ID A0A0E0L3D9_ORYPU Unreviewed; 825 AA.
AC A0A0E0L3D9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC05G16770.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC05G16770.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC05G16770.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Probable ATP-dependent zinc metallopeptidase.
CC {ECO:0000256|ARBA:ARBA00003497}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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DR AlphaFoldDB; A0A0E0L3D9; -.
DR STRING; 4537.A0A0E0L3D9; -.
DR MEROPS; M41.023; -.
DR EnsemblPlants; OPUNC05G16770.1; OPUNC05G16770.1; OPUNC05G16770.
DR Gramene; OPUNC05G16770.1; OPUNC05G16770.1; OPUNC05G16770.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_2_1; -.
DR OMA; ARQKGNF; -.
DR Proteomes; UP000026962; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.1690.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF2; SD01613P; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 371..511
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 25..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 90675 MW; 3D5350DE8008C4B7 CRC64;
MNYAIRQERV EVPILHLQAP TQQGVTLTDG TENGFSLGGT RSPPPPPLPS VHGGEGGGLG
LGFVRGYLTA ALGRPAAGKV GTDWRSILAN PQFRRLFSDG SKKNYENYYP KGKKEAPKGD
GSNKSDSKQD SSTDDQWNFQ ETASKQLQNF LAPLLLLGLM FSSLSSSSSD QKEISFQEFK
NKLLEPGLVD RIVVSNKSVA KVYVRSSPQS NSQGQNTDAI VTTNDVPSKH TPSRYRYYFN
IGSVDSFEEK LEEAQEALGV DPHDFVPVTY VAEVNWFQEV MRFAPTVFLV GLIYLMSKRM
QSGFNIGGGP GKGGRGIFNI GKAQVTKMDK NSKNKVFFKD VAGCDEAKQE IMEFVHFLKN
PKKYEELGAK IPKGALLVGP PGTGKTLLAK ATAGESGVPF LSISGSDFME MFVGVGPSRV
RNLFQEARQC APSIIFIDEI DAIGRARGRG GFSGANDERE STLNQLLVEM DGFGTTSGVV
VLAGTNRPDI LDKALLRPGR FDRQITIDKP DIKGRDQIFR IYLKKLKLDN EPSFYSQRLA
ALTPGFAGAD IANVCNEAAL IAARCEQTQI TMQHFESAID RIIGGLEKKN KVISKLERRT
VAYHESGHAV AGWFLEHAEP LLKVTIVPRG TAALGFAQYV PNENLLMTKE QLFDMTCMTL
GGRAAEEVLI GKISTGAQND LEKVTKMTYA QVAVYGFSEK VGLLSFPQRD DGFEMTKPYS
NQTASIIDDE VREWVGKAYK KTVELITEHK EQVAKIAEML LEKEVLHQDD LVRVLGERPF
KAVEPTNYDL FKQGFQDEDS KNQEAAKTPQ PDDDGTPSLG EVVPT
//
