ID G2Z3N3_FLABF Unreviewed; 489 AA.
AC G2Z3N3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Xaa-His dipeptidase {ECO:0000313|EMBL:CCB70487.1};
DE EC=3.4.13.3 {ECO:0000313|EMBL:CCB70487.1};
GN Name=pepD {ECO:0000313|EMBL:CCB70487.1};
GN OrderedLocusNames=FBFL15_2482 {ECO:0000313|EMBL:CCB70487.1};
OS Flavobacterium branchiophilum (strain FL-15).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1034807 {ECO:0000313|EMBL:CCB70487.1, ECO:0000313|Proteomes:UP000009186};
RN [1] {ECO:0000313|EMBL:CCB70487.1, ECO:0000313|Proteomes:UP000009186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FL-15 {ECO:0000313|EMBL:CCB70487.1,
RC ECO:0000313|Proteomes:UP000009186};
RX PubMed=21926215; DOI=10.1128/AEM.05625-11;
RG 1:IP;
RG Microbial Evolutionary Genomics,F-75015 Paris;
RG France 2:CNRS;
RG URA2171;
RG F-75015 Paris,France 3:Unite de Virologie et Immunologie Mol.;
RG INRA,78352 Jouy en Josas Cedex;
RG France. 4:Unite de Mathemathique;
RG Informatique et Genome,INRA;
RG 78352 Jouy en Josas Cedex;
RG France. 5:CEA/Genoscope;
RG Evry;
RG France;
RA Touchon M., Barbier P., Bernardet J.F., Loux V., Vacherie B., Barbe V.,
RA Rocha E.P., Duchaud E.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT branchiophilum.";
RL Appl. Environ. Microbiol. 77:7656-7662(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ859183; CCB70487.1; -; Genomic_DNA.
DR RefSeq; WP_014084946.1; NC_016001.1.
DR AlphaFoldDB; G2Z3N3; -.
DR STRING; 1034807.FBFL15_2482; -.
DR KEGG; fbr:FBFL15_2482; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_028526_0_0_10; -.
DR Proteomes; UP000009186; Chromosome.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd03890; M20_pepD; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR001160; Peptidase_M20C.
DR NCBIfam; TIGR01893; aa-his-dipept; 1.
DR PANTHER; PTHR43501; CYTOSOL NON-SPECIFIC DIPEPTIDASE; 1.
DR PANTHER; PTHR43501:SF1; CYTOSOL NON-SPECIFIC DIPEPTIDASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF016599; Xaa-His_dipept; 1.
DR PRINTS; PR00934; XHISDIPTASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Dipeptidase {ECO:0000313|EMBL:CCB70487.1};
KW Hydrolase {ECO:0000313|EMBL:CCB70487.1};
KW Protease {ECO:0000313|EMBL:CCB70487.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009186}.
FT DOMAIN 211..278
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 489 AA; 53548 MW; 39007B83F26E95FD CRC64;
MNEDVRNLEP KVLWNKFADL NAVPRPSKRE EKVIAFMKNF GLQLGLETFE DDIRNVIIRK
PATKGMENRK PIVLQGHLDM VHQKNNDTLF DFDTQGIEMF VADDWVRAKG TTLGADNGLG
VAAIMAVLES TTLAHPAIEA LFTIDEETGM TGALNLKGGV LQGEILLNLD TEEDDELDIG
CAGGIDVTAT RTYVEETVDQ ATSKGYTLIV KGLKGGHSGM DIDKGLGNAN KIMNRLLHHG
FESFGLQIAS INGGSLRNAI PRESVAHLII ASMFEDTFVF DMQSKINAIK KEFQTTEPFL
DIAITPSALP EKVMDLSVQE GLLRAIYAAH NGVYRMSADM ENLVETSNNI ARVSVENGHI
SIQNLCRSSV ESSKMDLAYA LQSAFELIGC EVTLTGSYPG WTPNVNSPIL DLLVQLYEQQ
NQQKPKVVAC HAGLECGILG THYPTMDMIS FGPTIHGAHS PDERASISSA QKFWTFLVAI
LANIPLKNE
//