ID A0A1C3N8B9_9ACTN Unreviewed; 623 AA.
AC A0A1C3N8B9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Serine protease, subtilisin family {ECO:0000313|EMBL:SBV28827.1};
GN ORFNames=GA0070620_4384 {ECO:0000313|EMBL:SBV28827.1};
OS Micromonospora krabiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=307121 {ECO:0000313|EMBL:SBV28827.1, ECO:0000313|Proteomes:UP000199393};
RN [1] {ECO:0000313|Proteomes:UP000199393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45344 {ECO:0000313|Proteomes:UP000199393};
RA Varghese N.;
RL Submitted (JUN-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; LT598496; SBV28827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C3N8B9; -.
DR STRING; 307121.GA0070620_4384; -.
DR PATRIC; fig|307121.4.peg.4479; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000199393; Chromosome i.
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:UP000199393};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..623
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008678778"
FT DOMAIN 501..623
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 623 AA; 61930 MW; 67F9737BD63C413C CRC64;
MGLAHRSVLV GVATLSMLVA ATPALAAEPT GTIRAAGGET AVADSYIVVF KDTAVGRDTV
GDNASRLVGR HGGTVARTYG AALRGFEVRV GAKAAARIAA DPAVAYVEQN HTVSIAGTQT
NPPSWGLDRI DQRNLPLNSS YTYPNTASNV RAYIIDTGVL YGHNDFGGRA VSGFDAVDGG
SADDCNGHGT HVAGTVGGSA YGVAKGVQIV GVRVLNCQGS GTNAQVVAGI DWVTANAVKP
AVANMSLGGS ANSSIDTAVN NSINSGVTYA VAAGNGNALG VRQNACNYSP ARVPAAITVG
ATQNNDAAAS FSNFGTCVDI LAPGVNITSA WYTSASATNT ISGTSMASPH VAGAAALVLS
ANPSWTPQQV RDNLVSNSTP NVVTNVGTGT PNQLLYVVNG TPPANDFSVS VSPTSGSTAP
GGSVTATVGT ATTAGSAQSV SLSASGLPTG ATASFSPATV TSGGSSTLTI ATSASTPAGT
YPITITGTGT AGARTATYTL TVTGSGGGGC SGTNGTDVAI PDTGATVAST IAIAGCNRNA
SSSSTVAVNI VHTYRGDLVI DLVAPDGSSY RLKNSSYFDG ADNVNTTYTA NLSSEAANGT
WRLQVRDVYA GDTGYINTWT LTL
//
