GenomeNet

Database: UniProt
Entry: A0A2R5G8K9_9STRA
LinkDB: A0A2R5G8K9_9STRA
Original site: A0A2R5G8K9_9STRA 
ID   A0A2R5G8K9_9STRA        Unreviewed;       758 AA.
AC   A0A2R5G8K9;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:GBG24391.1};
GN   ORFNames=FCC1311_006092 {ECO:0000313|EMBL:GBG24391.1};
OS   Hondaea fermentalgiana.
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Labyrinthulomycetes;
OC   Thraustochytrida; Thraustochytriaceae; Hondaea.
OX   NCBI_TaxID=2315210 {ECO:0000313|EMBL:GBG24391.1, ECO:0000313|Proteomes:UP000241890};
RN   [1] {ECO:0000313|EMBL:GBG24391.1, ECO:0000313|Proteomes:UP000241890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sedici K., Godart F., Aiese Cigliano R., Sanseverino W., Barakat M.,
RA   Ortet P., Marechal E., Cagnac O., Amato A.;
RT   "Sequencing, de novo assembly and annotation of complete genome of a new
RT   Thraustochytrid species, strain FCC1311.";
RL   Submitted (DEC-2017) 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:GBG24391.1}.
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; BEYU01000005; GBG24391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R5G8K9; -.
DR   EnsemblProtists; GBG24391; GBG24391; FCC1311_006092.
DR   InParanoid; A0A2R5G8K9; -.
DR   Proteomes; UP000241890; 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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   ATP-binding {ECO:0000313|EMBL:GBG24391.1};
KW   Hydrolase {ECO:0000313|EMBL:GBG24391.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:GBG24391.1};
KW   Protease {ECO:0000313|EMBL:GBG24391.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241890}.
FT   DOMAIN          422..697
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          629..724
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   758 AA;  79575 MW;  0BA65A0BD62C42AD CRC64;
     MAWLSGSSRN GDLGSASATS TSTLQGAGGS GGGNGGGDAV GLCPKCQRKL ELVDSGSQGS
     SDLVFKCQCS PGVHYVMMDT SKSTLDRIKQ VESMTSATAA SSSPASSAWT SSRGNGSYTP
     GPASADMSAG NQFRRQPQSG DAVTGGAPGN FTGSTGNNDD KGSGLKWLDD SQRAGSRTDQ
     PQQYSGEPTG PLPGAGGSQA AAPAVNEAPR WANKTPRELF NGLNEFVIGQ DRVKKVLSVS
     VHNHYNILSY NAKQRKARAA RDAAVGSGAG GLAKSGITPG VSTHTNAGST TSGGPGSGPP
     QSLRQFDDKQ VRRWYQGREV DLGDGEIPPQ NADVSPLAWR TGEGYVRGDD GEPRATIVKL
     ADGGLGGDRV PGRESASADH GRSREASDAL EEVDNDARAK ANAGSAGASA SSETQLDVTH
     IDKSNVLLIG PTGSGKTLMA RTLARMTGVP LVIFDATCLT QAGYIGEDVE AILYKLYQEA
     DYDVDLAQRG IVYIDEIDKI AKSSGPGATR DVSGEGVQQA LLKLLEGTVA NVPKKGAKSV
     RSEYVQIDTS EILFICGGAF SGLEKTISRR TMKSSMGFEA SVLPNSSETL QGVTADDLFK
     QVQPKDLVQY GLIPEFLGRF SHVLSTRQLT IDELCQVLTE PKNAIVRQYR TLFSLQNVDF
     VITDGALRRI AIMAHERETG ARGLRAILDS ILTETMFVLP EKGDVKAVVV HEDAVLGLKQ
     PLLVKKGPTP ASEIASRLDS GEDDADLWSQ VEEASAGF
//
DBGET integrated database retrieval system