ID A0A0V0WRB2_9BILA Unreviewed; 644 AA.
AC A0A0V0WRB2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial {ECO:0000313|EMBL:KRX77827.1};
GN Name=Clpx {ECO:0000313|EMBL:KRX77827.1};
GN ORFNames=T06_13482 {ECO:0000313|EMBL:KRX77827.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX77827.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX77827.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX77827.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX77827.1}.
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DR EMBL; JYDK01000076; KRX77827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WRB2; -.
DR STRING; 92179.A0A0V0WRB2; -.
DR Proteomes; UP000054673; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 InterPro; IPR010603; Znf_CppX_C4.
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.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KRX77827.1};
KW Hydrolase {ECO:0000313|EMBL:KRX77827.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KRX77827.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 105..159
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 59..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 70570 MW; CBA38DD070AF21EB CRC64;
MISWVNLLNG KMLCTLRPVM RVAYRRLILR SINNDLEYID GKSGASRLPR FTSIRQVRGG
VHSSHYGSRQ GDRSGSNDAK PPQEISSNSQ SENCSSTTAG GDGGSEGDDG GRSTLMNCPK
CGEPCVHVET FVSSTRFVKC EKCLHFFVVL SENDTKKSMF DVANSQSHRK PPPPPKEIYN
YLDKFVVGQE QAKKVLSVAV YNHYKRVYLC PRPVPGSKND NGDSSRPVTP MMTTKGKCLF
VHAWIWMCCI CGMIKIVENV FDNFSTFPSG VHYGPGAIDD VPPPPQRKST AEIIGDESKP
ELRLEKSNIL LLGPTGCGKT LLAQTVAQCL DVPFAICDCT TLTQAGYVGE DVESVISRLL
QDANYNVEKA QMGIVFLDEV DKIGAVPGIH QLRDVGGEGV QQALLKMLEG SVVNVPQHGS
RKLRGENIQV DTTNVLFVAS GAFNGLDKIV GRRKHSKYLG FGAITNDDSP GRRAAALADV
ASLDSTANPD LELAEKDALL REVEAHDLIE FGMIPEFVGR LPVLVQFHSL DQNLLVRILT
EPQNSLIAQY RALFTMDQID LHFTDDALNA IARLALQKKT GARGLRAIVE NILLDPMFEC
PGTDVSSVTV TADAVNKIKP VDLVRRNKGA ENVKHEREMV TTQT
//
