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Database: UniProt
Entry: A0A6Q2Z8U1_ESOLU
LinkDB: A0A6Q2Z8U1_ESOLU
Original site: A0A6Q2Z8U1_ESOLU 
ID   A0A6Q2Z8U1_ESOLU        Unreviewed;       628 AA.
AC   A0A6Q2Z8U1;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial {ECO:0000313|Ensembl:ENSELUP00000074150.1};
GN   Name=CLPX {ECO:0000313|Ensembl:ENSELUP00000074150.1};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000074150.1, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000074150.1, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000074150.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_019895911.1; XM_020040352.1.
DR   AlphaFoldDB; A0A6Q2Z8U1; -.
DR   Ensembl; ENSELUT00000067421.1; ENSELUP00000074150.1; ENSELUG00000020619.2.
DR   GeneTree; ENSGT00390000017625; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000265140; LG19.
DR   Bgee; ENSELUG00000020619; Expressed in camera-type eye and 14 other cell types or tissues.
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:UP000265140};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          85..138
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          248..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   628 AA;  68603 MW;  E64EF4670ADC3D68 CRC64;
     MSCPCASAAR IFLNSAHRGL TCSRIQLYAL SRPGSREATV PHRVCVRSFH ETAVCFASKD
     GTTKDGPGDG GKKSIGEGKR LSGSSGGSGK GGNQLRCPKC GDPCTHVETF VSSTRFVKCE
     KCHHFFVVLS ETDSKKGLNK EPESAGDAVK MAFAQKPPPP PKKIYAYLDK YVVGQSYAKK
     VLAVAVYNHY KRIYNNIPPG SKPQQQVEVE KQASLTPREL EMRRREDEYR FTKLLQIAGI
     SPHGNALGAS MQQQATQQPA QERRGGDVLD STHTDIKLEK SNIVLLGPTG SGKTLLAQTL
     AKCLDVPFAI CDCTTLTQAG YVGEDIESVI AKLLQDANYS VDKAQQGIVF LDEVDKIGSV
     PGIHQLRDVG GEGVQQGLLK LLEGTIVNVP EKNSRKLRGE TVQVDTTNIL FVASGAFNGL
     DRIISRRKNE KYLGFGTPSN MGKGRRAAAA ADLANSSEQT DMVAEIEEKD RLLKLVEARD
     LIEFGMIPEF VGRLPVVVPL HSLDEETLVR ILTEPRNAVI PQYQALFSMD KCELNVTTDA
     LRAIARLALE RKTGARGLRS IMEKLLLEPM FEVPCSDIMA VELTKDVVQG KADPVYIRAP
     AKETSEEEYD SGIEEENWPR QADAAANN
//
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