ID A0A0A1TFY7_9HYPO Unreviewed; 433 AA.
AC A0A0A1TFY7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=VHEMI04308 {ECO:0000313|EMBL:CEJ87116.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ87116.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ87116.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247, ECO:0000256|PIRNR:PIRNR037226}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CDHN01000002; CEJ87116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1TFY7; -.
DR HOGENOM; CLU_031812_1_2_1; -.
DR OrthoDB; 1074531at2759; -.
DR Proteomes; UP000039046; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR CDD; cd05672; M20_ACY1L2-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR017144; Xaa-Arg_dipeptidase.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CEJ87116.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000039046};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 202..292
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 433 AA; 45782 MW; 060ACAFEF412C9F5 CRC64;
MTNVTTNGNG AQPKSAAPGT DAAFAAIDGL DTELRAINKK IWENPETSYE EVQAHDNIVA
MLRSLGFEVT PHAFGVQTSF SCEVGTGGRV VVYNAEYDAL PDIGHACGHN LIATSSIASF
LGVAAALKAS GGPGRVRLYG TPAEEGGAGK VRLINAGAYK DVDACLMVHP GPPNPPPQSA
DGHGCCAPSG VAYATSLANR KFDVTFTGRE AHAALAPYQG RNALDAVVLG YNGVSMLRQQ
TRPHDRIHSV IKAGGTRPNV ITSFTKTQYY VRSASIREAT ALEQRVRNCL DGAATATECS
IEYDEHEEYA DLRPNRTICS LYADAMALPA IDSKVECDFE HAPALSGSTD QGNVSYVVPS
FHGGFSIPCP PGAYNHTKPF TACAGTPEAH DLAIAASKGM AAAGLTILTD EAVAKKIWED
FKLDREQDKQ EIV
//