ID A0A0V1CUA9_TRIBR Unreviewed; 604 AA.
AC A0A0V1CUA9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial {ECO:0000313|EMBL:KRY52874.1};
DE Flags: Fragment;
GN Name=Clpx {ECO:0000313|EMBL:KRY52874.1};
GN ORFNames=T03_12952 {ECO:0000313|EMBL:KRY52874.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52874.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY52874.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY52874.1};
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:KRY52874.1}.
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DR EMBL; JYDI01000097; KRY52874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CUA9; -.
DR STRING; 45882.A0A0V1CUA9; -.
DR Proteomes; UP000054653; 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:KRY52874.1};
KW Hydrolase {ECO:0000313|EMBL:KRY52874.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KRY52874.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 104..158
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 58..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY52874.1"
SQ SEQUENCE 604 AA; 65995 MW; 70D47B7EA445F8FE CRC64;
LIMVNLLNGK MLCTLRPVMR VAYRRLILRS INNDLEYIDG KSGASRLPRF TSIRQVRGGV
HSSHYGSRQG DRSGSNDAKP PQEISSNSQS ENCSSTTAGG DGGSEGDDGG RSTLMNCPKC
GEPCVHVETF VSSTRFVKCE KCLHFFVVLS ENDTKKSMFD VANSQSHRKP PPPPKEIYNY
LDKFVVGQEQ AKKVLSVAVY NHYKRVYLCP RPVPGSKNDN ENVFDNFSTF PSGVHYGPGA
IDDVPPPPQR KSTAEIIGDE SKPELRLEKS NILLLGPTGC GKTLLAQTVA QCLDVPFAIC
DCTTLTQAGY VGEDVESVIS RLLQDANYNV EKAQMGIVFL DEVDKIGAVP GIHQLRDVGG
EGVQQALLKM LEGSVVNVPQ HGSRKLRGEN IQVDTTNVLF VASGAFNGLD KIVGRRKHSK
YLGFGAITND DSPGRRAAAL ADVASLDSTA NPDLELAEKD ALLREVEAHD LIEFGMIPEF
VGRLPVLVQF HSLDQNLLVR ILTEPQNSLI AQYKALFTMD QIDLHFTDDA LNAIARLALQ
KKTGARGLRA IVESILLDPM FECPGTDVSS VTVTADAVNK IKPVDLVRRN KGAENVKHER
EMVV
//
