ID   A0A1H9X2V6_9PSEU        Unreviewed;       517 AA.
AC   A0A1H9X2V6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Peptidase inhibitor I9 {ECO:0000313|EMBL:SES39973.1};
GN   ORFNames=SAMN04487818_112136 {ECO:0000313|EMBL:SES39973.1};
OS   Actinokineospora terrae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=155974 {ECO:0000313|EMBL:SES39973.1, ECO:0000313|Proteomes:UP000199051};
RN   [1] {ECO:0000313|EMBL:SES39973.1, ECO:0000313|Proteomes:UP000199051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44260 {ECO:0000313|EMBL:SES39973.1,
RC   ECO:0000313|Proteomes:UP000199051};
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,
CC       ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; FOGI01000012; SES39973.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9X2V6; -.
DR   STRING; 155974.SAMN04487818_112136; -.
DR   Proteomes; UP000199051; 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; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; 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   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
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; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 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   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:UP000199051};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..517
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011440576"
FT   DOMAIN          398..517
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        191
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        339
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   517 AA;  53320 MW;  DC8C58A49EB9769F CRC64;
     MQERRTRWIS SLFAVAIAAA AVATTTGVAA AQQAEADVVQ AKQHYSGQYI VVLKSGARAA
     AEGQAASLAQ RYGGQVTDTY SVTLNGFSAR GLTEQQARRL AADPSVKTVY QDGTTRANDD
     QLNPPSWGLD QVDQRTATLD KKYTYPNSGE GVTAYVIDSG VYAAHSEFEG RASYGYDFLD
     NDTDASDCYF HGTHVSGTIA GKTVGVAKKA KIVAVRSLDC KGSGPDSATV SAMEWVAKNA
     VKPAVVNLSL GMDTVGVGDE QAKAMVAKGI VVAVSAGNAG QDACGVSPAR VPEVITVGWF
     NKDRTRGGNF GTCVDLFAPG GNIYSSDHTG QFRNASGTSM ASPHVAGAAA LYLSANPSAT
     PQQVSDALVR SATPDLVSNP GTGSPNKLLY VGDIGGGTPP SQCGVKTNDD DVAIPDAGTA
     VGSSVSQSAC PGKASATLAV RVDIDHGYTG DLAIDLVGPS GTSYPLKKSG DVGESGGVHK
     SFSVDASRED ANGTWKLSVR DVYKFDAGTL TAWSITF
//