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Database: UniProt
Entry: A0A663EKV7_AQUCH
LinkDB: A0A663EKV7_AQUCH
Original site: A0A663EKV7_AQUCH 
ID   A0A663EKV7_AQUCH        Unreviewed;       630 AA.
AC   A0A663EKV7;
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:ENSACCP00020012813.1};
GN   Name=CLPX {ECO:0000313|Ensembl:ENSACCP00020012813.1};
OS   Aquila chrysaetos chrysaetos.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Aquila.
OX   NCBI_TaxID=223781 {ECO:0000313|Ensembl:ENSACCP00020012813.1, ECO:0000313|Proteomes:UP000472275};
RN   [1] {ECO:0000313|Ensembl:ENSACCP00020012813.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A663EKV7; -.
DR   Ensembl; ENSACCT00020013399.1; ENSACCP00020012813.1; ENSACCG00020008811.1.
DR   GeneTree; ENSGT00390000017625; -.
DR   InParanoid; A0A663EKV7; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000472275; 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:UP000472275};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          90..143
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          64..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  69075 MW;  8DEAF73DDEEB7D71 CRC64;
     MSACHSCAAA ARLLGSTLPS ARRGITCGRT RIPVLGKLGT FETCSLRRIP LRNFSETPAY
     FASKDGASKE GSGDGSKKSV GEGGGKKTSS GSSGKGGNQL RCPKCGDLCT HVETFVSSTR
     FVKCEKCHHF FVVLSEADTK KSIIKEPELA AEAVKLAFQQ KPPPPPKKIY NYLDKYVVGQ
     CFAKKVLSVA VYNHYKRIYN NIPANLRQQA EVEKQNSLTP RELEIRRRED EYRFTKLLQI
     AGISPHGNAL GASMQQQMNQ QIPQEKRGGE VLDSPNDDIK LEKSNILLLG PTGSGKTLLA
     QTLAKCLDVP FAICDCTTLT QAGYVGEDIE SVIAKLLQDA NYNVEKAQQG IVFLDEVDKI
     GSVPGIHQLR DVGGEGVQQG LLKLLEGTIV NVPEKNSRKL RGETVQVDTT NILFVASGAF
     NGLDRIISRR KNEKYLGFGT PSNMGKGRRA AAAADLANIS GESDPHEDIE EKDRLLRHVE
     ARDLIEFGMI PEFVGRLPVV VPLHSLDEKT LVRILTEPRN AVVPQYQALF SMDKCELNVT
     EDALKAIARL ALDRKTGARG LRSIMEKLLL EPMFEVPNSD IVCVEVDKDV VEGKKEPGYI
     RAPTKDSSEE EYDSGVEEEG WPRQADAANH
//
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