ID A0A058ZWV2_EUCGR Unreviewed; 517 AA.
AC A0A058ZWV2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 28-JAN-2026, entry version 41.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=EUGRSUZ_L00795 {ECO:0000313|EMBL:KCW45485.1};
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:KCW45485.1};
RN [1] {ECO:0000313|EMBL:KCW45485.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW45485.1};
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.
RN [2] {ECO:0000313|EMBL:KAK2632975.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KAK2632975.1};
RX PubMed=24919147; DOI=10.1038/nature13308;
RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA van der Merwe K., Singh P., van Jaarsveld I., Silva-Junior O.B.,
RA Togawa R.C., Pappas M.R., Faria D.A., Sansaloni C.P., Petroli C.D.,
RA Yang X., Ranjan P., Tschaplinski T.J., Ye C.Y., Li T., Sterck L.,
RA Vanneste K., Murat F., Soler M., Clemente H.S., Saidi N., Cassan-Wang H.,
RA Dunand C., Hefer C.A., Bornberg-Bauer E., Kersting A.R., Vining K.,
RA Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.E., Liston A.,
RA Spatafora J.W., Dharmwardhana P., Raja R., Sullivan C., Romanel E.,
RA Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van de Peer Y., Rokhsar D.S., Schmutz J.;
RT "The genome of Eucalyptus grandis.";
RL Nature 510:356-362(2014).
RN [3] {ECO:0000313|EMBL:KAK2632975.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KAK2632975.1};
RA Myburg A., Grattapaglia D., Tuskan G., Hellsten U., Hayes R., Grimwood J.,
RA Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D., Dubchak I.,
RA Poliakov A., Mizrachi E., Kullan A., Hussey S., Pinard D., Van D.,
RA Singh P., Van J., Silva-Junior O., Togawa R., Pappas M., Faria D.,
RA Sansaloni C., Petroli C., Yang X., Ranjan P., Tschaplinski T., Ye C.,
RA Li T., Sterck L., Vanneste K., Murat F., Soler M., Clemente H., Saidi N.,
RA Cassan-Wang H., Dunand C., Hefer C., Bornberg-Bauer E., Kersting A.,
RA Vining K., Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.,
RA Liston A., Spatafora J., Dharmwardhana P., Raja R., Sullivan C.,
RA Romanel E., Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J.,
RA Kudrna D., Brommonschenkel S., Pasquali G., Byrne M., Rigault P.,
RA Tibbits J., Spokevicius A., Jones R., Steane D., Vaillancourt R., Potts B.,
RA Joubert F., Barry K., Pappas G., Strauss S., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van D., Rokhsar D., Schmutz J.;
RT "WGS assembly of Eucalyptus grandis.";
RL Submitted (APR-2023) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KAK2632975.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KAK2632975.1};
RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA Van D.M., Singh P., Van J.I., Silva-Junior O.B., Togawa R.C., Pappas M.R.,
RA Faria D.A., Sansaloni C.P., Petroli C.D., Yang X., Ranjan P.,
RA Tschaplinski T.J., Ye C.Y., Li T., Sterck L., Vanneste K., Murat F.,
RA Soler M., Clemente H.S., Saidi N., Cassan-Wang H., Dunand C., Hefer C.A.,
RA Bornberg-Bauer E., Kersting A.R., Vining K., Amarasinghe V., Ranik M.,
RA Naithani S., Elser J., Boyd A.E., Liston A., Spatafora J.W.,
RA Dharmwardhana P., Raja R., Sullivan C., Romanel E., Alves-Ferreira M.,
RA Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van D.P., Rokhsar D.S., Schmutz J.;
RL Submitted (JUL-2023) to the EMBL/GenBank/DDBJ databases.
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 EMBL; MU848300; KAK2632975.1; -; Genomic_DNA.
DR EMBL; KK198814; KCW45485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A058ZWV2; -.
DR FunCoup; A0A058ZWV2; 1319.
DR Gramene; KCW45485; KCW45485; EUGRSUZ_L00795.
DR eggNOG; KOG0743; Eukaryota.
DR InParanoid; A0A058ZWV2; -.
DR OMA; WYPNDDE; -.
DR Proteomes; UP000030711; Unassembled WGS sequence.
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 FunFam; 3.40.50.300:FF:001122; AAA-ATPase ASD, mitochondrial; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000030711};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 241..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 313..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..490
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 58653 MW; 31E0CDC2C0B7BEE5 CRC64;
MTALEMWGNL GSFIAALMFA WAMFRQYFPP QLRMHVEAYA QKAVGHVYPY VQIKFPEFTG
EWLERGEAYT AIQNYLTRSA SARAKRLKAE SVKDSMSLVL SMDENEEVID EFEGVKLWWS
SSLIVSQKSP FSWSPSSEDR RFYRLTFHRS HRDLITGSYI KHVLEKGKVV AADNRQRKLF
TNNPSSNWSY HKPSKWSHVA FKHPSTFDTL AMEPSKKREI MNDLLKFQRG KEYYERIGKA
WKRGYLLYGP PGTGKSTMTA AMANFLNYDV YDVELTTVKD NTELRKLLID TSEKAIIVIE
DIDCSLDLTG QRKTKKQEKD DDGEKADPVK RMAKGGEESK DSKVTLSGLL NFSDGLWSAC
GGERIIVFTT NFVEKLDPAL IRRGRMDKHI EMLYCCFESF KVLARNYLGI ESHPLFTSVR
QLLEGTEMTP ADVAENLMPK SDDEDEEACL EGLIKALEKV KEDARKKSEE EKAAAAEAEA
TAARAMAQEE GQQTSSAGEQ EKGGRGCAEE VKENGVL
//
