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Database: UniProt
Entry: A0A0A1TFY7_9HYPO
LinkDB: A0A0A1TFY7_9HYPO
Original site: A0A0A1TFY7_9HYPO 
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}.
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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
//
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