ID A0A0V0TUV6_9BILA Unreviewed; 594 AA.
AC A0A0V0TUV6;
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:KRX42779.1};
GN Name=Clpx {ECO:0000313|EMBL:KRX42779.1};
GN ORFNames=T05_2761 {ECO:0000313|EMBL:KRX42779.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX42779.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX42779.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX42779.1};
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:KRX42779.1}.
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DR EMBL; JYDJ01000135; KRX42779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TUV6; -.
DR STRING; 144512.A0A0V0TUV6; -.
DR Proteomes; UP000055048; 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:KRX42779.1};
KW Hydrolase {ECO:0000313|EMBL:KRX42779.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KRX42779.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 94..148
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 48..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 64872 MW; F13B42C3189AAA34 CRC64;
MLCTLRPVMR VAYRRLILRS INNDLEYIDG KSGASRLPRF TSIRQVRGGV HSSHYGSRQG
DRSGSNDAKP PQEISSNSQS ENCSSTTAGG DGGSEGDDGG RSTLMNCPKC GEPCVHVETF
VSSTRFVKCE KCLHFFVVLS ENDTKKSMFD VANSQSHRKP PPPPKEIYSY 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
//