ID   DPEP2_TALSN             Reviewed;         470 AA.
AC   B8LWT1;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Putative dipeptidase TSTA_079200;
DE            EC=3.4.13.19 {ECO:0000255|PROSITE-ProRule:PRU10073};
GN   ORFNames=TSTA_079200;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- FUNCTION: Hydrolyzes a wide range of dipeptides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC         Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC         ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10073};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10073};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}.
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DR   EMBL; EQ962652; EED24564.1; -; Genomic_DNA.
DR   RefSeq; XP_002341951.1; XM_002341910.1.
DR   AlphaFoldDB; B8LWT1; -.
DR   SMR; B8LWT1; -.
DR   STRING; 441959.B8LWT1; -.
DR   EnsemblFungi; EED24564; EED24564; TSTA_079200.
DR   GeneID; 8105978; -.
DR   VEuPathDB; FungiDB:TSTA_079200; -.
DR   eggNOG; KOG4127; Eukaryota.
DR   HOGENOM; CLU_031404_4_0_1; -.
DR   InParanoid; B8LWT1; -.
DR   OMA; TWSGRKW; -.
DR   OrthoDB; 1272387at2759; -.
DR   PhylomeDB; B8LWT1; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01301; rDP_like; 1.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008257; Pept_M19.
DR   PANTHER; PTHR10443; PTHR10443; 1.
DR   Pfam; PF01244; Peptidase_M19; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE   3: Inferred from homology;
KW   Dipeptidase; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..470
FT                   /note="Putative dipeptidase TSTA_079200"
FT                   /id="PRO_0000411219"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         371
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        143..237
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
SQ   SEQUENCE   470 AA;  52221 MW;  EA8D2B1EAA5F4B18 CRC64;
     MATLNTRGND IALNILSSTT ESSQAVVLSR ARGSPNSQRA WLFGLGTLGI ILASVLLNPF
     TSTQESPLNI DPTDYAARTK HILSTTPLID GHNDLPYLIR TELKHQIYND RFTFNTGLLS
     NTDRKKLRDG MVGGQFWSAY IHCPKDSETN KDVPLDEATW TLRDTLEQID ITKRFVDEFP
     DLFQFCSNSS CAREAFANGK IGSFIGIEGA HQIGNSLASL RQLYDLGARY ITTTHNCDNV
     FGTAASTVSA GGEDKGLTLF GEEYVAEMNR LGMMLDLSHV SHETMRDTLR LSEAPVIFSH
     TGAYALSKTL RFAPDDVLKA TAEKGGIIMI TFINRFLRPD DPDAATIHDV VDHIWHVAQV
     AGWDHVGVGS DFDGTPVTPR GLEDVSKYPR LVELLMERGA TDDQIRKFAG DNILRVWSEV
     EKAAERIQVE GRKPNEAIWE GRTWVRSEMS PPIMFRDSIG RRIPSYLGEP