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
//