ID   A0A0R0C8N3_9GAMM        Unreviewed;       723 AA.
AC   A0A0R0C8N3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Dipeptidyl carboxypeptidase II {ECO:0000313|EMBL:KRG66009.1};
GN   ORFNames=ABB26_02010 {ECO:0000313|EMBL:KRG66009.1};
OS   Stenotrophomonas humi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG66009.1, ECO:0000313|Proteomes:UP000050864};
RN   [1] {ECO:0000313|EMBL:KRG66009.1, ECO:0000313|Proteomes:UP000050864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG66009.1,
RC   ECO:0000313|Proteomes:UP000050864};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-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}.
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:KRG66009.1}.
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DR   EMBL; LDJI01000004; KRG66009.1; -; Genomic_DNA.
DR   RefSeq; WP_057631899.1; NZ_LDJI01000004.1.
DR   AlphaFoldDB; A0A0R0C8N3; -.
DR   PATRIC; fig|405444.3.peg.2811; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000050864; 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:KRG66009.1};
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   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..723
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006393681"
FT   DOMAIN          261..715
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   723 AA;  79252 MW;  FDA3052F4F61E9F0 CRC64;
     MNTRLALALA ATLGLALPAY SVTANAAATQ SAEQANPFFA ESPLPLHYPQ FDRIKDADFA
     PAFDAGMAQQ LKEVEAIANN PAAPTFENTL IALENSGAVL DRATTVFFSL IGADTNDTRK
     KLQADYSAKF AAHSDAINLN GKLFQRIEKL YNDRATLGLD AEGLRLVEKY HDNFVRSGAK
     LGDADKAKLK AMNAELANLG TKFSQNVLAE VNGSFIVVDD VKQLDGLSAE QIAAAAEAAK
     ARKLDGKYVI ALLNTTGQPS LTNLTNRELR QKIYETSVSR GSRGGEYDNT ALVSRIMTLR
     AEKAALMGFP NFAAYSLGNQ TAKTPEAVNA MLGQLAPAAV ANAKREASDL QAMIDAEQKA
     AGKPTFELQP WDWAFYSEKV RQAKYNFDES QLKPYFEMTK VLEDGVFFAA GKEFGLSFKQ
     RTDLPVYHAD VTVYDVFNED GSQLAIFIFD PYARESKRGG AWMNAYVSQS GLTGDLPVVA
     NHLNIPKPPA GKPTLLTWDE VTTTFHEFGH ALHGMFSDVK YPYFAGTAVP RDFVEFPSQV
     NEMWSDEPTI LANYAKHYQS GAAMPQALLD KVIAAAKFNQ GFATTEYLGA AMLDQNWHQI
     GVKDVPAPAD VIKFERAALE KDGIYYAPVP PRYRTTYFSH IMGGYSAGYY AYIWSEVLDA
     NTQKWFRENG GLTRANGDRF RETLLSKGGS VDAMELFRNF AGHEPQIEPL LEKRGLTTGA
     ASN
//