P20D1_UNCRE
ID P20D1_UNCRE Reviewed; 445 AA.
AC C4JXT1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Probable carboxypeptidase UREG_07869;
DE EC=3.4.17.-;
DE AltName: Full=Peptidase M20 domain-containing protein UREG_07869;
DE Flags: Precursor;
GN ORFNames=UREG_07869;
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476619; EEP83004.1; -; Genomic_DNA.
DR RefSeq; XP_002583096.1; XM_002583050.1.
DR AlphaFoldDB; C4JXT1; -.
DR SMR; C4JXT1; -.
DR STRING; 33188.XP_002583096.1; -.
DR EnsemblFungi; EEP83004; EEP83004; UREG_07869.
DR GeneID; 8440320; -.
DR KEGG; ure:UREG_07869; -.
DR VEuPathDB; FungiDB:UREG_07869; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_3_0_1; -.
DR InParanoid; C4JXT1; -.
DR OrthoDB; 1432382at2759; -.
DR Proteomes; UP000002058; 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; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Protease; Reference proteome; Secreted; Signal;
KW Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..445
FT /note="Probable carboxypeptidase UREG_07869"
FT /id="PRO_0000411242"
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"
SQ SEQUENCE 445 AA; 48226 MW; 9D3E6A37EC01E79A CRC64;
MKSLILTTLA LLPLVSCKPW VQLSHQTPIS ADRNLIPGAA EKSQLDKIIA DSELLSLHRS
LTEIESISSR EGDVGDFLVD YLQKHGFTVE KQHVSSDGNE ADKMKPSSFN VYAYPRSSPA
PEIILTSHID TVPPFIPYSL SLPKSSSTGS IDRRAIHISG RGTVDDKGSV ACQIIAILSH
LKSHPDARLG LLFVVGEETG GQGMHHFSRS PLNTSPPTFH TVIFGEPTEN KLVSGHKGML
QFTVSVHGKP AHSGYPWLGR SAVSEILPIL SKIDQLGDIP ESEGGLPSSE KYGKTTLNIG
FMEGGVATNV VPARAFARVA VRLAGGTVEQ AKERITAAVR SASREYRADV RLWFFSGGGY
PPIDLDTDVE GFDILAVNYG TDVPNLMIHD HDQPEDKKVK RYLYGPGSIF SAHGENEGLS
VGDMEDAVEG YGRLIRAAVE RGQRK
