ID A0A4W6D800_LATCA Unreviewed; 606 AA.
AC A0A4W6D800;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit X {ECO:0000313|Ensembl:ENSLCAP00010020850.1};
GN Name=CLPX {ECO:0000313|Ensembl:ENSLCAP00010020850.1};
OS Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010020850.1, ECO:0000313|Proteomes:UP000314980};
RN [1] {ECO:0000313|Proteomes:UP000314980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sai Rama Sridatta P.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLCAP00010020850.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A4W6D800; -.
DR Ensembl; ENSLCAT00010021307.1; ENSLCAP00010020850.1; ENSLCAG00010009631.1.
DR GeneTree; ENSGT00390000017625; -.
DR Proteomes; UP000314980; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
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.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000314980};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..606
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021247314"
FT DOMAIN 80..133
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 58..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 66157 MW; 8AF742902BF8863C CRC64;
NSGSTCQSKL MLLFVTGLSC SRIQFFSLSR QGSRETPLPT RVRVRSFSET AVCYASKDGT
TKDGDGGKKS ISEGKRLSGS GGSGKGGSQL RCPKCGDPCT HVETFVSSTR FVKCEKCHHF
FVVLSETDSK KGLNKEPESA AEAVKLAFAQ KPPPPPKKIY AYLDKYVVGQ SYAKKVLAVA
VYNHYKRIYN NIPAGSRQQV EVEKQPSLTP RELLQIAGIS PHGNALGASM QQQASQQAPQ
EKRGGEVLDS THTDIKLEKS NIILLGPTGS GKTLLAQTLA RCLDVPFAIC DCTTLTQAGY
VGEDIESVIA KLLQDANYSV EKAQQGIVFL DEVDKIGSVP GIHQLRDVGG EGVQQGLLKL
LEGTIVNVPE KNSRKLRGET VQVDTTNILF VASGAFNGLD RIISRRKNEK YLGFGTPSNL
GKGRRAAAAA DLANTSGETD TVAEIEEKDR LLKHVEARDL IEFGMIPEFV GRLPVVVPLH
SLDEETLVRI LTEPRNAVVP QYQALFSMDK CDLNVTQDAL RAIARMALER KTGARGLRSI
MEKLLLEPMF EVPHSDIVAV ELDRDVVQGK SQPRYIRTPA KESAEEEYDS GIEEENWPRQ
ADAANN
//