ID A0A0V1BVH6_TRISP Unreviewed; 700 AA.
AC A0A0V1BVH6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Caseinolytic peptidase B-like protein {ECO:0000313|EMBL:KRY40936.1};
GN Name=Clpb {ECO:0000313|EMBL:KRY40936.1};
GN ORFNames=T01_6447 {ECO:0000313|EMBL:KRY40936.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY40936.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY40936.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY40936.1};
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:KRY40936.1}.
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DR EMBL; JYDH01000010; KRY40936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1BVH6; -.
DR eggNOG; KOG1051; Eukaryota.
DR Proteomes; UP000054776; 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; 1.25.40.20; 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; 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:UP000054776}.
FT DOMAIN 7..95
FT /note="Roadblock/LAMTOR2"
FT /evidence="ECO:0000259|SMART:SM00960"
FT REPEAT 226..258
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 295..327
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 403..552
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 700 AA; 79834 MW; 3944C88F7AC7B58B CRC64;
MIRPTVLNSI LCQANAEGLT GTLLMNREGM VLCHAGCDES RAEAIAAIAS NIWCSYEKSG
QETFRDDKLK WFFLEGSEGR IAICKVATLL LCMVANNTVE IGMLRSKLHA VKHCLEPEKC
ENINMWRLFA SRMRRHCYWV WLRSYFRYLG CRFAVAPFLR KINANDGWFY GFTFYTTYEF
SGMNGDRNHG EDIRKMQLMY AARDDDERTI KKLLQSGVDP NERHFLGWTA LHVASFHGSC
KALKVLLENG ADVNTKDNFS NVQTVARDMR ISFLEALFIR EEFFNFQLNK NIEFRNMTPL
HYAVLGNNKP AVEMLMEYGA DPLSSNESGQ LPVNYAQNQQ IEELLKGYTK KYTEKKALLE
RLERQNYPFE ERVKKNMIGQ DGAISSVASA IRRRENGWTN DEHPLVFLFL GSSGVGKTEL
AKQVAQYLYK DNKKSFIRID MSEYQEKHEV AKFIGSPPGY VGHQQGGQLT KSLTECPNAV
VLFDEVEKAH PDVLTIMLQL FDEGRLTDGM GKTVDCKEAI FIMTSNLAAE EIASHALKLR
KETADMVEKR LSNTLEDLNE AENVTISRKF KETVVQPILK RHLKRDEFIG RITEILVTRE
LEFWKMKALQ KHKIHLTWDQ NVLEVLADGY NVRYGARSIK HEIERQVVSK LAAAHERSLI
NDGSEVRISA TLPPGEQDRS KSIITIDVVN SNSGKGSANL
//