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Database: UniProt
Entry: A0A090LEL7_STRRB
LinkDB: A0A090LEL7_STRRB
Original site: A0A090LEL7_STRRB 
ID   A0A090LEL7_STRRB        Unreviewed;       353 AA.
AC   A0A090LEL7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Peptidase M20 family and Peptidase M20, dimerisation domain-containing protein {ECO:0000313|EMBL:CEF68191.1, ECO:0000313|WBParaSite:SRAE_2000284900.1};
GN   ORFNames=SRAE_2000284900 {ECO:0000313|EMBL:CEF68191.1,
GN   ECO:0000313|WBParaSite:SRAE_2000284900.1,
GN   ECO:0000313|WormBase:SRAE_2000284900};
OS   Strongyloides ratti (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF68191.1};
RN   [1] {ECO:0000313|EMBL:CEF68191.1, ECO:0000313|Proteomes:UP000035682}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC   ECO:0000313|WBParaSite:SRAE_2000284900.1}, and ED321 Heterogonic
RC   {ECO:0000313|EMBL:CEF68191.1};
RA   Martin A.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SRAE_2000284900.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; LN609529; CEF68191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090LEL7; -.
DR   STRING; 34506.A0A090LEL7; -.
DR   MEROPS; M20.A16; -.
DR   EnsemblMetazoa; SRAE_2000284900.1; SRAE_2000284900.1; WBGene00263063.
DR   WBParaSite; SRAE_2000284900.1; SRAE_2000284900.1; WBGene00263063.
DR   WormBase; SRAE_2000284900; SRP02182; WBGene00263063; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   OMA; NCDVDGF; -.
DR   OrthoDB; 2875217at2759; -.
DR   Proteomes; UP000035682; Chromosome X.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          172..269
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   353 AA;  38829 MW;  CCCDB28A43858500 CRC64;
     MSIISKLGKK NVSDLLVSLM KIESTTGNEG TLCKELKQYM EDNNWVVYEQ PMKNNEKRNN
     LLITRKGVNV KDIKILFNSH LDTVPPYIPP RVENGIIYGR GANDAKGQVA AMIVAGEKLI
     EENENLGKNI GFLFVVGEET DHIGMITANE LNLQPDYMII GEPTENIFGS LQKGAAKLEI
     HCTGIPAHSG YPEKGISAIE KLLDILNDIR NYNWPKNEIV GNTTCNIGFI KGGQALNALA
     GEASAQLMFR ITTSVEDITS KLASIVGEKG EIKVFGSNEP VQLSSPPLGY KSQSVSFNTD
     LPYFKNKDKL KGVYLYGGGS ITNAHSENEY IKIDDLEEAV KTYVTLAKYF LSS
//
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