ID A0A093XGT0_9PEZI Unreviewed; 579 AA.
AC A0A093XGT0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=V490_05702 {ECO:0000313|EMBL:KFX91838.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX91838.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX91838.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX91838.1,
RC ECO:0000313|Proteomes:UP000029320};
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}.
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:KFX91838.1}.
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DR EMBL; JPJS01001643; KFX91838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XGT0; -.
DR STRING; 1437433.A0A093XGT0; -.
DR HOGENOM; CLU_021802_11_0_1; -.
DR Proteomes; UP000029320; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05674; M20_yscS; 1.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017141; Pept_M20_carboxypep.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037217-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000029320};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037217-2}.
FT DOMAIN 294..446
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 548
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
SQ SEQUENCE 579 AA; 64081 MW; 4EAF7DEA62E4B54D CRC64;
MAKEKSALGD KNISQLSLPR FAIASALIAA VIAVSNTSLK SFLSERLDVF GSARSGKYAP
GNQWGVCQQQ PELVPKDTNI EQFIRMKVES PEYHKEIIDK LTGIIQIPSE SYDDLGPIGE
DGRWDVFYQI EDYIKVTYPA LLKSAKLDHA NTHGLILTWE GSVPASKAKP ILMLAHQDVV
PVLADTVQDW THPPYSGHYD GEIIWGRGAT DDKGYMISIL ESLNLLIEGG FKPKRTVILA
FGCDEEISGE NCGRPISDFL YKRYGNDGIY LIMDEGSMGI QSEFDQSFAM VSVSEKGYLD
VGVNVTSTGG HASTPPDHNA IGITSEIIMA IENNPFSGKV TTKNPMFGYL GCVAAHAPGP
SLPLAVRSNL EKVSRGNEKA QVELAQQLDD LRYYFRTSQS VGKINGGLKI NAIPEMVSTF
VNLRLAVETS ISQIQEHYER LIRPIAQKHG MVFEGFHSLY DSPERRKISL FGVDALEPAP
VSPVDAESFQ VLSGTIKRTL KPLRQDDELI VTPYLMPANT DTKFFWALTK NIYRFTPVNL
VHSLNRAHTT DEFIRADEFV REPLFFATLI LNADDAVGE
//
