ID   A0A0P1H1J8_9RHOB        Unreviewed;       671 AA.
AC   A0A0P1H1J8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Peptidyl-dipeptidase dcp {ECO:0000313|EMBL:CUH88813.1};
DE            EC=3.4.15.5 {ECO:0000313|EMBL:CUH88813.1};
GN   Name=dcp {ECO:0000313|EMBL:CUH88813.1};
GN   ORFNames=PH5382_02756 {ECO:0000313|EMBL:CUH88813.1};
OS   Phaeobacter sp. CECT 5382.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH88813.1, ECO:0000313|Proteomes:UP000050782};
RN   [1] {ECO:0000313|EMBL:CUH88813.1, ECO:0000313|Proteomes:UP000050782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH88813.1,
RC   ECO:0000313|Proteomes:UP000050782};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CYSG01000012; CUH88813.1; -; Genomic_DNA.
DR   RefSeq; WP_058334938.1; NZ_CYSG01000012.1.
DR   AlphaFoldDB; A0A0P1H1J8; -.
DR   STRING; 1712645.PH5382_02756; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000050782; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.40; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:CUH88813.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050782};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          226..667
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   671 AA;  73686 MW;  B666D07153F988FE CRC64;
     MTNPLLAHWD TAFEIAPFDQ ISDADFAPAL DVALSQHKAE IAQIATNPEP ATFANVIEAL
     ETPSRGLEQV LSVFFTVAGA DSNPQREELQ REFSPKLAAH FSEITANKAL FARVNAVWEQ
     RDQLDLTPEK SRVLMLTHRG FVRGGAALEG AQDQRMQAIK GRLATLGTEF TQNLLADERD
     WFMELSEADL EGLPDFVISA ARAAGAEKGA AGPVVTLSRS IITPFLQFSP RRDLRQKAFV
     AWAARGANGG ATDNRAIAAE ILALRAERAT LLGYDSFADY KLETEMAKTP AAVRALLMDV
     WKPAKAQAEA DAEVLARMMH EDGVNGDLEP WDWRYYAAKR RKAEHDLDEA ELKPYLQLDR
     MIEASFACAN RLFGLEFAPL DVPLYHPDCR AWEVTRDGKH LAVFIGDYFA RGSKRSGAWC
     SAMRSQAKFP KEQTPIVINV CNFAKGDPAL LSWDDARTLF HEFGHALHQM LSNVSYESIS
     GTSVARDFVE LPSQLYEHWL EVPEVLGEFA THAQTGAAMP PELLKKVLGA ATFDMGFQTV
     EYVASALVDL AFHEGAAPQD VMAKQAEVLQ DIGMPHAIAM RHASPQFAHV FSGDGYSSGY
     YSYMWSEVMD ADAFAAFEEA GGAFDPERAA ALEKYILSTG GSVDPAELYT AFRGRLPGVE
     ALLKGRGLAA K
//