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Database: UniProt
Entry: A0A0H5CTP7_9PSEU
LinkDB: A0A0H5CTP7_9PSEU
Original site: A0A0H5CTP7_9PSEU 
ID   A0A0H5CTP7_9PSEU        Unreviewed;       556 AA.
AC   A0A0H5CTP7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Carboxypeptidase T {ECO:0000313|EMBL:CRK61383.1};
DE            EC=3.4.17.18 {ECO:0000313|EMBL:CRK61383.1};
OS   Alloactinosynnema sp. L-07.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae.
OX   NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK61383.1, ECO:0000313|Proteomes:UP000076116};
RN   [1] {ECO:0000313|Proteomes:UP000076116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-07 {ECO:0000313|Proteomes:UP000076116};
RA   Ramaraj T.;
RL   Submitted (MAY-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}.
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DR   EMBL; LN850107; CRK61383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H5CTP7; -.
DR   STRING; 1653480.gene:80950281; -.
DR   KEGG; alo:CRK61383; -.
DR   Proteomes; UP000076116; Chromosome i.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03859; M14_CPT; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR033810; Carboxypeptidase_T.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002884; P_dom.
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; PF01483; P_proprotein; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:CRK61383.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CRK61383.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076116};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..556
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005217073"
FT   DOMAIN          436..556
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
SQ   SEQUENCE   556 AA;  59966 MW;  53BEA7A6262D11B6 CRC64;
     MNRKRLSVTV GALAAFAMVI SMNGGSAAGD KAAQTARASA EYHVTGVKTV QQRSAIAATG
     AAINGTEDSR LLITATPGEV AKIRAQGFTV EAEAAPAVTQ GTQGANGVND FPSADAGYHN
     YAEMNSVLNT AVANYPSIIS KQVIGKSYEN RDILAFKISD NVATDENEPE VLFTHHQHAR
     EHLTVEMALY LVKTFTQGYA TDARIKGLVD SREIWILPDV NPDGGEFDIA TGSYRSWRKN
     RQPNAGSSNV GTDMNRNWDY KWGCCNGSSG STGSETYRGT APESAKEVKV LSDFVRSRVV
     GGTQQISVAI DFHTYSELVL WPFGWTYNDT APGLNAEEHN IFSTMGRAMA QTNGYTPEQA
     SDLYITDGTI DDYLWGVHRI WGYTFEMFPS GAGGGGFYPG DEIIDRETAR NKAAVLYLLD
     YADCPKRSIG LTCDGTPPPP GKVFENANNV NIPDSPAAAV FSDVVVSGVT GNAPATLKVD
     VDIKHTWRGD LVIDLVAPDG SLYRLKNSSG NDSADNVIAT YTVNASTEVA NGTWRLKVQD
     VARYDTGYID NFKLTF
//
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