(data stored in ACNUC7421 zone)

HOGENOM: SHEDO_1_PE1007

ID   SHEDO_1_PE1007                       STANDARD;      PRT;   630 AA.
AC   SHEDO_1_PE1007; Q12QH2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Secreted peptidase A. Serine peptidase MEROPS family
DE   S08A;Flags: Precursor; (SHEDO_1.PE1007).
GN   OrderedLocusNames=Sden_1016;
OS   SHEWANELLA DENITRIFICANS OS217.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHEDO_1.PE1007.
CC       Shewanella denitrificans OS217, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:Q12QH2_SHEDO
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC   -!- GENE_FAMILY: HOG000199176 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q12QH2; -.
DR   EMBL; CP000302; ABE54304.1; -; Genomic_DNA.
DR   RefSeq; YP_562027.1; NC_007954.1.
DR   ProteinModelPortal; Q12QH2; -.
DR   SMR; Q12QH2; 129-406.
DR   STRING; Q12QH2; -.
DR   MEROPS; S08.050; -.
DR   GeneID; 4016584; -.
DR   GenomeReviews; CP000302_GR; Sden_1016.
DR   KEGG; sdn:Sden_1016; -.
DR   NMPDR; fig|318161.14.peg.997; -.
DR   eggNOG; COG1404; -.
DR   OMA; LRGYSAY; -.
DR   PhylomeDB; Q12QH2; -.
DR   ProtClustDB; CLSK873886; -.
DR   BioCyc; SDEN318161:SDEN_1016-MONOMER; -.
DR   GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   InterPro; IPR000209; Peptidase_S8/S53.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; Prot_inh_S8A.
DR   Gene3D; G3DSA:3.40.50.200; Pept_S8_S53; 1.
DR   PANTHER; PTHR10795; SubtilSerProt; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF04151; PPC; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Pept_S8_S53; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
DR   HOGENOMDNA; SHEDO_1.PE1007; -.
KW   peptidase S8/S53 subtilisin kexin sedolisin;
KW   Complete proteome; Hydrolase; Protease; Serine protease; Signal.
SQ   SEQUENCE   630 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEINMQNKHK IALAVLASLS TMSLQTQAAE LLSIDSANAI KDTYIVVFDT PSVLNTQDAS
     AMADFATQQG NSLANEYNIS VINNFGSALN GVLIKANAKQ VNELLNDPKI KYIEQDQMMS
     ITPQVSIAGD QASPTWGIDR IDQRDLPLSN SYHYDYDGTG VTAYVVDTGV LNGHNEFGGR
     ASSGYDFIDN DSDTTDCNGH GTHVAGTIGG STYGVAKNVN IVGVRVLNCS GSGSNSGVIA
     GINWVKNNAS GPSVANMSLG GGASQATDDA VNAAVAAGIS FVVAAGNDNS NACNYSPARA
     ADAVTVGSTT STDARSSFSN YGTCLDIYAP GSSIKSAWYT SNSATNTISG TSMAAPHVAG
     VAALYLNETP SMTPTQVTGM LSSRASSGKV SDAKTGSPNA LLYSLAGGCG SDCPPPPGDT
     ELFDEQAVST SGAQGSETHY FIEVPANATS LAVNLAGGSG DADIYVSQGT KPTLTSYQCR
     PFKNGNNESC NFTNPAAGKW YVMVQGYSAY ANANLTADYT VGGGSTCNTS DCLVNGVPRT
     GLAGASGSQT FYKVIVPANR TLTVAMSGGS GDADLYVKAG TQPTTGSFDC RPYLNGNNET
     CSFTPTVETT YHVMLRGYSA YSGTSLVANY
//

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