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
//