ID A0A0V1PP63_9BILA Unreviewed; 696 AA.
AC A0A0V1PP63;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Caseinolytic peptidase B-like protein {ECO:0000313|EMBL:KRZ98037.1};
GN Name=Clpb {ECO:0000313|EMBL:KRZ98037.1};
GN ORFNames=T08_1046 {ECO:0000313|EMBL:KRZ98037.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ98037.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ98037.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ98037.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GAMAD family.
CC {ECO:0000256|ARBA:ARBA00007191}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ98037.1}.
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DR EMBL; JYDM01000001; KRZ98037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PP63; -.
DR STRING; 92180.A0A0V1PP63; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
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; 3.30.450.30; Dynein light chain 2a, cytoplasmic; 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 InterPro; IPR004942; Roadblock/LAMTOR2_dom.
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; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR Pfam; PF03259; Robl_LC7; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SMART; SM00960; Robl_LC7; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF103196; Roadblock/LC7 domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 3: Inferred from homology;
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:UP000054924}.
FT DOMAIN 7..95
FT /note="Roadblock/LAMTOR2"
FT /evidence="ECO:0000259|SMART:SM00960"
FT REPEAT 205..237
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 274..306
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 382..531
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 580..664
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 696 AA; 78958 MW; 54C14121F043C897 CRC64;
MIRPTVLNSI LCQANAEGVT GTLLMNREGM VLCHAGCDES RAEAIAAIAS NIWCSYEKSG
QETFRDDKLK WFFLEGSEGR IAICKVATLL LCMVANDTVE IGMLRSKLHA VKHCLEPKHV
AIVRFTNAST LLFVAPFLRK INANDGWFYG FTFYTTYEFS GMNGDRNHGE DIRKMQLMYA
ARDDDERTIK QLLQSGVDPN ERHFLGWTAL HVASFHGSCK ALKVLLENGA DVNTKDNFSN
VQTVSRDMRI SFLEALFIRE EFFNFQMHKN IEFRNMTPLH YAVLGNNKPA VEMLMEYGAD
PLSSNESGQL PVNYAQNQQI EELLKGYTKK YTEKKALLER LERQNYPFEE RVKKNMIGQD
GAISSVASAI RRRENGWTND EHPLVFLFLG SSGVGKTELA KQVAQYLYKD NKKSFIRIDM
SEYQEKHEVA KFIGSPPGYV GHQQGGQLTK SLTECPNAVV LFDEVEKAHP DVLTIMLQLF
DEGRLTDGMG KTVDCKEAIF IMTSNLAAEE IASHALKLRK ETADMVEKRL SNTLEDLNEA
ENVTISRKFK ETVVQPILKR HLKRDEFIGR ITEIVYFLPF SRPELLQLVT RELEFWKMKA
LQKHKIHLTW DQNVLEVLAD GYNVRYGARS IKHEIERQVV SKLAAAHERS LINDGSEVRI
SATLPPGEQD RSKSIITIDV VNSNSGKGET FSITLD
//