ID A0A672I297_SALFA Unreviewed; 624 AA.
AC A0A672I297;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit {ECO:0000313|Ensembl:ENSSFAP00005035185.1};
GN Name=clpx {ECO:0000313|Ensembl:ENSSFAP00005035185.1};
OS Salarias fasciatus (Jewelled blenny) (Blennius fasciatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Blenniimorphae; Blenniiformes; Blennioidei; Blenniidae;
OC Salariinae; Salarias.
OX NCBI_TaxID=181472 {ECO:0000313|Ensembl:ENSSFAP00005035185.1, ECO:0000313|Proteomes:UP000472267};
RN [1] {ECO:0000313|Ensembl:ENSSFAP00005035185.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A672I297; -.
DR Ensembl; ENSSFAT00005036515.1; ENSSFAP00005035185.1; ENSSFAG00005016757.1.
DR InParanoid; A0A672I297; -.
DR OMA; HRSDFTN; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000472267; Unplaced.
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:UP000472267};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 84..137
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 63..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 68517 MW; 8F457E58AAC4D2D6 CRC64;
MSCPCTSAAR VFLTTAHRGL SCSRIQLYSL SRQGFRETHL PSRVRVRSFS ETAVCYAAKD
GTTKDGGNDS GKKSISEGKR LSGSGGSGKG GSQLRCPKCG DPCTHVETFV SSTRFVKCEK
CHHFFVVLSE TDSKKGLNKE PESAAEAVKL AFAQKPPPPP KKIYAYLDKY VVGQSYAKKV
LAVAVYNHYK RIYNNIPAGS RQQVEVEKQP SLTPRELEMR RREDEYRFTK LLQIAGISPH
GNALGASMQQ QASQQAPQER RGGEVLDSTH TDIKLEKSNI ILLGPTGSGK TLLAQTLARC
LDVPFAICDC TTLTQAGYVG EDIESVIAKL LQDANYSVEK AQQGIVFLDE VDKIGSVPGI
HQLRDVGGEG VQQGLLKLLE GTIVNVPEKN SRKLRGETVQ VDTTNILFVA SGAFNGLDRI
ISRRKNEKYL GFGTPSNLGK GRRAAAAADL ANTSGETDTV AEIEEKDRLL KHVEARDLIE
FGMIPEFVGR LPVVVPLHSL DEETLVRILT EPRNAVVPQY QALFSMDKCE LNVTPDALRA
IARMALERKT GARGLRSIME KLLLEPMFEV PHSDIMAVEM DKEVVLGKSQ PRYIRAPAKD
AAEEEYDSGI EEENWPRQAD AANN
//