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Database: UniProt
Entry: A0A3N6GJ71_9ACTN
LinkDB: A0A3N6GJ71_9ACTN
Original site: A0A3N6GJ71_9ACTN 
ID   A0A3N6GJ71_9ACTN        Unreviewed;       278 AA.
AC   A0A3N6GJ71;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=D-aminopeptidase {ECO:0000313|EMBL:RPK84034.1};
DE            EC=3.4.11.- {ECO:0000313|EMBL:RPK84034.1};
GN   Name=dppA3 {ECO:0000313|EMBL:RPK84034.1};
GN   ORFNames=EES45_05210 {ECO:0000313|EMBL:RPK84034.1};
OS   Streptomyces sp. ADI97-07.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1522762 {ECO:0000313|EMBL:RPK84034.1, ECO:0000313|Proteomes:UP000281409};
RN   [1] {ECO:0000313|EMBL:RPK84034.1, ECO:0000313|Proteomes:UP000281409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ADI97-07 {ECO:0000313|EMBL:RPK84034.1,
RC   ECO:0000313|Proteomes:UP000281409};
RA   Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA   Busche T., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT   secondary metabolite biosynthesis gene clusters and some of their
RT   products.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RPK84034.1}.
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DR   EMBL; RPGY01000023; RPK84034.1; -; Genomic_DNA.
DR   RefSeq; WP_056792227.1; NZ_ML123098.1.
DR   AlphaFoldDB; A0A3N6GJ71; -.
DR   Proteomes; UP000281409; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08663; DAP_dppA_1; 1.
DR   Gene3D; 3.30.1360.130; Dipeptide transport protein; 1.
DR   Gene3D; 3.40.50.10780; Dipeptide transport protein; 1.
DR   InterPro; IPR027476; DppA_N.
DR   InterPro; IPR007035; Peptidase_M55.
DR   InterPro; IPR036177; Peptidase_M55_sf.
DR   Pfam; PF04951; Peptidase_M55; 1.
DR   PIRSF; PIRSF015853; Pep_DppA; 1.
DR   SUPFAM; SSF63992; Dipeptide transport protein; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:RPK84034.1};
KW   Hydrolase {ECO:0000313|EMBL:RPK84034.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015853-2};
KW   Protease {ECO:0000313|EMBL:RPK84034.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281409};
KW   Zinc {ECO:0000256|PIRSR:PIRSR015853-2}.
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-1"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
SQ   SEQUENCE   278 AA;  29494 MW;  7DA480B7EA81E6F0 CRC64;
     MKILVSADME GATGVTWPAD VLPGTPQWER CRAMFTSDVN AAALGFYDGG ADEVLVNEAH
     WSMRNLLLEQ LDDRVQMLTG RHKSLSMVEG IQHGDVDAVA FIGYHTGAGA EGVLAHTYLA
     NSITGVWLNG VRASEGLLNA HVAAEYGVPV ILVTGDDLTC KDAELYAPAA RMVAVKDHVS
     RYAAVCRTPA RTAADIRAAA SEATALAVRH APVTTGDGYT VQLEFDAEHL AAAATVVPGV
     ARDGERRVAY TSGTMYEGIR TFKAVTTIVS SAVEEQYG
//
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