P20D1_ASPFU
ID P20D1_ASPFU Reviewed; 440 AA.
AC Q4WNC9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable carboxypeptidase AFUA_6G06800;
DE EC=3.4.17.-;
DE AltName: Full=Peptidase M20 domain-containing protein AFUA_6G06800;
DE Flags: Precursor;
GN ORFNames=AFUA_6G06800;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000006; EAL88535.1; -; Genomic_DNA.
DR RefSeq; XP_750573.1; XM_745480.1.
DR AlphaFoldDB; Q4WNC9; -.
DR SMR; Q4WNC9; -.
DR STRING; 746128.CADAFUBP00007081; -.
DR EnsemblFungi; EAL88535; EAL88535; AFUA_6G06800.
DR GeneID; 3508779; -.
DR KEGG; afm:AFUA_6G06800; -.
DR VEuPathDB; FungiDB:Afu6g06800; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_3_0_1; -.
DR InParanoid; Q4WNC9; -.
DR OMA; VSGHKGM; -.
DR OrthoDB; 1432382at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..440
FT /note="Probable carboxypeptidase AFUA_6G06800"
FT /id="PRO_0000411230"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 440 AA; 46378 MW; 022BC85527D9338C CRC64;
MKPLTSLLLS AALSAAAPHP ASPQAPLADI PSIVGETRTE FSQNSLDDVV NASPLLSFHR
DLVSIESISG NEGAAGAFVA DFLASHNFTV IKQPVTTESD ARFNIFAIPE SQYHSLDESH
SSHSPQILLT SHIDTVPPFI PYSLHRDAND TDDRNILIAG RGTVDAKGSV AAQIFAALDI
LAAQPSAPLG LLFVVGEETG GDGMKAFSQS THLNPSPSRF HTVIFGEPTE LALVAGHKGM
LGFEVAAHGH AAHSGYPWLG ESAISAILPA LARVDQLGDI PVEEGGLPAS DKYGRTTVNI
GRMEGGVATN VVPSKARAGV AVRLAAGTHD EAREVVLKAV RDVTGGDDRV VVNFSLEGYG
PQDLDTDVPG FNITTVNYGT DVPNLQLHPR PDGKVRRYLY GPGTIHVAHG DNEALTVAQL
EEAVRGYKKL IQAALDRSAS
