ID A0A094ENN3_9PEZI Unreviewed; 426 AA.
AC A0A094ENN3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=V499_00931 {ECO:0000313|EMBL:KFY80174.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY80174.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY80174.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY80174.1,
RC ECO:0000313|Proteomes:UP000029295};
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:KFY80174.1}.
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DR EMBL; JPKB01000101; KFY80174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094ENN3; -.
DR HOGENOM; CLU_031812_1_2_1; -.
DR Proteomes; UP000029295; 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 Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 202..293
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 426 AA; 45181 MW; 6382CEFD752D0116 CRC64;
MTLIRSTLPV TESVPVQSHD SISYDIAKAI IFDNIDSHDA DLQGINHKIH ANPELCFEEF
QAHDNLADFL ESHNFTVTRH AHGLPTAFSA EFGSGGRVLT FCAEYDALPG IGHACGHNLI
AVTSVASFLG IAAALAASSI PGRVHLLRTP AEEGGGGKIK LIDAGAFSDV DASMMIHPVG
KDAVPAGTAG VAYGTCLTGQ IGNVEFTGKA AHCGTAPWEG INALDAATLA YSAIGMLRQQ
MRPENRSGIV IKEGGQKSNI TTPHTTIEYS IRTRTLKEAK SIKTRVENCF RGAALATACE
VVFKDAMGVY ADLRSNETLC NEFTSAMSEL GELYHNNIAS NTAASFGTDM GNVSHVVPTF
HGLFAIAAAK GEANHTPDFK RIAISNEAYK SAINAAKGMA ITGWKFLADD SVAESILLDF
ERLSQL
//
