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Database: UniProt
Entry: A0A1G9SK45_9ACTN
LinkDB: A0A1G9SK45_9ACTN
Original site: A0A1G9SK45_9ACTN 
ID   A0A1G9SK45_9ACTN        Unreviewed;       409 AA.
AC   A0A1G9SK45;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   10-APR-2019, entry version 5.
DE   SubName: Full=Peptidase inhibitor I9 {ECO:0000313|EMBL:SDM35864.1};
GN   ORFNames=SAMN05444921_10792 {ECO:0000313|EMBL:SDM35864.1};
OS   Streptomyces wuyuanensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1196353 {ECO:0000313|EMBL:SDM35864.1, ECO:0000313|Proteomes:UP000199063};
RN   [1] {ECO:0000313|EMBL:SDM35864.1, ECO:0000313|Proteomes:UP000199063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7042 {ECO:0000313|EMBL:SDM35864.1,
RC   ECO:0000313|Proteomes:UP000199063};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; FNHI01000007; SDM35864.1; -; Genomic_DNA.
DR   Proteomes; UP000199063; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd04077; Peptidases_S8_PCSK9_Proteinase; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
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; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000199063};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355};
KW   Protease {ECO:0000256|RuleBase:RU003355};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199063};
KW   Serine protease {ECO:0000256|RuleBase:RU003355};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28    409       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5011621188.
FT   DOMAIN       65    107       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      162    388       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
SQ   SEQUENCE   409 AA;  42108 MW;  E4A133799EE04148 CRC64;
     MRLFARRAAA ALLLAVSAAA PGTAAQADSE GPTPAPLYRS AEPVKGSYIV SLREGADPVA
     VARDAGVKRR YTYNRAMRGF SATLNATQLE TMRLAPGVAA VEEDARVFAH RLPEGPRVAS
     PDRLPEPVDV PAFARQAMSW GLDRADQRAL PLDGQFTAAS TGKGVTVYVV DTGIDYEHSE
     FGGRAVFGFD AIGDGRRGQD CEGHGTHVAG TAAGATYGVA PEARLVSVRV LNCEGEGAWS
     RIIAGLDWVA KNAQQPAVLN ASLGGSTSPS ANAAAKAVFD SGVLPVVAAG NSAEDACGVS
     PASAPNVLTV GATDTEDTET DYSNYGQCLR LYAPGSDIRS ARMGGGTTTM NGTSMAAPHV
     AGVAALYKAA HPAAGPQEVA DWLVAQSTKN VVKSITRGSP NRLLFTGGL
//
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