ID A0A0F0KDR8_9MICO Unreviewed; 683 AA.
AC A0A0F0KDR8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Peptidyl-dipeptidase dcp {ECO:0000313|EMBL:KJL17416.1};
DE EC=3.4.15.5 {ECO:0000313|EMBL:KJL17416.1};
GN Name=dcp {ECO:0000313|EMBL:KJL17416.1};
GN ORFNames=RL72_03662 {ECO:0000313|EMBL:KJL17416.1};
OS Microbacterium azadirachtae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL17416.1, ECO:0000313|Proteomes:UP000033448};
RN [1] {ECO:0000313|EMBL:KJL17416.1, ECO:0000313|Proteomes:UP000033448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL17416.1,
RC ECO:0000313|Proteomes:UP000033448};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL17416.1}.
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DR EMBL; JYIT01000086; KJL17416.1; -; Genomic_DNA.
DR RefSeq; WP_045252298.1; NZ_JYIT01000086.1.
DR AlphaFoldDB; A0A0F0KDR8; -.
DR PATRIC; fig|582680.7.peg.3719; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000033448; 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; 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:KJL17416.1};
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:UP000033448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 234..680
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 683 AA; 75707 MW; C0A1FFCD08E2646E CRC64;
MTVETNPLLT PSPLPYAVPD YGRIRAEHYL PAFRQGFDEQ LAEIRRITMA RSMPTFENTM
EALERSGELL DRVAHAFYTV SSADATAEIQ AIDEELAPLM AAHHDAILLN AALYWRISQL
HAQLGVLPLE PEQRRLVERW HREMTLAGAA LDDEAKVRLT DLNQRLSSLS ATFEKNLLAD
TNELAVVFED PAELDGLSAG ELSAAARAAA ERGLDGGYLI ALPLFTGHPA LAVLTNRESR
RRIMEASRSR GSHGGEHDNR AVLSEIVALR AERAALLGYP THAAAVTADE TAGTPEAVER
MLRDLAAPAA RNAETERAAL QQLIDETEDE PFPLEAHDWA YYTEKLRTAR YDIDTAALRA
WFEAERVLQD GVFAAAGRLY GLSFQERPDL PVYHPGARTF EVFQEDGSPL GLYVLDLYTR
DSKRGGAWMN EIVSQSALRG TKPVVANNLN VARPADGEPT LLTLDEVNTL FHEFGHALHG
LFSDVTYPHF SGTEVFRDFV EFPSQVNEMW MLWPDIVGAY ARHHATGEPL PSDVIARLQA
TETFNQGFET SEYLAAAWLD QALHALRAGM RIDDVAAFEA NALVDIGLAD PAVPTRYSSA
YFAHIFAGGY SAGYYSYIWS EVLDADTVEW FRENGGLTRA NGERFRRRLL AVGGSQDPLE
AYRGFRGRDA EIAPLLKRRG LDV
//