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Database: UniProt
Entry: A0A059AQN0_EUCGR
LinkDB: A0A059AQN0_EUCGR
Original site: A0A059AQN0_EUCGR 
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
//
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