(data stored in ACNUC7421 zone)

SWISSPROT: B4SIC8_STRM5

ID   B4SIC8_STRM5            Unreviewed;       703 AA.
AC   B4SIC8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   SubName: Full=Endothelin-converting enzyme 1 {ECO:0000313|EMBL:ACF50133.1};
DE            EC=3.4.24.71 {ECO:0000313|EMBL:ACF50133.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0428 {ECO:0000313|EMBL:ACF50133.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50133.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50133.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50133.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001111; ACF50133.1; -; Genomic_DNA.
DR   RefSeq; WP_012509925.1; NC_011071.1.
DR   STRING; 391008.Smal_0428; -.
DR   MEROPS; M13.009; -.
DR   EnsemblBacteria; ACF50133; ACF50133; Smal_0428.
DR   KEGG; smt:Smal_0428; -.
DR   eggNOG; ENOG4105C9K; Bacteria.
DR   eggNOG; COG3590; LUCA.
DR   HOGENOM; HOG000245572; -.
DR   KO; K07386; -.
DR   OMA; HLYDNFT; -.
DR   OrthoDB; 305005at2; -.
DR   BioCyc; SMAL391008:SMAL_RS02205-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd08662; M13; 1.
DR   Gene3D; 1.10.1380.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR018497; Peptidase_M13_C.
DR   InterPro; IPR042089; Peptidase_M13_dom_2.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   PANTHER; PTHR11733; PTHR11733; 1.
DR   Pfam; PF01431; Peptidase_M13; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   PRINTS; PR00786; NEPRILYSIN.
PE   4: Predicted;
DR   PRODOM; B4SIC8.
DR   SWISS-2DPAGE; B4SIC8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000313|EMBL:ACF50133.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    703       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002825986.
FT   DOMAIN       65    448       Peptidase_M13_N. {ECO:0000259|Pfam:
FT                                PF05649}.
FT   DOMAIN      500    700       Peptidase_M13. {ECO:0000259|Pfam:
FT                                PF01431}.
SQ   SEQUENCE   703 AA;  76249 MW;  41646991106C8D14 CRC64;
     MSKLRRPTLA LAIVASLSLA ACDRPAEPAA GTAAPADAAP AAAKPMLGSF GFDASGMDRS
     IAAGDDFFGF ANGTWVKNTE IPADRSRFGS FNVIAEKTLA DTRAILEGAA GNAQANGDDK
     LIGDYYAAFM DEAGIEQHGL APVQPQLKAI EAIADKAGLA RTLGGDMRAD VDLLNATNFY
     TDRLFGLWVS VDMLQPDRTA PYLVQGGLGM PDRDFYLGGG RMAELRKQYQ AYIAQMLQLA
     GVADPAGKAQ RILALETKIA QAHATQEETN DVTKGANPWT QADFNAKAPG MDWNAFLDAA
     ALGKQQDFIV WQPKAVAGLS KLVATEPLDA WKDYLAFHAL DRAAAYLPKK FADARFAFHG
     TALSGTPQQS DRWKRAVDDA NHAVGEAIGK RYVEKHFDAK TKERADEMAK NIIAAFAKRI
     DALAWMSPQT KASAKAKVAG LTVGMGYPEK WRDYSGLEIR RDDALGNAQR AELFEYQRNI
     AKLGKPVDHS EWAMLPQTIN AMNVPLENRL VFPAAILQPP FFDGAADDAV NYGAIGAVIG
     HEISHGFDNA GALFDETGKL HNWWTAEDLK QFNAAGDALA AQFSSYEPFP GVHVNGKLSL
     GENIADVAGL GTAYDAYQLS LQGKPAQTLE GFTPDQRFFL GFAQAWRSKS REQALRNSLL
     TDVHAPGQFR ALTVRNIDAW YPAFEVKEGQ KLYLAPDKRV KVW
//

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