ID A0A2K5XK51_MANLE Unreviewed; 677 AA.
AC A0A2K5XK51;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit B {ECO:0000313|Ensembl:ENSMLEP00000003696.1};
GN Name=CLPB {ECO:0000313|Ensembl:ENSMLEP00000003696.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000003696.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000003696.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_011849049.1; XM_011993659.1.
DR AlphaFoldDB; A0A2K5XK51; -.
DR Ensembl; ENSMLET00000017693.1; ENSMLEP00000003696.1; ENSMLEG00000015735.1.
DR GeneID; 105549229; -.
DR CTD; 81570; -.
DR GeneTree; ENSGT00390000012961; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000233140; Unplaced.
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; 2.
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:UP000233140}.
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..497
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"
FT REGION 51..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 75660 MW; 156BD0DE3AB15999 CRC64;
MLGSLVLRRK ALAPRLLLRL LRSPTLRGHG GASGRNVTTG SLGEPQWLRA AAGGRPGTSP
ALFSGRGAAT GGRQGGRFDT KCLAAATWGR LLGPEETLPG QDSWNGVPNR ARLGMWALAT
ALVVHCYSKS PSNKDAALLE AARANNVQEV TRLLSEGADV NAKHRLGWTA LMVAAINRNN
SVVQVLLAAG ADPNLGDDFS SVYKTAKEQG IHSLEVLITR EDDFNNRLNN RASFKGCTAL
HYAVLADDYR TVKELLDGGA NPLQRNEMGH TPLDYAREGE VMKLLRTSET KYQEKQRKRE
AEERRRFPLE QRLKEHIIGQ ESAIATVGAA IRRKENGWYD EEHPLVFLFL GSSGIGKTEL
AKQTAKYMHK DAKKGFIRLD MSEFQERHEV AKFIGSPPGY VGHEEGGQLT KKLKQCPNAV
VLFDEVDKAH PDVLTIMLQL FDEGRLTDGK GKTIDCKDAI FIMTSNVASD EIAQHALQLR
QEALEMSRNR IAENLGDVQI SDKITISKNF KENVIRPILK AHFRRDEFLG RINEIVYFLP
FCHSELIQLV NKELNFWAKR AKQRHNITLL WDREVADVLV DGYNVHYGAR SIKHEVERRV
VNQLAAAYEQ DLLPGGCTLR ITVEDSDKQL LKSPELPSPQ TEKRLPKLRL EIIDKDSKTR
KLDIRAPLHP EKVCNTI
//