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Database: UniProt
Entry: A0A1G8HYW0_9MICC
LinkDB: A0A1G8HYW0_9MICC
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ID   A0A1G8HYW0_9MICC        Unreviewed;      1029 AA.
AC   A0A1G8HYW0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Peptidase inhibitor I9 {ECO:0000313|EMBL:SDI11711.1};
GN   ORFNames=SAMN04488693_10671 {ECO:0000313|EMBL:SDI11711.1};
OS   Arthrobacter subterraneus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=335973 {ECO:0000313|EMBL:SDI11711.1, ECO:0000313|Proteomes:UP000199258};
RN   [1] {ECO:0000313|EMBL:SDI11711.1, ECO:0000313|Proteomes:UP000199258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP_1H {ECO:0000313|EMBL:SDI11711.1,
RC   ECO:0000313|Proteomes:UP000199258};
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|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; FNDT01000006; SDI11711.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8HYW0; -.
DR   STRING; 335973.SAMN04488693_10671; -.
DR   Proteomes; UP000199258; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02120; PA_subtilisin_like; 1.
DR   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 2.60.40.2310; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034197; Peptidases_S8_3.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000199258};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          44..139
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          172..649
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          453..522
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          701..793
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   REGION          1006..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        181
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        279
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        605
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1029 AA;  104480 MW;  363A8BE1BC883842 CRC64;
     MVGLPLILGS MSAVPAAAVP AGPTATQQIQ PVKKVDPGNY PDGRYIVVLN EEPAAMYDGG
     VPGIEATKPE KGEKLSEKKD FQKYKSHLEQ KQQAVAGEKG VAIKRSYTAA LNGFSAKLTS
     DQAVELAKDP GVRMVAPDVE NAPDDYSSLD ILNLRGEGGA WNTQFGGEAN AGAGTVVGVI
     DTGYTPSSPF FQGTEVVKLK KGEQPQVGQP YRAKGGIAML KSDGTTFLGE CEVGVRFSGT
     ECNSKVLAAQ YFSEDFEEYV PKANRAPEEV LSPIDVDSHG THTASTAVGN SNVTQTVAGR
     DFGKSSGVAP AAKLSVYKVC WADNDPNTGG CYSSASIAAI NQAVLDGVDV LNYSISGSAT
     TTTDPVSLAF LGAASAGVFV SASAGNSGPT ASTVNHGAPW VTTVAASTFS HALQGTAEFA
     DGTKFRGASI MSAGVPASPV VLSANAAAAG AKDGDLCAPN SLDPTRVAGK IVVCDRGVYD
     RVAKSAEVAR TGGVGMILVN LTDSSMDTDK HSVPTIHVNT PASLELKEKV AANPDMLVAL
     VDEDTTGEPL PPVPQIAGFS SRGPLLATGS DLLKPDVAAP GVAVLAGVSP IGTGGDEFGF
     LSGTSMAAPH VAGVGALILA KNPAWSPAAV KSAMMTTADP VKNAQGGVDG DVFATGAGQV
     DPISVLNPGL VYDAGRIEYL QFVEGTGYAD VKGVEGIDAK NMNVPSFAVG NLTGKTTVTR
     TVTALTPGTY TATANVPGVN VKVTPSVLNF TKAGEKQTFE VTFENAEAQL GKFAKGSLVW
     EGQGKVVASP VAVRPQSVVA PSQVAFTSEG PDGSGTIPVT SGTNAPVSMT LQGLSKANSS
     PLSLVPGPVV VENNASNYVT EVTVPKDTPF ASLSVLSADP GADFDLFVFD PNGRLYQVAT
     ASASETLNLQ NPVPGVYKAI VNLYASPNGQ ATAATFDAAI LGADEGNASI APNPLELANG
     ESGEVTLNWA GLEPGSYVGR VTYAGSTAVT FVSVVVDGAG VAAPTAVSPT GGANKLPSAD
     GDSTPTNGQ
//
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