ID P20D1_ARTGP Reviewed; 461 AA.
AC E4UW91;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Probable carboxypeptidase MGYG_04702;
DE EC=3.4.17.-;
DE AltName: Full=Peptidase M20 domain-containing protein MGYG_04702;
DE Flags: Precursor;
GN ORFNames=MGYG_04702;
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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; DS989825; EFR01699.1; -; Genomic_DNA.
DR RefSeq; XP_003172110.1; XM_003172062.1.
DR AlphaFoldDB; E4UW91; -.
DR SMR; E4UW91; -.
DR STRING; 535722.E4UW91; -.
DR GeneID; 10027378; -.
DR VEuPathDB; FungiDB:MGYG_04702; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_3_0_1; -.
DR InParanoid; E4UW91; -.
DR OMA; RLHKGVM; -.
DR OrthoDB; 2875217at2759; -.
DR Proteomes; UP000002669; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05652; M20_ArgE_DapE-like_fungal; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Metal-binding; Protease; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..461
FT /note="Probable carboxypeptidase MGYG_04702"
FT /id="PRO_0000411225"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 461 AA; 49743 MW; 8513CBA7EFEF3CA7 CRC64;
MQKTYLLALV SLLASSLVEA RSTIADQTRL DVGGSDESFD GIDGIDPNNS NVLTHKLMDK
VIASSELLSL HRSLVEIKSI SDNEQAVGGF LMDYLSSKNF TVEKQYVDYD DPTGKPIRSN
RRFNIYAYPG DSASPGIILT SHIDTVPPFI PYSLSHPESD SFKRDDILIS GRGTVDDKAS
VACQIIAAME HLEKHPDIPI GLLFVVSEEV GGKGMSTFSD SRLNSGTYHT IIFGEPTERA
LVAGHKGMVS FGIRVHGKPA HSGYPWLGRS AVSEILPILA EVDRLGDIPV SQGGLPSSEK
YGRTTLNIGF MSGGVAANVV PEQAVAKVAV RLAAGDPEDA KDIIFRAIRN AATKHRKDAT
VVISNGHEQP KGDIEVIFGL EAYGVVDIDA DVDGFNVTTV NYGTDVPHWK IYGDNVKRYL
YGPGTIFVAH GKDEALTVGE LEAGLEGYKT LVAKAAERER T
//
