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Database: UniProt
Entry: A0A673CEW8_9TELE
LinkDB: A0A673CEW8_9TELE
Original site: A0A673CEW8_9TELE 
ID   A0A673CEW8_9TELE        Unreviewed;       622 AA.
AC   A0A673CEW8;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit {ECO:0000313|Ensembl:ENSSORP00005050648.1};
GN   Name=clpx {ECO:0000313|Ensembl:ENSSORP00005050648.1};
OS   Sphaeramia orbicularis (orbiculate cardinalfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX   NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005050648.1, ECO:0000313|Proteomes:UP000472271};
RN   [1] {ECO:0000313|Ensembl:ENSSORP00005050648.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A673CEW8; -.
DR   Ensembl; ENSSORT00005051863.1; ENSSORP00005050648.1; ENSSORG00005022724.1.
DR   Proteomes; UP000472271; 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:UP000472271};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          86..139
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          63..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  68533 MW;  4CBA5796B5F32FA3 CRC64;
     NNNCKWCLVQ KVMVFAVIFT GLSCSRIQLY SLSRQGSREA HLIPRVRVRS FSETAICYAS
     KDGTTKDSGS DGGKKSISEG KRLSGSGGSG KGGSQLRCPK CGDPCTHVET FVSSTRFVKC
     EKCHHFFVVL SETDSKKGLN KEPESAAEAV KLAFVRTKNT IYAYLDKYVV GQSYAKKVLA
     VAVYNHYKRI YNNIPAGSRQ QVEVEKQPSL TPRELEMRRR EDEYRFTKLL QIAGISPHGN
     ALGASMQQQA SQQAPQERRG GEVLDSTHAD IKLEKSNIIL LGPTGSGKTL LAQTLARCLD
     VPFAICDCTT LTQAGYVGED IESVIAKLLQ DANYSVEKAQ QGIVFLDEVD KIGSVPGIHQ
     LRDVGGEGVQ QGLLKLLEGT IVNVPEKNSR KLRGETVQVD TTNILFVASG AFNGLDRIIS
     RRKNEKYLGF GTPSNLGKGR RAAAAADLAN TSGETDTVAE IEEKDRLLKH VEARDLIEFG
     MIPEFVGRLP VVVPLHSLDE DTLVRILTEP RNAVVPQYQA LFSMDKCELN MTQDALRAIA
     RMALERKTGA RGLRSIMEKL LLEPMFEVPH SDIMAVELNK DVVHGKSEPR YIRAPAKESA
     EEEYDSGIEE ENWPRQADAA NN
//
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