P20D1_ASPTN
ID P20D1_ASPTN Reviewed; 433 AA.
AC Q0CTS9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Probable carboxypeptidase ATEG_02905;
DE EC=3.4.17.-;
DE AltName: Full=Peptidase M20 domain-containing protein ATEG_02905;
DE Flags: Precursor;
GN ORFNames=ATEG_02905;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CH476597; EAU36179.1; -; Genomic_DNA.
DR RefSeq; XP_001212083.1; XM_001212083.1.
DR AlphaFoldDB; Q0CTS9; -.
DR SMR; Q0CTS9; -.
DR STRING; 341663.Q0CTS9; -.
DR EnsemblFungi; EAU36179; EAU36179; ATEG_02905.
DR GeneID; 4317488; -.
DR VEuPathDB; FungiDB:ATEG_02905; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_3_0_1; -.
DR OMA; VSGHKGM; -.
DR OrthoDB; 1432382at2759; -.
DR Proteomes; UP000007963; 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 InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Metal-binding; Protease; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..433
FT /note="Probable carboxypeptidase ATEG_02905"
FT /id="PRO_0000411232"
FT REGION 20..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 433 AA; 45628 MW; 79468AC9DCE3B502 CRC64;
MKSAISLLLA SAATYVGASP HPEPPQLVLS PSTSTGVHGD EATSAIASSA ADDVISDSPF
LSFHRDLVQI SSISGHERKA GDFVAEFLQA HNFTVVKQPV PSKDGRQPDE DRFNVFAYPS
GASAAPKILL TSHIDTVPPF IPYSAARVDN DIRISGRGSV DAKGSVAAQV FAALDILERD
PSAPLGLLFV VDEEVGGTGM KVFSDSSLNP SPSPFRAVIF GEPTDLALVS GHKGMLGFEL
VATGQAAHSG YPWLGHSAVS ALLPALLRVD RLGDIPAQEG GLPSSPKYGR TTVNIGRMEG
GVAANVVPAS AHANVAVRLA AGTPDEARDI VRRAVRDATG GDENVYPDFS EWSEGYPPQD
LDTDVDGFEV TTVNYGTDVP NLRIHERADG APVRRYLYGP GSIHVAHGDH EAITVAQLEE
ALQGYRKLIE AAM