
DR PaxDb; 4081-Solyc05g007470.2.1; -.
DR EnsemblPlants; Solyc05g007470.3.1; Solyc05g007470.3.1; Solyc05g007470.3.
DR Gramene; Solyc05g007470.3.1; Solyc05g007470.3.1; Solyc05g007470.3.
DR InParanoid; A0A3Q7H5U9; -.
DR OMA; GEVWTNT; -.
DR Proteomes; UP000004994; Chromosome 5.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-ARBA.
DR CDD; cd19510; RecA-like_BCS1; 1.
DR Gene3D; 6.10.280.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR025753; AAA_N_dom.
DR InterPro; IPR058017; At3g28540-like_C.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR050747; Mitochondrial_chaperone_BCS1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF14363; AAA_assoc; 1.
DR Pfam; PF25568; AAA_lid_At3g28540; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000004994}.
FT DOMAIN 242..359
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 428..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 56108 MW; 60F3A063A51281F0 CRC64;
MMQDLWTQLG PTIAAIMFTW TMYQNYFPHE LRGHIRRYTD KLVNYFYPYM HIIFYELETE
GWFERSKAYV SIERYLSKSS STQAKRLKAN SVKDGQSLVL TMDDHEEITD EYKGEKVWWI
SSKKPASRQT ISLYKEDEKR YFKLKFHKKN RDLVTNSYLK YVLDEGKAIS VKERQRKLYT
NNKGDGGGYR YRGGRMWSGV VFEHPSTFDT LAMDPNKKQE IIDDLETFSK SKDYYAKIGK
AWKRGYLLYG PPGTGKSSMI AAMANYLKYD VYDLELTSVK DNTELRKLLI DTTGKSIIVI
EDIDCSLDLT GLLNFIDGLW SAIGGERLIV FTTNYVEKLD PALIRRGRMD KHIVLSYCCF
ESFKVLAHNY LDVVESHVHF PQIRRLLEET NMTPADIAEN LMPKSSKENA DICLERLIKA
LETAKEEAKL KAEEEERAKA AEKEKEEKDR EEKKEVTATE EAKSVDSVNE KDNGVKENGN
VSKS
//
