ID A0A094I0A7_9PEZI Unreviewed; 442 AA.
AC A0A094I0A7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=V501_00074 {ECO:0000313|EMBL:KFZ20542.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ20542.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ20542.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ20542.1}.
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DR EMBL; JPKD01000025; KFZ20542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094I0A7; -.
DR HOGENOM; CLU_031812_1_2_1; -.
DR Proteomes; UP000029315; 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 Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 210..301
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 442 AA; 47140 MW; 1DEEFCF8368511E7 CRC64;
MKLVDSPVIE GTVGLRQSTV PSKESSTATD TIINTINGYD SKLRAINKKI FDNPELGYKE
FQAHDNIVAL LHSLGFEVTP HAFGLATSFS CEVGTGGRVV VYNAEYDALP GIGHACGHNL
IATSSIASFL GLAAALRASN LPGRVRLYGT PAEEGGGGKL KLIDAGAYKD VDACLMVHPG
PPRPAPKSHD GHGCCVPTGL SYGTSLANKK FNVTYTGRPA HAAMAPYQGR NALDAVVLSY
NGVSMLRQQT RPYDRIHSVI LDGGRVPNVI TSFTKSEYYV RSATLKEATA LEERVKACLD
GAATATGCEI EYEVENEYAD LRPNRTICTL YAEAMSLPSI NSPVTCDFSN TEPGPGSTDQ
GNVSYVVPSF HGGFAIPCPP GAYNHTPGFT ACAGTDEAHD LAVVTSKGMA IAGWKVLSEE
AVAEKIWEDF EKDRREVDVE PY
//
