(data stored in ACNUC7421 zone)

SWISSPROT: C3MFU1_SINFN

ID   C3MFU1_SINFN            Unreviewed;       389 AA.
AC   C3MFU1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   SubName: Full=Metal-dependent amidase/aminoacylase/carboxypeptidase {ECO:0000313|EMBL:ACP23992.1};
GN   OrderedLocusNames=NGR_c01920 {ECO:0000313|EMBL:ACP23992.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23992.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23992.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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DR   EMBL; CP001389; ACP23992.1; -; Genomic_DNA.
DR   RefSeq; WP_012706777.1; NC_012587.1.
DR   RefSeq; YP_002824745.1; NC_012587.1.
DR   ProteinModelPortal; C3MFU1; -.
DR   STRING; 394.NGR_c01920; -.
DR   EnsemblBacteria; ACP23992; ACP23992; NGR_c01920.
DR   GeneID; 7790770; -.
DR   KEGG; rhi:NGR_c01920; -.
DR   PATRIC; fig|394.7.peg.2989; -.
DR   eggNOG; ENOG4105CH2; Bacteria.
DR   eggNOG; COG1473; LUCA.
DR   HOGENOM; HOG000241406; -.
DR   KO; K01451; -.
DR   OMA; GAAYWTR; -.
DR   OrthoDB; POG091H022P; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE   4: Predicted;
DR   PRODOM; C3MFU1.
DR   SWISS-2DPAGE; C3MFU1.
KW   Carboxypeptidase {ECO:0000313|EMBL:ACP23992.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Hydrolase {ECO:0000313|EMBL:ACP23992.1};
KW   Protease {ECO:0000313|EMBL:ACP23992.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN      185    281       M20_dimer. {ECO:0000259|Pfam:PF07687}.
SQ   SEQUENCE   389 AA;  41951 MW;  A1EB86F54B9045F7 CRC64;
     MKLSAAISNA LPELVAIRRD LHAHPELGLE ERRTSAFIAG HLEALGYTVT TGLAKTGVVG
     TLKVGAGPRS IGIRADIDAL PILEETGLDY ASKTPGLMHA CGHDGHTAML LGAARALAER
     RNFDGTIHLI FQPAEENFGG AKIMIDEGLF DKFPCDAVFA LHNEPNLPFG QFALREGPIG
     AAVDEARITV HGRGGHGAEP QETADPIVCG ASIVMALQTI VSRNIHPMDP TVVTVGAFHA
     GSASNIIPER AEIVVGIRSF DPAVRDALER RIRMIAEAQA ASFGMRATVD YQRSYDATIN
     HKSETDFVRD LAVRFAGADK VVDLARPYMG SEDFAYMLKE RPGTYFFLGS RVTGEEKPLH
     HPGYNFNDDL LPIGAAFWTE LAEAYLARA
//

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