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Database: UniProt/TrEMBL
Entry: H6RB75_NOCCG
LinkDB: H6RB75_NOCCG
Original site: H6RB75_NOCCG 
ID   H6RB75_NOCCG            Unreviewed;       320 AA.
AC   H6RB75;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   29-OCT-2014, entry version 13.
DE   RecName: Full=Proline iminopeptidase {ECO:0000256|RuleBase:RU003421};
DE            EC=3.4.11.5 {ECO:0000256|RuleBase:RU003421};
GN   Name=pip {ECO:0000313|EMBL:CCF62509.1};
GN   OrderedLocusNames=NOCYR_1723 {ECO:0000313|EMBL:CCF62509.1};
OS   Nocardia cyriacigeorgica (strain GUH-2).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF62509.1, ECO:0000313|Proteomes:UP000008190};
RN   [1] {ECO:0000313|EMBL:CCF62509.1, ECO:0000313|Proteomes:UP000008190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GUH-2 {ECO:0000313|EMBL:CCF62509.1,
RC   ECO:0000313|Proteomes:UP000008190};
RX   PubMed=22461543; DOI=10.1128/JB.00161-12;
RA   Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA   Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA   Nazaret S., Neto M., Petit S., Roche D., Vallenet D.,
RA   Rodriguez-Nava V., Richard Y., Cournoyer B., Blaha D.;
RT   "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT   cyriacigeorgica GUH-2.";
RL   J. Bacteriol. 194:2098-2099(2012).
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal proline from a peptide.
CC       {ECO:0000256|RuleBase:RU003421}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|RuleBase:RU003421}.
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DR   EMBL; FO082843; CCF62509.1; -; Genomic_DNA.
DR   RefSeq; WP_014349974.1; NC_016887.1.
DR   RefSeq; YP_005263149.1; NC_016887.1.
DR   MEROPS; S33.001; -.
DR   EnsemblBacteria; CCF62509; CCF62509; NOCYR_1723.
DR   GeneID; 11926611; -.
DR   KEGG; ncy:NOCYR_1723; -.
DR   KO; K01259; -.
DR   OMA; WYYQFGV; -.
DR   BioCyc; NCYR1127134:GLHX-1718-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   InterPro; IPR005944; Pro_iminopeptidase.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF006431; Pept_S33; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01249; pro_imino_pep_1; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU003421,
KW   ECO:0000313|EMBL:CCF62509.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008190};
KW   Hydrolase {ECO:0000256|RuleBase:RU003421};
KW   Protease {ECO:0000256|RuleBase:RU003421};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008190}.
FT   ACT_SITE    114    114       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006431-1}.
FT   ACT_SITE    270    270       {ECO:0000256|PIRSR:PIRSR006431-1}.
FT   ACT_SITE    298    298       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006431-1}.
SQ   SEQUENCE   320 AA;  35457 MW;  FC6A2D7EDCB896DD CRC64;
     MRTLYPPIEP HQRGMLDVGA GQSVYWEVSG NPEGKPAVFL HGGPGGGTAP FHRQFFDPEQ
     YRIVLFDQRG CGRSTPHIAD GADLSVNTTD HLIADIEQLR EALGIEQWLV FGGSWGSTLA
     LAYAQRYPQR VTELVLRGIF LLRRKEIDWY YNGAAGYVYP DEWEKFLAPV PEAERDGDLV
     EAYHRLLHSP DEEIATAAAV AWSTWEGATS SLLPQPDRVA ETGEPRFALA FARIENHYFR
     HGGFLDEGQL LRDIDKIAGI PAVIVQGRHD IVCPAVSAWE LHRAWPGSVL HIVDDAGHAA
     NEPGITHHLV EATDGFAKGR
//
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