ID   A0A1G9DE93_9ACTN        Unreviewed;       854 AA.
AC   A0A1G9DE93;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:SDK62157.1};
GN   ORFNames=SAMN05421869_117106 {ECO:0000313|EMBL:SDK62157.1};
OS   Nonomuraea jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=633440 {ECO:0000313|EMBL:SDK62157.1, ECO:0000313|Proteomes:UP000199202};
RN   [1] {ECO:0000313|EMBL:SDK62157.1, ECO:0000313|Proteomes:UP000199202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6533 {ECO:0000313|EMBL:SDK62157.1,
RC   ECO:0000313|Proteomes:UP000199202};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNDJ01000017; SDK62157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9DE93; -.
DR   STRING; 633440.SAMN05421869_117106; -.
DR   Proteomes; UP000199202; 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   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   Carboxypeptidase {ECO:0000313|EMBL:SDK62157.1};
KW   Hydrolase {ECO:0000313|EMBL:SDK62157.1};
KW   Protease {ECO:0000313|EMBL:SDK62157.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199202};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..854
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011472591"
FT   DOMAIN          102..352
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
FT   REGION          27..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   854 AA;  90661 MW;  BDDD2DE4F11B1A55 CRC64;
     MRLPIALLGV AVSAALLVIP QHAVADPVAP PASPTRDFGN GPERNEVAAG VSEQAQTLRA
     VTPGEQAVYG HSRDRGYPRQ TRLPVPAENP ADAAIKLGLT PYHGIAPKLN ELQKRSNRVS
     AEIIGSSAGG HDLYLVTLTA PESAHEAREQ AKIRERIEND PAGAARDRKL AKQYKAPVFF
     NDNIHGNEWE GTDGALRVIE ELATSRDPKI IDLLARTRLY FNVTANPDGR AGNTRQNGNG
     FDMNRDFITA SQPEVRAMRQ VMIDTQPVAM VDLHGYVNGT LIEPTTPPHG ANYEYDLFIQ
     NTYANGLGME AAVNALGYTF EKDGVHPAQI PFRDDAEGWD DWPPIFTPQY APFHGAVASH
     TVEIPLRVNN ADYNQLPVEE LRRRSAINTD VAAAAIRATY SFVQAKHDKL IADQIEVFRR
     GSAGEPSKEV PLGIVPGFGP EDVYNTTYPR AYVITGERSA TAAARLVDHL IANDVRVERA
     RKSFRVSGTT YPAGSYIVDM HQPKRGLANV MLEAGADISD KVDAMYDISG WSHSLLWGAT
     VDSVTSAPRV TAEPVTAAAP TGSMPRTRGP LALKVTDGKE VQALNDLLGQ GVEVTWANGT
     AIVPASAWRA AETVSGRYGV AFTPAGQGSG VPLAQVRVAA AASADELFTL RELGFAVTPV
     STATLNAGFD WSGTDVLFVS SGLSYTALNP AARTALDAFL TTGGVITRGG TGATFNAAAG
     LLTVTAVAGR GDANGVVRVT STGGPVGAGS PDYSFVYSPR WFTGLGAEVT VEQSYATDGP
     LVSGHWRPEA NGTGGQDSAR GQAAVVSGRD ERGAAVVLFG TEPMFRNHPK GLFPQVARAL
     YWSASVTGAS VTTP
//