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Database: UniProt
Entry: I0GUR3_SELRL
LinkDB: I0GUR3_SELRL
Original site: I0GUR3_SELRL 
ID   I0GUR3_SELRL            Unreviewed;       377 AA.
AC   I0GUR3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Putative carboxypeptidase {ECO:0000313|EMBL:BAL84500.1};
GN   OrderedLocusNames=SELR_27920 {ECO:0000313|EMBL:BAL84500.1};
OS   Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL84500.1, ECO:0000313|Proteomes:UP000007887};
RN   [1] {ECO:0000313|EMBL:BAL84500.1, ECO:0000313|Proteomes:UP000007887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA   Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA   Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT   TAM6421.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AP012292; BAL84500.1; -; Genomic_DNA.
DR   RefSeq; WP_014425917.1; NC_017068.1.
DR   AlphaFoldDB; I0GUR3; -.
DR   KEGG; sri:SELR_27920; -.
DR   PATRIC; fig|927704.6.peg.2881; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_7_0_9; -.
DR   OMA; HADTVWP; -.
DR   OrthoDB; 9783294at2; -.
DR   Proteomes; UP000007887; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd03885; M20_CPDG2; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR017150; Pept_M20_glutamate_carboxypep.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF9; BLL0789 PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037238; Carboxypeptidase_G2; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:BAL84500.1};
KW   Hydrolase {ECO:0000313|EMBL:BAL84500.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000313|EMBL:BAL84500.1}.
FT   DOMAIN          176..276
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   377 AA;  40538 MW;  A264C00CF0ADB0DA CRC64;
     MELEKQRYLD ELAKLVNIDS VSSEPEGAGK IAAFMKEKYE SLGWLAEEVR LSPTIAPCLR
     IVNREADHYD VLVLAHMDTV FPLGTAAKRP FTIDGNRAYG PGVIDCKAGM LSGFYALANL
     QARGVLQEAS ICVFLNSDHE GISSRYSAVY STELARKSRY VLVLEAGRAN GNLVHKRKGI
     ARYHINIKGV AAHAGVDYQA GRNAVEELAH WIIALQSATD FTKETTVNVG KVWGGTGISA
     VPGEAGAEVD VRYYDKAEIE RVSGVMKALH NQPHVEGTAA AVEGGITRPP MLPTEKTMEL
     CRRIDEIGQE IGVDFGWTAS GGGSDGSFAA AGGTPTIDGL GPVGGGAHSE GEYLEIDSII
     PRYELLCRII QHIIGSR
//
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