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Database: UniProt
Entry: A0A0N1GQA2_9ACTN
LinkDB: A0A0N1GQA2_9ACTN
Original site: A0A0N1GQA2_9ACTN 
ID   A0A0N1GQA2_9ACTN        Unreviewed;       402 AA.
AC   A0A0N1GQA2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   10-APR-2019, entry version 15.
DE   SubName: Full=Aqualysin 1 {ECO:0000313|EMBL:KPI29893.1};
DE            EC=3.4.21.111 {ECO:0000313|EMBL:KPI29893.1};
DE   Flags: Precursor;
GN   ORFNames=OV320_3309 {ECO:0000313|EMBL:KPI29893.1};
OS   Actinobacteria bacterium OV320.
OC   Bacteria; Actinobacteria.
OX   NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI29893.1, ECO:0000313|Proteomes:UP000037870};
RN   [1] {ECO:0000313|EMBL:KPI29893.1, ECO:0000313|Proteomes:UP000037870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV320 {ECO:0000313|EMBL:KPI29893.1,
RC   ECO:0000313|Proteomes:UP000037870};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074
RT   OV450 and OV320.";
RL   Submitted (AUG-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:KPI29893.1}.
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DR   EMBL; LJCX01000023; KPI29893.1; -; Genomic_DNA.
DR   RefSeq; WP_054239306.1; NZ_LJCX01000023.1.
DR   EnsemblBacteria; KPI29893; KPI29893; OV320_3309.
DR   PATRIC; fig|1592329.3.peg.2511; -.
DR   Proteomes; UP000037870; 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; 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; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000037870};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000313|EMBL:KPI29893.1};
KW   Protease {ECO:0000256|RuleBase:RU003355};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037870};
KW   Serine protease {ECO:0000256|RuleBase:RU003355};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     33       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        34    402       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5005872565.
FT   DOMAIN       53    121       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      154    383       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
SQ   SEQUENCE   402 AA;  39671 MW;  2820244D53B0B2D9 CRC64;
     MAQLRSNKAR ITAAATVAAA ALVGGLTALP AQAAPAEGKV LAAGSPTAVK DSYIVTLKSQ
     AGFKASSATG KNLVKGYGGT VGKTFGSALN GYTATLSATE ARRLAADPAV ATVEQNQTVR
     VSDTTQSSAP WGLDRVDQTS LPLSGTYTYP DTAGSGVTAY VIDTGVRITH SQISGRASYG
     YDAVDGDTTA SDGNGHGTHV ATTIAGSTYG VAKKAKIVAV RVLDNAGSGT TAGVIAGIDW
     VTNNHSGPSV ANLSLGGGAS TTLDTAVRNS IASGVAYAVA AGNSSANASS YSPARVTQAI
     TVGATTSTDA RASYSNYGSV LDIFAPGSSI TAGWYTSDTA TNTISGTSMA TPHVAGAAAV
     YLAGHTSATP AQVATALVNG ATSNVVTSPG TGSPNKLLKI VP
//
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