ID A0A372M4I4_9ACTN Unreviewed; 305 AA.
AC A0A372M4I4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:RFU85844.1};
GN ORFNames=DY218_15620 {ECO:0000313|EMBL:RFU85844.1};
OS Streptomyces triticagri.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2293568 {ECO:0000313|EMBL:RFU85844.1, ECO:0000313|Proteomes:UP000263094};
RN [1] {ECO:0000313|EMBL:RFU85844.1, ECO:0000313|Proteomes:UP000263094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY421 {ECO:0000313|EMBL:RFU85844.1,
RC ECO:0000313|Proteomes:UP000263094};
RA Han C.;
RT "Isolation, diversity and antifungal activity of Actinobacteria from
RT wheat.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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:RFU85844.1}.
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DR EMBL; QUAK01000083; RFU85844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372M4I4; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000263094; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07025; Peptidase_S66; 1.
DR Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30237:SF2; MUREIN TETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:RFU85844.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..133
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 176..288
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 305 AA; 32539 MW; 0433928EF62F4C64 CRC64;
MRRAPRLAPG ARVAVVAPSG PVPEDLLQAG LDILRGWGLE VTVAPHVLAG HREFGYLAGS
DADRAADLQN AWCDPAVDAV FCARGGYGAQ RMVDLVDWAA VRAAGPKVFL GYSDITALHE
AFAVRAGVAT LHGPMVAVRD FIKTPATQEH LRATLFEPES VLTHEAGRAL IPGRARGVVL
GGCLSLLSSD LGTPHARPSA GGGLLCIEDV DEEDYRLDRC LTQLLRSGWL EGVRGVLLGS
WVDCGPYRDV RAVLRDRLSD LGVPVAEEFG FGHADAPRTL PFGLPATLTT DANRSTLRYE
VPALR
//
