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Database: UniProt
Entry: A0A3Q1MW31_BOVIN
LinkDB: A0A3Q1MW31_BOVIN
Original site: A0A3Q1MW31_BOVIN 
ID   A0A3Q1MW31_BOVIN        Unreviewed;       618 AA.
AC   A0A3Q1MW31;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit X {ECO:0000313|Ensembl:ENSBTAP00000059506.1};
GN   Name=CLPX {ECO:0000313|Ensembl:ENSBTAP00000059506.1,
GN   ECO:0000313|VGNC:VGNC:27462};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000059506.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000059506.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000059506.1,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000059506.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000059506.1};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   RefSeq; XP_010807298.1; XM_010808996.1.
DR   AlphaFoldDB; A0A3Q1MW31; -.
DR   Ensembl; ENSBTAT00000067946.1; ENSBTAP00000059506.1; ENSBTAG00000008386.6.
DR   VEuPathDB; HostDB:ENSBTAG00000008386; -.
DR   VGNC; VGNC:27462; CLPX.
DR   GeneTree; ENSGT00390000017625; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000008386; Expressed in semen and 109 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1MW31; baseline and differential.
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:UP000009136};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          78..131
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          53..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  68080 MW;  95D4C8C0F5CB3AEE CRC64;
     CVDQTNFIVF SGISCSRIHI PVLGRLGTFE TQLLRRAPFR AFTETPAYFA SRDGISKDGS
     GDGNKKSASE GSSKKSGSGN SGKGGNQLRC PKCGDLCTHV ETFVSSTRFV KCEKCHHFFV
     VLSEADSKKS IIKEPESAAE AVKLAFQQKP PPPPKKIYNY LDKYVVGQSF AKKVLSVAVY
     NHYKRIYNNI PANLRQQAEV EKQTSLTPRE LEIRRREDEY RFTKLLQIAG ISPHGNALGA
     SVQQQVNQQI PQEKRGGEVL DSSHDDIKLE KSNILLLGPT GSGKTLLAQT LAKCLDVPFA
     ICDCTTLTQA GYVGEDIESV IAKLLQDANY NVEKAQQGIV FLDEVDKIGS VPGIHQLRDV
     GGEGVQQGLL KLLEGTIVNV PEKNSRKLRG ETVQVDTTNI LFVASGAFNG LDRIISRRKN
     EKYLGFGTPS NLGKGRRAAA AADLANRSGE SNTHQDIEEK DRLLRHVEAR DLIEFGMIPE
     FVGRLPVVVP LHSLDEKTLV QILTEPRNAV IPQYQALFSM DKCELNVTED ALKAIARLAL
     ERKTGARGLR SIMEKLLLEP MFEVPNSDIV CVEVDKEVVE GKKEPGYIRA PTKESSEEEY
     DSGVEEEGWP RQADAANS
//
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