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Database: UniProt
Entry: A0A0F4JGB8_9ACTN
LinkDB: A0A0F4JGB8_9ACTN
Original site: A0A0F4JGB8_9ACTN 
ID   A0A0F4JGB8_9ACTN        Unreviewed;       393 AA.
AC   A0A0F4JGB8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   10-APR-2019, entry version 19.
DE   SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KJY33397.1};
GN   ORFNames=VR44_14005 {ECO:0000313|EMBL:KJY33397.1};
OS   Streptomyces katrae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY33397.1, ECO:0000313|Proteomes:UP000033551};
RN   [1] {ECO:0000313|EMBL:KJY33397.1, ECO:0000313|Proteomes:UP000033551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY33397.1,
RC   ECO:0000313|Proteomes:UP000033551};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KJY33397.1}.
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DR   EMBL; JZWV01000360; KJY33397.1; -; Genomic_DNA.
DR   RefSeq; WP_045947806.1; NZ_JZWV01000360.1.
DR   EnsemblBacteria; KJY33397; KJY33397; VR44_14005.
DR   PATRIC; fig|68223.7.peg.7104; -.
DR   Proteomes; UP000033551; 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:UP000033551};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355};
KW   Protease {ECO:0000256|RuleBase:RU003355};
KW   Serine protease {ECO:0000256|RuleBase:RU003355};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    393       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002470913.
FT   DOMAIN       70    106       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      146    372       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
SQ   SEQUENCE   393 AA;  39793 MW;  F5780E88C4FDBBAA CRC64;
     MRTLARLAAA ALLTATPVTA GTASAAGPEP TPAPLHTAVN AVPGQYIVTL QKGVDAAKTA
     QKLGLKPAFV YTSAMNGFAV PLTPLQLTIV RNSLGVKAVE EDARVQSVPT PSSRAGVRAP
     AASWGLDRID QRSLPLNDEF ITHGNGAGVT AYILDTGIDY AHSEFGGRAT FGFDAMGDGQ
     GGQDCNGHGT HVAGTVAGST YGVARKANLV SVRVLGCDAK GSWSGIIAGM DWVAKNATQP
     AVLNASLGGD RSQAVNDAAT ALSDAGVLPV VAAGNSAKDA CTVSPASAAR VVTVGATDWF
     DQEASFSNYG SCLSLYAPGR DILSAKLGGG SVALNGTSMA SPHVAGVAAL YKAAHPKADP
     AELKQFLDHT STKDVITNIG EGSPNKLLFT GAQ
//
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