(data stored in ACNUC7421 zone)

SWISSPROT: B4SSK4_STRM5

ID   B4SSK4_STRM5            Unreviewed;       718 AA.
AC   B4SSK4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   SubName: Full=Peptidyl-dipeptidase Dcp {ECO:0000313|EMBL:ACF49886.1};
DE            EC=3.4.15.5 {ECO:0000313|EMBL:ACF49886.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0181 {ECO:0000313|EMBL:ACF49886.1};
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:ACF49886.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49886.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49886.1,
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.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP001111; ACF49886.1; -; Genomic_DNA.
DR   RefSeq; WP_012509732.1; NC_011071.1.
DR   STRING; 391008.Smal_0181; -.
DR   MEROPS; M03.005; -.
DR   EnsemblBacteria; ACF49886; ACF49886; Smal_0181.
DR   KEGG; smt:Smal_0181; -.
DR   eggNOG; ENOG4105DGW; Bacteria.
DR   eggNOG; COG0339; LUCA.
DR   HOGENOM; HOG000245984; -.
DR   KO; K01284; -.
DR   OMA; FASQRYA; -.
DR   OrthoDB; 1935578at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00910-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.10; -; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   Pfam; PF01432; Peptidase_M3; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SSK4.
DR   SWISS-2DPAGE; B4SSK4.
KW   Carboxypeptidase {ECO:0000313|EMBL:ACF49886.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000256|RuleBase:RU003435,
KW   ECO:0000313|EMBL:ACF49886.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17    718       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002823294.
FT   DOMAIN      270    713       Peptidase_M3. {ECO:0000259|Pfam:PF01432}.
SQ   SEQUENCE   718 AA;  79609 MW;  25251359C38F75E8 CRC64;
     MSRTVVLAAA ISLALAACSG KESTPVSDAQ KAPAQQPAEA STNPLLSAST LPFQAPQFDK
     IKDSDYLPAF EEGMRQHLAD VRKIADNPEP ATFDNTLVAM ERSGETLNRV SRIFFGLVQA
     DGTEARQKIQ EDIAPKLAAH QDEINLDPKL FARVKSLYDQ RDTLELDPVQ KRLVEHYYDG
     LVRAGAQLSD ADKASLRKLN VEETTLSTQF HTRLVAATAA AAVVVDDKAK LAGLDDNAIN
     NAASAAKDRK LDGKFLLPLQ NTTQQPVLGS LTDRDQRAAV LKASETRAER GDANDTRQTV
     QRLAQLRAQK AKLLGFDTFA DYQLGDQMAK TPAAALKLLT DTVPAATVKA RAEAGEIQKV
     IDAQKGGFQV AASDWDFYAE QVRKAKYDLD ESQIKPYFEL DNVLQNGVFY AATQLYGITF
     KPRTDIPTYN PDMKVYEVFD KDGTSLALFY TDYFKRDTKS GGAWMDVFVE QDGLTGAKPV
     VYNVCNFTKP ADGQPALISF DDVTTMFHEF GHALHGMFSN VKYPSIAGTA TSRDFVEFPS
     QFNEHWALDP KVFANYAKHY KTGEAMPQEL VDKILKARSF NQGYATTEYL SAALLDLAWH
     TQKADAPLQD VGAFEASALK KFKVDLPQVP PRYRTTYFDH IWGGGYSAGY YAYFWAEVLD
     HDAYQWFTEH GGLTAANGQE FRDKILSRGN SVELSTLYRD FRGKDPSVEP LLKFRGLK
//

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