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Database: UniProt
Entry: A0A0V1PP63_9BILA
LinkDB: A0A0V1PP63_9BILA
Original site: A0A0V1PP63_9BILA 
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
//
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