(data stored in SCRATCH zone)

SWISSPROT: C1ARZ0_RHOOB

ID   C1ARZ0_RHOOB            Unreviewed;       379 AA.
AC   C1ARZ0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   SubName: Full=Putative Xaa-Pro dipeptidase {ECO:0000313|EMBL:BAH48817.1};
DE            EC=3.4.13.9 {ECO:0000313|EMBL:BAH48817.1};
GN   Name=pepQ {ECO:0000313|EMBL:BAH48817.1};
GN   OrderedLocusNames=ROP_05700 {ECO:0000313|EMBL:BAH48817.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48817.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48817.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48817.1,
RC   ECO:0000313|Proteomes:UP000002212};
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
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M24B family.
CC       {ECO:0000256|RuleBase:RU000590}.
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DR   EMBL; AP011115; BAH48817.1; -; Genomic_DNA.
DR   RefSeq; WP_012687824.1; NC_012522.1.
DR   ProteinModelPortal; C1ARZ0; -.
DR   STRING; 632772.ROP_05700; -.
DR   MEROPS; M24.034; -.
DR   EnsemblBacteria; BAH48817; BAH48817; ROP_05700.
DR   KEGG; rop:ROP_05700; -.
DR   PATRIC; fig|632772.20.peg.628; -.
DR   eggNOG; ENOG4105DC7; Bacteria.
DR   eggNOG; COG0006; LUCA.
DR   HOGENOM; HOG000008760; -.
DR   OMA; IHEWPYL; -.
DR   OrthoDB; POG091H02MH; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.350.10; -; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR028980; Creatinase/Aminopeptidase_P_N.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SUPFAM; SSF53092; SSF53092; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ARZ0.
DR   SWISS-2DPAGE; C1ARZ0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Dipeptidase {ECO:0000313|EMBL:BAH48817.1};
KW   Hydrolase {ECO:0000313|EMBL:BAH48817.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU000590};
KW   Protease {ECO:0000313|EMBL:BAH48817.1}.
FT   DOMAIN       19    151       Creatinase_N. {ECO:0000259|Pfam:PF01321}.
FT   DOMAIN      159    361       Peptidase_M24. {ECO:0000259|Pfam:
FT                                PF00557}.
SQ   SEQUENCE   379 AA;  39697 MW;  D3386C729F1BFBC0 CRC64;
     MSSLGASTSR FPTTIYADRI ARAGALARDA GLDGLLITPG PDLRYLLGSR AESFERLTCL
     VIPANGDTAS VVVPRLELAA LTESATSDLG LTVRDWVDGV DPYALVSGLL PSPARTAVTD
     AMPALHLIPL SEALGALPIL ATEVLRELRM VKDDAEIDAL RRAGQAIDRV HARMGEFLKV
     GRTEAEVAAD ITAAILEEGH TEAAFVIVGS GPHGADPHHE VSERVVESGD VVVIDIGGPV
     EPGYNSDSTR TYSMGEPDPG VAEKFAVLEE AQAAAVALVR PGVTAEAVDA AARDLLAAQG
     LAEVFVHRTG HGIGLSVHEE PYIVSGNSIE LTEGMAFSVE PGIYFRGEWG ARIEDIVVVT
     ADGCEPVNTR PHGLTVLPG
//

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