ID E3RJ48_PYRTT Unreviewed; 503 AA.
AC E3RJ48;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=PTT_08140 {ECO:0000313|EMBL:EFQ94243.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ94243.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ94243.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; GL533442; EFQ94243.1; -; Genomic_DNA.
DR RefSeq; XP_003297653.1; XM_003297605.1.
DR AlphaFoldDB; E3RJ48; -.
DR EnsemblFungi; EFQ94243; EFQ94243; PTT_08140.
DR KEGG; pte:PTT_08140; -.
DR eggNOG; ENOG502QPR4; Eukaryota.
DR HOGENOM; CLU_024588_2_0_1; -.
DR OrthoDB; 5491171at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR CDD; cd03884; M20_bAS; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 277..371
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 503 AA; 55681 MW; DF7CD51102427D25 CRC64;
MALLNSRFLV ALRIASRRYP TLKAGPARIS WEHVRRFSNS PQWQIRTKEM NDEMLKDLKV
NQKRLMDDIH HTCQWGIGER WGEKPTETGM SRLALSDTDK AARDWFAETT KALGCEVTVD
AMGNQFAVRP GLRNDKPPTY VGSHLDTQPT GGRYDGILGV TAGVEMLRVL ADNWTETEYP
VGVVNWTNEE GARFPMSMVA SGVWAGSIPL ETAHSLREVH PGTTTMKSEL ERIGYLGSIP
ASHEAMPMAA HFELHIEQGP LLEMANKKVG VVTGVQAYKW LTVRVKGRDT HTGTTDLKSR
ADALLTASKM IIHSHRLATA NCALASTGIL NLKPGSTNTV PGEVTFSLDI RSPKDVTVAK
MEELVLRDFA KIAAGEDVDG SNYGCTSALP LTVDITEDFD SPATNFHADC ITSVRQSANK
ILGPNQYMEM TSGAGHDSVY ASKRCPTSMI FVPCREGVSH NPREFCKEED CALGTQVLLQ
SVVRFDRMRD ERRVSWKQEP YTL
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