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Database: UniProt
Entry: A0A1C5GUE1_9ACTN
LinkDB: A0A1C5GUE1_9ACTN
Original site: A0A1C5GUE1_9ACTN 
ID   A0A1C5GUE1_9ACTN        Unreviewed;       411 AA.
AC   A0A1C5GUE1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   10-APR-2019, entry version 11.
DE   SubName: Full=Peptidase inhibitor I9 {ECO:0000313|EMBL:SCG37384.1};
GN   ORFNames=GA0070614_0388 {ECO:0000313|EMBL:SCG37384.1};
OS   Micromonospora coxensis.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=356852 {ECO:0000313|EMBL:SCG37384.1, ECO:0000313|Proteomes:UP000198215};
RN   [1] {ECO:0000313|EMBL:SCG37384.1, ECO:0000313|Proteomes:UP000198215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45161 {ECO:0000313|EMBL:SCG37384.1,
RC   ECO:0000313|Proteomes:UP000198215};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; LT607753; SCG37384.1; -; Genomic_DNA.
DR   BioCyc; GCF_900090295:GA0070614_RS01945-MONOMER; -.
DR   Proteomes; UP000198215; Chromosome i.
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:UP000198215};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355};
KW   Protease {ECO:0000256|RuleBase:RU003355};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198215};
KW   Serine protease {ECO:0000256|RuleBase:RU003355};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     32       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        33    411       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008717021.
FT   DOMAIN       51    126       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      159    389       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
SQ   SEQUENCE   411 AA;  42411 MW;  65C86BE725C46022 CRC64;
     MSQPFARRLR AAAAGLLTVT MVTAAAGSPA TAAPAPGQIR YAGGTTAVPD SYIVVLKDRA
     VAHRADARTA ATRAASGLAS RYGATAVGHV YSAAIVGFEA RLSHRAARQL AADPTVAYVE
     QNHVVTASDV QVDPHWNLDR IDQRAAAPLD ARYHYTSSGQ GVTAYILDTG IRKTHVEFEG
     RAVDGFDAID GSLPADDCEG HGTHVAGTVG GRTYGVAKKV RLVSVRVLDC RGRATIDQVI
     AGIDWVTADH RAGEPAVANM SLGGSRSDAQ NDAVTNSIAD GVSYAIAAGN SAVDACQISP
     ASTPEAITVG ATWQDDSRTW FSNVGPCLDI FAPGVAVKSA YTGGDTWTRV MVGTSQAAPH
     VAGTAARVLS AHPSWTPAQV HAYLMANATA GTIPDPGPGS PNRVLYAPPA L
//
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