(data stored in ACNUC7421 zone)

SWISSPROT: B4SIH8_STRM5

ID   B4SIH8_STRM5            Unreviewed;       863 AA.
AC   B4SIH8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   SubName: Full=Peptidase M14 carboxypeptidase A {ECO:0000313|EMBL:ACF50183.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0478 {ECO:0000313|EMBL:ACF50183.1};
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:ACF50183.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50183.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50183.1,
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; ACF50183.1; -; Genomic_DNA.
DR   RefSeq; WP_012509956.1; NC_011071.1.
DR   STRING; 391008.Smal_0478; -.
DR   EnsemblBacteria; ACF50183; ACF50183; Smal_0478.
DR   KEGG; smt:Smal_0478; -.
DR   eggNOG; ENOG4105DX4; Bacteria.
DR   eggNOG; ENOG410XQDN; LUCA.
DR   HOGENOM; HOG000031448; -.
DR   OMA; LTDHHEM; -.
DR   OrthoDB; 96337at2; -.
DR   BioCyc; SMAL391008:SMAL_RS02455-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   4: Predicted;
DR   PRODOM; B4SIH8.
DR   SWISS-2DPAGE; B4SIH8.
KW   Carboxypeptidase {ECO:0000313|EMBL:ACF50183.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000313|EMBL:ACF50183.1};
KW   Protease {ECO:0000313|EMBL:ACF50183.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    863       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002823346.
FT   DOMAIN       60    345       Peptidase_M14. {ECO:0000259|SMART:
FT                                SM00631}.
SQ   SEQUENCE   863 AA;  93289 MW;  E9263F3BA1022F42 CRC64;
     MSLHRRAVLP LLIAAAALFL PHPVQAQSAY FFPQIADPAA FDTAVPTPEQ FLGYPIGSRY
     TRHDQLVAYF QELAKRSDRI SVREIGRSYE GRPLLIATVT AAGNHARLEQ IRQQHATLAD
     PAQPRSAAGD SPVVVWLGYS VHGNETSSAE AAMLTAYYLV ASRSAETQQW LQQAVVLFDP
     AQNPDGRDRA ANWHNAWASD PASADPADKE HVEPFPQGRT NHYFTDLNRD WLALTQQDSR
     PKVEVFHQWY PNVQIDFHEM GKDSTYYFEP SPKSMHSPLI PPASYEFNKT LAKYHAQALD
     ALGSLYYTGE NFDNFSPVYG STYPDFHGAV GVTVEQASSR GRVQESVNGL LTFPFTIRNQ
     VATGLGTVRG AVSERSGLFD LQKQFFQSAL KQAAQQPVKS FVFGDAHDPA LTRRLLELLL
     LHRIEVRALD RAVSVDGQHF EAGSAYVVPV QQAQFRLVHS IFAETPPIKG DVFYGSTSYA
     IAPAYGVAFA GSRSRIEGGA RVTAVPAAQG AVLGGQAGFA YAIDWRDYNA GRALAALQDK
     GLSARAAFQP FTTATAQGEV NFAAGSLVIP VAGQPLQGAA LLEAVTAAAR DAGVQVHSLA
     SGRSREGIDL GSDGVKALRK PAVALVMGEG VAATEIGSAW FLLDQQLHLP ASKLDPQQLG
     KVPLDRYTTI VLSGGTYTGV DATAVAALKR WVQAGGSLVT YGSASKWAIE QKLADGEKPG
     KDEDAADESR RAFGDQRDIA AIERVSGNIL SADVDTSHPL AFGVPRRQLA INKENTVTLQ
     PSANPFSTVV RIDATPRVNG YLSERNRARV AGSAWLLVSA QGQGNVVLFA DDPAHRKYWH
     GTDRLLINAI FFGNLVNPAK ARG
//

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