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Database: UniProt
Entry: R9NA85_9FIRM
LinkDB: R9NA85_9FIRM
Original site: R9NA85_9FIRM 
ID   R9NA85_9FIRM            Unreviewed;       482 AA.
AC   R9NA85;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Xaa-His dipeptidase {ECO:0000313|EMBL:EOS79861.1};
GN   ORFNames=C817_02276 {ECO:0000313|EMBL:EOS79861.1};
OS   Dorea sp. 5-2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=1235798 {ECO:0000313|EMBL:EOS79861.1, ECO:0000313|Proteomes:UP000014211};
RN   [1] {ECO:0000313|EMBL:EOS79861.1, ECO:0000313|Proteomes:UP000014211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-2 {ECO:0000313|EMBL:EOS79861.1,
RC   ECO:0000313|Proteomes:UP000014211};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Dorea bacterium 5-2.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EOS79861.1}.
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DR   EMBL; ASTD01000043; EOS79861.1; -; Genomic_DNA.
DR   RefSeq; WP_016219011.1; NZ_KE159770.1.
DR   AlphaFoldDB; R9NA85; -.
DR   STRING; 1235798.C817_02276; -.
DR   PATRIC; fig|1235798.3.peg.2418; -.
DR   eggNOG; COG2195; Bacteria.
DR   HOGENOM; CLU_028526_0_0_9; -.
DR   OrthoDB; 9773892at2; -.
DR   Proteomes; UP000014211; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000014211}.
FT   DOMAIN          207..288
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   482 AA;  53088 MW;  C36DA245B6D50DE4 CRC64;
     MAVLENVEPK KVFQFFEEIC RIPHGTFDTK RISDYCVSFA KERGLEVIQD EVNNVIIKKP
     GTAGYEDCEP VILQGHIDMV CEKTADSAHD FKTDGLELYI EDGYLKAKDT TLGGDDGIAV
     AMAMAVLDSD DIPHPPIEAL FTVDEEVGMG GADAVDLSLL RGRKLINMDS ETEGILTTGC
     AGGIRYEVSL PIRKEKVSGD KITIRVHGLL GGHSGMEIHK QRGNASKMMG RLLYRLAKEV
     PFHLVCINGG TKDNVITPDA DAEILVEPGK EQEVLAVVDE MKKIWTEEFM GEEPGLQADA
     AVSQGAGCEA MDQDSTKHVI AYLLLCPNGC QEYSRKIEGV VETSLNLGIL ETKEDCVRMI
     HQIRSSVETR KYQLQEQLEQ CVKAVGGEGT ITNEYPAWQY DPDSGLRQIM ADTYKELYGK
     EPVIAVIHAG LECGLFLGKR PDLDCVSFGP DVIDVHSVNE ALNLASTQRV WEHLKAILKN
     CR
//
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