ID A0A059CSP4_EUCGR Unreviewed; 518 AA.
AC A0A059CSP4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=EUGRSUZ_C02301 {ECO:0000313|EMBL:KCW80940.1};
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:KCW80940.1};
RN [1] {ECO:0000313|EMBL:KCW80940.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW80940.1};
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}.
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; KK198755; KCW80940.1; -; Genomic_DNA.
DR RefSeq; XP_010048623.1; XM_010050321.2.
DR AlphaFoldDB; A0A059CSP4; -.
DR STRING; 71139.A0A059CSP4; -.
DR EnsemblPlants; KCW80940; KCW80940; EUGRSUZ_C02301.
DR GeneID; 104437381; -.
DR Gramene; KCW80940; KCW80940; EUGRSUZ_C02301.
DR KEGG; egr:104437381; -.
DR eggNOG; KOG0743; Eukaryota.
DR InParanoid; A0A059CSP4; -.
DR OMA; SYPALMI; -.
DR OrthoDB; 819832at2759; -.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23070:SF110; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF14363; AAA_assoc; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..518
FT /note="AAA+ ATPase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001570130"
FT DOMAIN 236..391
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 475..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 58732 MW; C77E6CD0DE9E095A CRC64;
MKEFWTSLAS LLGVLAFCQS LLQMVFPPEL RFASLKFLNR LFNCFSFYCY YDITEIDGVN
TNELYNAVQL YLSSFVSASG SRLSLTRAIN SSATTFGLSN NDCINDVFDG VAVQWEHVVT
QRQSQTYSWP PLPDEKRGFM LRIRKRDKDI ILDFYLNYIM EKANDIRRKN QERLLYTNSR
GGSLDSRRHP WESVPFKHPS TFDTLAMDPE RKSNIEEDLR DFAAGQAFYQ RTGRAWKRGY
LLYGPPGTGK SSMIAAMANF LGYDIYDLEL TEVHSNSELR KLLMKTSSKS IIVIEDIDCS
VNLSNRAKAT HAGAPRSYYD SGAPDAARGG EDGNNNNTIT LSGLLNFTDG LWSCCGSERI
FVFTTNHIEK LDPALLRSGR MDMHIYMSYC SYPALKILLR NYLGSEAEEL GEAAASELRE
AAEKAKMTPA DISEVLIKNR RNKERAVGEL LEVLRARAER NEKCGGLREE CELNGVVEEM
EEEEQEKRAL ESPKEGSDCD DDSCKKVEDD DEEKEKAK
//
