ID B3RSC2_TRIAD Unreviewed; 563 AA.
AC B3RSC2;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=ClpX-type ZB domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIADDRAFT_50037 {ECO:0000313|EMBL:EDV26489.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV26489.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV26489.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV26489.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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DR EMBL; DS985243; EDV26489.1; -; Genomic_DNA.
DR RefSeq; XP_002110485.1; XM_002110449.1.
DR AlphaFoldDB; B3RSC2; -.
DR STRING; 10228.B3RSC2; -.
DR EnsemblMetazoa; TriadT50037; TriadP50037; TriadG50037.
DR GeneID; 6751700; -.
DR KEGG; tad:TRIADDRAFT_50037; -.
DR CTD; 6751700; -.
DR eggNOG; KOG0745; Eukaryota.
DR HOGENOM; CLU_014218_0_1_1; -.
DR InParanoid; B3RSC2; -.
DR OMA; RIYQKKP; -.
DR OrthoDB; 452393at2759; -.
DR PhylomeDB; B3RSC2; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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; IPR027417; P-loop_NTPase.
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:UP000009022}.
FT DOMAIN 209..359
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 432..526
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 16..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 62141 MW; 4601853CDE59091B CRC64;
MAKHCTLQIV TIRYNGGNNE NIGKSSSHSG SGGGNSDSRN GSGKTTTTCP KCGDPCLVMQ
PFAYSNRFVK CNSCNHLFLL QNDSQQQQKV NDERAKAKPP EEMLKKPPPP RKIYDYLCRY
IVGQERAKRI LSVAVYNHYK RLYFNNLPVL SKPAFDKQNW KQKTDGTKDQ GNLMQIRGRN
ATQTNQLQQE TPINGTDLLD NNISALKLEK SNIVLFGPTG KTLLAQTLAR CLDVPFAICD
CTTLTQAGYV GEDIESVIGK LLQDANYNVS RAQQGIVFLD EVDKIGCVPG IHQLRDVGGE
GVQQGLLKML EGSIVNVPEK SLRKMRGDAN SFAVDTTHIL FVASGAFNGL DRVVSRRKHK
KFLGFGAPSL QKLGRRAAAE ASLASDPIES SIEDLKERDL LLSDVEAQDM IDFGLIPEFV
GRFPVLCHIE SLDEEALMRI LTEPENALLR QYKALFEMDK VQLAITDGAC LAIAKMALQK
KTGARGLRSI MERLLLDSMF EVPGSDIVEI IIDEDVVNGR KSPVYISDSS QASKPSTEES
DNQFSDDIVS ENYVRKSADA IQA
//