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Database: UniProt
Entry: A0A0X3XIH4_9ACTN
LinkDB: A0A0X3XIH4_9ACTN
Original site: A0A0X3XIH4_9ACTN 
ID   A0A0X3XIH4_9ACTN        Unreviewed;       525 AA.
AC   A0A0X3XIH4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-FEB-2019, entry version 15.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:KUL69754.1};
GN   ORFNames=ADL34_29235 {ECO:0000313|EMBL:KUL69754.1};
OS   Streptomyces sp. NRRL WC-3605.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL69754.1, ECO:0000313|Proteomes:UP000052945};
RN   [1] {ECO:0000313|EMBL:KUL69754.1, ECO:0000313|Proteomes:UP000052945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL69754.1,
RC   ECO:0000313|Proteomes:UP000052945};
RA   Gilbert D.G.;
RL   Submitted (OCT-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:KUL69754.1}.
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DR   EMBL; LLZN01000091; KUL69754.1; -; Genomic_DNA.
DR   RefSeq; WP_062668647.1; NZ_LLZN01000091.1.
DR   EnsemblBacteria; KUL69754; KUL69754; ADL34_29235.
DR   OrthoDB; 923655at2; -.
DR   BioCyc; GCF_001509795:G1EPH-5963-MONOMER; -.
DR   Proteomes; UP000052945; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd04077; Peptidases_S8_PCSK9_Proteinase; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002884; P_dom.
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   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000052945};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355};
KW   Protease {ECO:0000256|RuleBase:RU003355, ECO:0000313|EMBL:KUL69754.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052945};
KW   Serine protease {ECO:0000256|RuleBase:RU003355};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     38       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        39    525       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007058042.
FT   DOMAIN      409    525       P/Homo B. {ECO:0000259|PROSITE:PS51829}.
SQ   SEQUENCE   525 AA;  53485 MW;  C54AFA7D1D333741 CRC64;
     MAVMRTPQRT TRRRLALLST AATAVLAAGL VTALPASAAP EGHVQYAGAA NAVADSYIVT
     LKADRARSDS KTARALVERY GAGIERTYRT ALNGYEVEAS ETEAARLAAD PAVASVVQNR
     TFHVEGTQPS PPSWGLDRID QKNLPLDNSY TYPDSAGQGV TAYIIDTGVR ITHQDFGGRA
     SYGYDAIDND NTAQDGHGHG THVAGTVAGS SYGVAKKAKI VGVRVLNNSG SGTTAQVVAG
     IDWVARNAVK PAVANMSLGG GADTALDTAV RNAIASGVTF AVAAGNESTN ASTKSPARVT
     EAITVGATTS TDARASYSNY GSALDLFAPG SSITSSWNSG DSATNTISGT SMATPHVAGA
     AALYLADNPS ATPAQVASAL TEAATSGVVG SPGSGSPNRL LYVGGGTTTP PGPRFENTAD
     HTIADNATAE SPVTVSGVSG NAPSALAVEV HIVHTYIGDL QIQLVAPDGS AYTLKSYGTG
     GSADNIDTTY TVNASSETAD GTWKLRVSDN ARLDTGRIDA WALQF
//
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