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Database: UniProt
Entry: H0V6H2_CAVPO
LinkDB: H0V6H2_CAVPO
Original site: H0V6H2_CAVPO 
ID   H0V6H2_CAVPO            Unreviewed;       675 AA.
AC   H0V6H2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   SubName: Full=ClpB homolog, mitochondrial AAA ATPase chaperonin {ECO:0000313|Ensembl:ENSCPOP00000005291.2};
GN   Name=CLPB {ECO:0000313|Ensembl:ENSCPOP00000005291.2};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000005291.2, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000005291.2}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000005291.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   EMBL; AAKN02051221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02051222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02051223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02051224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0V6H2; -.
DR   Ensembl; ENSCPOT00000005928.3; ENSCPOP00000005291.2; ENSCPOG00000005865.4.
DR   VEuPathDB; HostDB:ENSCPOG00000005865; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   GeneTree; ENSGT00390000012961; -.
DR   HOGENOM; CLU_005070_9_3_1; -.
DR   TreeFam; TF328654; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000005865; Expressed in testis and 12 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   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF93; CASEINOLYTIC PEPTIDASE B PROTEIN HOMOLOG; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00248; ANK; 4.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT   REPEAT          133..165
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          166..198
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          235..267
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          343..487
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          541..630
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   675 AA;  75847 MW;  28BCED8A6D26A18D CRC64;
     TMLGSLVLRS APAPRNLLRL LRASSIQSRG IASSRTIISE DRGELQWLRA TAGGHRGTSL
     ALLLGRGAAT WGRQGGRTKT QCLTTPTSGH LPSPEEIVPG QDNWNGFSNP AGLGVWALAT
     ALVVHCYSKN PSDKDAALME AARTNNIQEL NRLLSQGADI NARHRLGWTA LMVAAINRND
     SVVQILLAAG ADPNLGDDFS SVYKTAKEQG IHSLEVLVTR EDDFNNRLNN RASFKGCTAL
     HYAVLADDYR TVKELLDGGA NPLQRNEMGH TPLDYAREGE VMKLLRTSEA KYQEKQRKRE
     AEERRRFPLE QRLREHIIGQ ENAITTVGAA IRRKENGWYD EEHPLVFLFL GSSGIGKTEL
     AKQTAKYMHK DAKKGFIRLD MSEFQERHEV AKFIGSPPGY IGHEEGGQLT KKLKQCPNAV
     VLFDEVDKAH PDVLTIMLQL FDEGRLTDGK GKTIDCKDAI FIMTSNVASD EIAQHALQLR
     QEALEISRNR IAENLGDVQI SDKITISKNF KENVIRPILK AHFRRDEFLG RINEIVYFLP
     FCHSELIQLV NKELNFWAKR AKQRHNITLL WDREVADVLV DGYNVHYGAR SIKHEVERRV
     VNQLAAAYEQ DLLPGGCTLR ITVEDSDKQL LKSPELPQAE KRTPKLRLEI IDKDSKTHKL
     DIRTPLHPEK VCYTI
//
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