ID S7MV70_MYOBR Unreviewed; 599 AA.
AC S7MV70;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Caseinolytic peptidase B protein like protein {ECO:0000313|EMBL:EPQ08349.1};
GN ORFNames=D623_10028643 {ECO:0000313|EMBL:EPQ08349.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ08349.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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DR EMBL; KE162454; EPQ08349.1; -; Genomic_DNA.
DR AlphaFoldDB; S7MV70; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 2.
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; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
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; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
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:UP000052978}.
FT REPEAT 19..51
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 52..84
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 265..409
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 463..552
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 599 AA; 67857 MW; 45D632D9E8E48569 CRC64;
MWALATALVV HCYSKSPSNK DAALMEAARA NNVQEVSRLL SEGADVNTRH KLGWTALMVA
AISRNDSVVQ VLLAAGADPN LGDNFSSVYK TAKEQGIHSL EVLVTREDDF NNRLNNRASF
KGCTALHYAA LADDYRTVKE LLNGDLMEQN ITVKICVRDK QAKQDQAYLL PLETSFQITS
GANPLQRNEM GHTPLDYARE GEVMKLLRTS EAKYQEKQRK REAEERRRFP LEQRLKEHII
GQESAIATVG AAIRRKENGW YDEEHPLVFL FLGSSGIGKT ELAKQTAKYM HKDAKKGFIR
LDMSEFQERH EVAKFIGSPP GYIGHEEGGQ LTKKLKQCPN AVVLFDEVDK AHPDVLTIML
QLFDEGRLTD GKGKTIDCKD AIFIMTSNVA SDEIAQHALQ LRQEALEMSH NRIAENLGDV
QISDKITISK NFKENVIRPI LKAHFRRDEF LGRINEIVYF LPFCHSELIQ LVNKELNFWA
KRAKQRHNIT LLWDREVADV LVDGYNVHYG ARSIKHEVER RVVNQLAAAY EQDLLPGGCT
LRITVEDSDK QLLKSPDLPS PQTEKRSPTL RLEIIDKDSK THKLDIRAPL HPEKVCHTL
//
