ID A0A6G0WMI3_9STRA Unreviewed; 598 AA.
AC A0A6G0WMI3;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=ClpX-type ZB domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Ae201684_013698 {ECO:0000313|EMBL:KAF0728514.1};
OS Aphanomyces euteiches.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=100861 {ECO:0000313|EMBL:KAF0728514.1, ECO:0000313|Proteomes:UP000481153};
RN [1] {ECO:0000313|EMBL:KAF0728514.1, ECO:0000313|Proteomes:UP000481153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 201684 {ECO:0000313|EMBL:KAF0728514.1,
RC ECO:0000313|Proteomes:UP000481153};
RA Gaulin E.;
RT "Genomics analysis of Aphanomyces spp. identifies a new class of oomycete
RT effector associated with host adaptation.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF0728514.1}.
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DR EMBL; VJMJ01000176; KAF0728514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G0WMI3; -.
DR VEuPathDB; FungiDB:AeMF1_010037; -.
DR Proteomes; UP000481153; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd19497; RecA-like_ClpX; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00382; clpX; 1.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000481153}.
FT DOMAIN 272..429
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 479..573
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 143..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 65794 MW; 636F4F8EC14E08BE CRC64;
MELVASMRKL MTRASSARRL SYFPIHSAAS ERSIGYPPVL ADVSRFHCRH QNLASLSPFK
FSVRTLSSDT RSHVGGSPLA CPQCGNGLKM VSSSVTEVDS MGMENNPVQP PAIPTALDEG
DILSCEDCKV HYTVKAASGV KTKHISSGDY SSSPQYMSPP NQRLASEYEY EERNADRKDR
SDHRGEDAVL TPRQIFDGLN KYVIGQETVK KALSVGVHNH YKRLSMNLKK KKTEESAAAN
GPVYSLGHGI HVERVSSTRK PKKSEEEEVE LDKTNMLIVG PTGSGKTLMA KTLARMAQVP
LVITDATCLT QAGYVGEDVE SILFKLYQAA NYNIESAQRG IIYIDEIDKI SRKSENVSIT
RDVSGEGVQQ ALLKMLEGTV VNVPEKGGRK NPRGEFIAID TSNILFICGG AFAGLEHIIS
RRTANASIGF GAQMPNTKLN KLDHVGKLLS QSEPQDLVSY GLIPEFVGRF PVIVSTLGLN
REELVRVLTE PRNSLVKQYR ALFALHDVDF HVSPCGLEAV ADLAVERNTG ARGLRAIFER
ALMDTMFHIP DMMNVKAVYV DGDVINGSKQ PVLIRDDVSI DQYLQEKEKE FEVEHPAA
//