ID A0A0Q8VF83_9ACTN Unreviewed; 449 AA.
AC A0A0Q8VF83;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=ASE19_12680 {ECO:0000313|EMBL:KRC53213.1};
OS Nocardioides sp. Root79.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC53213.1, ECO:0000313|Proteomes:UP000051414};
RN [1] {ECO:0000313|EMBL:KRC53213.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC53213.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC53213.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC53213.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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: 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:KRC53213.1}.
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DR EMBL; LMIP01000011; KRC53213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8VF83; -.
DR Proteomes; UP000051414; 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; cd00306; Peptidases_S8_S53; 1.
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; IPR023828; Peptidase_S8_Ser-AS.
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.
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:UP000051414};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 179..414
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 149..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 399
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 449 AA; 48498 MW; F620CFA2D502AF2C CRC64;
MRPTDTTTGS EARIAREKLR VQAKVIRDAF DGAVAAAGRE DTPVKDDADL HYLYRPGHAL
VRADRFEDVL DFFRRRENDF RGEPKHVSSP APGLVLVALP SRRDEADDVL TTLAEIDKFF
GRPEDSRSAP IASPDHVVYV TGTKPGLCPA DEPSPPTPRA AQPWPRPTAT RTRIRDEDRV
RVAVVDTGLW TGAIGSPKSP WLEKGDVLAD AEDIEVVDPN KIHPYAGHGT FVAGVVSCLA
PDTRIEVEGV LTHGGAVLES EIVEQLHQAI NDDNHPQVIS ISAGTHTRGD FASLAFEMLG
SANKLSERDD ILIVAAAGND SSDKPFWPAA FDWVVGVGSV DPDGKVSDFS NVGESWVTVY
ARGRDHVNAF PKGTYTCYEP PNVGQVRTFD GLARWSGTSF STPLVTGLVA ARVRETGQSV
RDAWKDVLGT ATSTTDPRGG QIKVVGPLT
//
