ID C0ZSX1_RHOE4 Unreviewed; 416 AA.
AC C0ZSX1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Putative amidohydrolase {ECO:0000313|EMBL:BAH31944.1};
GN OrderedLocusNames=RER_12360 {ECO:0000313|EMBL:BAH31944.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31944.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH31944.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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DR EMBL; AP008957; BAH31944.1; -; Genomic_DNA.
DR RefSeq; WP_020906516.1; NC_012490.1.
DR AlphaFoldDB; C0ZSX1; -.
DR KEGG; rer:RER_12360; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_6_0_11; -.
DR Proteomes; UP000002204; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:BAH31944.1}.
FT DOMAIN 192..287
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 416 AA; 43202 MW; 64FC27971E789C83 CRC64;
MTSSVHETIA VDLDLIDLYK DLHGNPELGF HEHRTSSLVE GHLTALGFDT TTGVGTTGVV
GVLKNGAGPT ALLRADMDAL PVREETGLDY ASTVTTTDDQ GKTVSVSHAC GHDLHTTCLL
GAARILSQDT TTWSGTLVLV FQPAEELGAG AQAMVDDGLF EQFPKPDIVL GQHVSPLPAG
TIAGHAGPSY AGSDSLRVRL VGKGAHGSMP ENSVDPVVMA AETVLRLQTV ISREVPSTAT
AVLTVGSIHA GDAANVIPGE AELQLNIRSY DAVVRQRILD SVDRIVHGEA ATAGAPTPPT
ITETEHFPIV VNDPAALDKT LDAFAEWLGT NKILDPGAGA GSEDVGILAT SAGAPLSYWL
LGGTDPSLFT TGDMTDPALR TVPSNHSPHY APVIEPTLTI GVNALVVAAR TWLPTP
//
