ID   A0A285KEM6_9ACTN        Unreviewed;       422 AA.
AC   A0A285KEM6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:SNY71084.1};
GN   ORFNames=SAMN05421748_13918 {ECO:0000313|EMBL:SNY71084.1};
OS   Actinoplanes atraurantiacus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1036182 {ECO:0000313|EMBL:SNY71084.1, ECO:0000313|Proteomes:UP000219612};
RN   [1] {ECO:0000313|EMBL:SNY71084.1, ECO:0000313|Proteomes:UP000219612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6857 {ECO:0000313|EMBL:SNY71084.1,
RC   ECO:0000313|Proteomes:UP000219612};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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}.
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DR   EMBL; OBDY01000039; SNY71084.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285KEM6; -.
DR   OrthoDB; 5240362at2; -.
DR   Proteomes; UP000219612; 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:SNY71084.1};
KW   Hydrolase {ECO:0000313|EMBL:SNY71084.1};
KW   Protease {ECO:0000313|EMBL:SNY71084.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219612};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..422
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013148685"
FT   DOMAIN          152..174
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
FT   DOMAIN          296..306
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   422 AA;  46175 MW;  A6F82AD4A261E5C7 CRC64;
     MRRRFGFLTA LTLLGSAFLV AGPVSAAPSG TEIPGQFEVY DVRTAAQRNA IARSGAAIDA
     IQHGVAEITA TGREVRDLKR QGFTVQPVLT TLDFPPSDAP YHNYSEMIAD VNQVVAAYPA
     IASKRVIGKS YENRDIVAVK ISDNVGTDEA EPEVLYDANH HAREHLTVEM AIYLLKLYTS
     SYASDTRVRT IVNSREIWIV PSVNPDGAEY DIATGSYRSW RKNRQPNSGS SAVGTDPNRN
     YGYKWGCCGG SSGTPSSLTY RGPSAFSTPE TRAIRDFVNS RVVGGRQQIG AAMDFHTYSE
     LVLWPFGHTT ANTTTGMTAD DYNTFSTFGR QMAATNRYTP EQSSDLYVTD GDLLDWLWGT
     HKIFAYTFEM YPTSSSAGGF YPPASVITRE TTRNKEAALL LAEVADCPYK VIGRQSTYCA
     AA
//