ID   A0A367EUZ2_9ACTN        Unreviewed;       445 AA.
AC   A0A367EUZ2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=DUF2817 domain-containing protein {ECO:0000313|EMBL:RCG21482.1};
GN   ORFNames=DTL70_18855 {ECO:0000313|EMBL:RCG21482.1};
OS   Streptomyces diacarni.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2800381 {ECO:0000313|EMBL:RCG21482.1, ECO:0000313|Proteomes:UP000252914};
RN   [1] {ECO:0000313|EMBL:RCG21482.1, ECO:0000313|Proteomes:UP000252914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW51701 {ECO:0000313|EMBL:RCG21482.1,
RC   ECO:0000313|Proteomes:UP000252914};
RA   Li L.;
RT   "Streptomyces reniochalinae sp. nov. and Streptomyces diacarnus sp. nov.
RT   from marine sponges.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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:RCG21482.1}.
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DR   EMBL; QOIN01000046; RCG21482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367EUZ2; -.
DR   OrthoDB; 9758209at2; -.
DR   Proteomes; UP000252914; Unassembled WGS sequence.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06242; M14-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000252914};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..445
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016991714"
FT   DOMAIN          53..280
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   445 AA;  48123 MW;  37CB99C063E695C9 CRC64;
     MVIRARLGRS RWKTAALTSA ALLVPLLATT AQAAPRDGSA ALRTGFERTH GQHWTTQSEE
     EEFLRAVDAA GRRVTLDTIG RTEQGRPLRL ARIGAPSPEG PAKVRRGNSL LLICSQHGNE
     PAGREACLST IRDLAFAEDR ATQRFLSATT VLVVPTANPD GRAADTRGNA DGVDINRDHL
     ALETAEARAM AAVLRDYRPD TVYDLHEYGA HEPYYVKDLL SLWPRNLNTA KGVHKESVTL
     SEKYARPSAE DSGHTTGIYG IWTDPQTGEP VKQVAGDGQE RILRNTVGVK GGVGLLAETR
     IEPLTGADKG DEARNNRRRV GAHLAALEGA FDFTGERRAR IEKATGAARR AGFADRGPVY
     LGGADNERPA EEQVLDDPPC GYRLTGDQFE DVEPVLDLHG VRAEPRRGGG VLVPLRQSQR
     ALVPLLLDPR AEFALTAGAP VRDCG
//