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Database: UniProt
Entry: A0A0N0ATQ1_9ACTN
LinkDB: A0A0N0ATQ1_9ACTN
Original site: A0A0N0ATQ1_9ACTN 
ID   A0A0N0ATQ1_9ACTN        Unreviewed;       404 AA.
AC   A0A0N0ATQ1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:KOX24283.1};
GN   ORFNames=ADL05_00195 {ECO:0000313|EMBL:KOX24283.1};
OS   Nocardiopsis sp. NRRL B-16309.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1519494 {ECO:0000313|EMBL:KOX24283.1, ECO:0000313|Proteomes:UP000037694};
RN   [1] {ECO:0000313|Proteomes:UP000037694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16309 {ECO:0000313|Proteomes:UP000037694};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) 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:KOX24283.1}.
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DR   EMBL; LGEC01000002; KOX24283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0ATQ1; -.
DR   STRING; 1519494.ADL05_00195; -.
DR   PATRIC; fig|1519494.3.peg.41; -.
DR   Proteomes; UP000037694; 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; cd03859; M14_CPT; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR033810; Carboxypeptidase_T.
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   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KOX24283.1};
KW   Hydrolase {ECO:0000313|EMBL:KOX24283.1};
KW   Protease {ECO:0000313|EMBL:KOX24283.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037694}.
FT   DOMAIN          136..158
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
FT   DOMAIN          280..290
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   404 AA;  44479 MW;  E55AE1C3EACDF9D7 CRC64;
     MTLGLIGPTG AGADSDPRLF EVHGPNTPVE RTAVAATGAA VEEVRDGSVV VTATPSEAET
     LADLGHELTE ITPSPVRPLA PDEGYTTFGE LRETIDEVVA DHPGIVTQSV VGQSYEGRDL
     VAVKISDNAA VDEDEPEVLF THSQHAREHL TVEMAVYLMR LLTDEYGSDA RITDLVDSRE
     IWILPNVNPD GSEYDMAGSD WRSWRKNRQP NQGSSAVGTD MNRNWDHLWG CCNGSSGSPS
     SSTYRGAAPE SAPEVSAVAD FVRGRVVGGE QQITAAIDFH TYSELILWPY GYTYDEVGPG
     MTREEYDTHA ALGTHMADAN GYTPQQSSDL YITDGTINDW LWGDQRIVNF TYEMYPRSWW
     GGGFYPPSYV IDRETSRNRE AVLRLLDYAD CPYRIIGEEE AYCS
//
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