ID A0A0M2S0V5_9ACTN Unreviewed; 437 AA.
AC A0A0M2S0V5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:KKK07107.1};
GN ORFNames=LQ51_04150 {ECO:0000313|EMBL:KKK07107.1};
OS Micromonospora sp. HK10.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKK07107.1, ECO:0000313|Proteomes:UP000034330};
RN [1] {ECO:0000313|EMBL:KKK07107.1, ECO:0000313|Proteomes:UP000034330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK10 {ECO:0000313|EMBL:KKK07107.1,
RC ECO:0000313|Proteomes:UP000034330};
RA Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT National park, Assam, India.";
RL Submitted (NOV-2014) 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:KKK07107.1}.
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DR EMBL; JTGL01000030; KKK07107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2S0V5; -.
DR STRING; 1538294.LQ51_04150; -.
DR PATRIC; fig|1538294.3.peg.4925; -.
DR HOGENOM; CLU_019326_3_0_11; -.
DR OrthoDB; 5240362at2; -.
DR Proteomes; UP000034330; 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:KKK07107.1};
KW Hydrolase {ECO:0000313|EMBL:KKK07107.1};
KW Protease {ECO:0000313|EMBL:KKK07107.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..437
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039560747"
FT DOMAIN 170..192
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 314..324
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 437 AA; 47188 MW; 46E09C2CC8BAD88F CRC64;
MALRTSPLRR RLALAAAVGL TLVTALGTPA AARPAPDPSD APAAASYRVL GPRTVADRSA
VARTGAAIDY SEHGVLHVTA TSAEAAAITR LGFRLEREAT PAAAAGAVAY AFPSADSNYH
DYAELTAVVN KVVADHPAIA RKLSIGTSYQ GRDLMAVKIS DNVGTDENEP EILFNAQQHA
REHLTVEMAI YLLNLFTDSY GTDSRITNIV NSREIWIVPT VNPDGSEYDI ATGSYRSWRK
NRQPNSGSTA VGTDLNRNWG YQWGCCGGSS SSKSSETYRG PSAFSAPETA ALRNFVNSRV
VGGVQQLKAN IDFHTYSQLV LWPYGYTYSN TATGMTADQY NTFATIGRQL ASSNGYTPEQ
SSDLYIADGT SIDWMWGTHK IWAYTFEMYP GSSSGGGFYP PDEVIPAQTS RNKEAVLLLS
EYADCPYRAI GKQSTYC
//
