ID A0A0X3S6Y0_9ACTN Unreviewed; 584 AA.
AC A0A0X3S6Y0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Subtilisin, serine endopeptidase {ECO:0000313|EMBL:KUJ39738.1};
GN ORFNames=ADL25_20275 {ECO:0000313|EMBL:KUJ39738.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ39738.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUJ39738.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMWH01000205; KUJ39738.1; -; Genomic_DNA.
DR RefSeq; WP_059129181.1; NZ_LMWH01000205.1.
DR AlphaFoldDB; A0A0X3S6Y0; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000054048; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054048};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 283..514
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 59862 MW; 2A193691C63E3572 CRC64;
MVKVDVMVKE KPGHSREGGS EGAGAGGPGP EGKDAAPRKK GAPSPIAVHP RRERYMVTPL
PQHLLPPGVP ELGMDAVCDR LERMPEVRVI RRLRPAERLQ SAGVHPSCPE IAVVEAAEAQ
VPAMRSLHVH IEPDLPLAGT GLAAMPTAGT LPLRDPGLVL SLGRPVEITL RVCGPDGEPL
SGAAVFLIGA TWPGQGITGA DGTATVTLAT DTVESVRSLY VRPVGGYNDR WIHRPDLSET
QENLVMLTPL AKAYPELEER QQYGWGQQAM RLDRLPPTFR AFGVRIAVIG SGVSADHPDL
KQRVRSGVDL VHGTADGWAH DVMGSGTHAA GVIAGADTGK GVIGIAVDAE IEVCEVMPGG
HFSDLIAALD HCIDREVDIA NIAVATPYPS SLVSHKLADA NAAGIACVAP AGDTGGPVAF
PGSLPTVFAV GALGVYGSFP PDTSQATHTG PPLTPEGLFA APFSGYGPGV DAAAPGVAVL
SCAPGGGYAS LDGTGTASAH VAGLAALVLA HHEDFHGQLL PRGPGRVQHL FQIIATSCRA
LAAPGTMEAA RVGRGLPDAL VALGLAPGVQ LAPALSPFVP SLAG
//
