ID A0A0G4J299_PLABS Unreviewed; 787 AA.
AC A0A0G4J299;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=PBRA_008695 {ECO:0000313|EMBL:CEP01753.1}, PLBR_LOCUS8689
GN {ECO:0000313|EMBL:SPR01474.1};
OS Plasmodiophora brassicae (Clubroot disease agent).
OG Mitochondrion {ECO:0000313|EMBL:SPR01474.1}.
OC Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC Plasmodiophoridae; Plasmodiophora.
OX NCBI_TaxID=37360 {ECO:0000313|EMBL:CEP01753.1, ECO:0000313|Proteomes:UP000039324};
RN [1] {ECO:0000313|EMBL:CEP01753.1, ECO:0000313|Proteomes:UP000039324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:CEP01753.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPR01474.1, ECO:0000313|Proteomes:UP000290189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Fogelqvist J.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CDSF01000117; CEP01753.1; -; Genomic_DNA.
DR EMBL; OVEO01000017; SPR01474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4J299; -.
DR STRING; 37360.A0A0G4J299; -.
DR EnsemblProtists; CEP01753; CEP01753; PBRA_008695.
DR OMA; ARQKGNF; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000039324; Unassembled WGS sequence.
DR Proteomes; UP000290189; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; 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:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; 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; 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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000313|EMBL:SPR01474.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000039324}.
FT DOMAIN 330..470
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 54..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 86013 MW; A6AFEEDC8778CF2F CRC64;
MLRSLASRLR LVSPLAAAPA RSSAYQRLWA VSPAIVRASK IPYGFRRFFP DGAPELAKEG
DGKNDPSSSS SSSGRSSHEK PGGGNDKSPW PNWETHLTLA ILTALGLTLS SSRITDGERE
ITFQEFRKRL LEPGLVDRIV IMNKQTARVY LRPSRTTTPT DRYRFEDDAE DAAPARRASL
PDDAALMDLQ APRAQYYFTI GSVETFENSL NRVQEEMGVS PTDFVPIKYV NRTSWGQELL
KFGPTLLLIG FWLFIMRGLS SSVGSGGGIG GGMKNIFQIG KAPAVRAGKD AKNKVLFKDV
AGLDEAKREV SEFVDFLKNP KKYTQLGAKI PRGALLVGPP GTGKTMLARA TAAEASVPFF
SISGSDFIEM FVGVGPSRVR DLFAQAREAA PCIVFIDEID AVGRARGKGG FSGGNDEREN
TLNQLLVEMD GFSTQSGVVV LAGTNRVDIL DKALLRPGRF DRQISIDLPD IKGRQQIFKV
HLKPLSLANP VDDIARRLAS LTPGFSGADI ANICNEAALI AARTDKQAVE LVDFEAAVDR
VIGGLAKENK IMTKQERELV AHHEAGHAVV GWFLRHADPL LKVTIVPRGT AALGFAQYLP
KELNLMSEDQ LRDMMCMALG GRASEQVFFD EVSTGAADDL KKITRIAYST VTLFGMSKRV
GNLSFPLDES SGNPAFYKPY SEKTAELIDE EVRSMVDQLY DRTLALVAEK RVLIEALAAR
LLVQETVTHK DLVEVLGERP YKSQQYIDYV EETSKEIPTK EDTPPEPAEK ADAAAQTGTD
DLSLKPA
//
