ID A0A059AQN0_EUCGR Unreviewed; 496 AA.
AC A0A059AQN0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=EUGRSUZ_I01907 {ECO:0000313|EMBL:KCW56153.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW56153.1};
RN [1] {ECO:0000313|EMBL:KCW56153.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW56153.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; 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:ARBA00001836};
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 EMBL; KK198761; KCW56153.1; -; Genomic_DNA.
DR RefSeq; XP_010029271.1; XM_010030969.2.
DR AlphaFoldDB; A0A059AQN0; -.
DR STRING; 71139.A0A059AQN0; -.
DR EnsemblPlants; KCW56153; KCW56153; EUGRSUZ_I01907.
DR GeneID; 104419336; -.
DR Gramene; KCW56153; KCW56153; EUGRSUZ_I01907.
DR KEGG; egr:104419336; -.
DR eggNOG; KOG0743; Eukaryota.
DR InParanoid; A0A059AQN0; -.
DR OMA; YLEIDTH; -.
DR OrthoDB; 819832at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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:UniProt.
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; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23070:SF189; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF14363; AAA_assoc; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..401
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 323..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 56141 MW; A51C5B56CB809563 CRC64;
MKIDQPIKTA NSGGGGNAFA HLGSVVAGMM FAWAILQQFL PPDLRAYVTK YSQRFLRYVY
PYIQITFNEY TGERLMRSEA YLAIENYLSS AATTQAKRLK GDLVKNNQSL VVSMDDHEEV
SDKHNGVKLW WASGKKESRR RASSFHADGV DESGYYKLTF HKAQRELVFG PYLRHVLKQG
KEIRFQNRQR KLYTNNNWYW THVVFEHPAN FKTLAMDPSE KQEIINDLIT FSKNEEFYAR
IGRAWKRGYL LFGPPGTGKS TMIAAMANLL NYDIYDLELT AVKDNTSLRR LLIETSSKSI
IVIEDIDCSL DLTGQRKKAA KVEEVKDGEA SNQAKRAEKD PDGEKASRVT LSGLLNFIDG
LWSSCGGERL LVFTTNHIEK LDPALIRKGR MDKHVKLSYC RFEAFKVLAK NYLEIDTHPL
FDHIGKLLNE VDLTPADVAE HLMPKSASNN VEVCLESLVE ALEEAKTAKL KGEEGTEEVK
TETKDLVFVS GSPEGD
//