ID A0A150IP87_9EURY Unreviewed; 471 AA.
AC A0A150IP87;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Pyrolysin {ECO:0000313|EMBL:KYC46662.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:KYC46662.1};
GN Name=pls {ECO:0000313|EMBL:KYC46662.1};
GN ORFNames=AMQ22_02086 {ECO:0000313|EMBL:KYC46662.1};
OS Candidatus Methanofastidiosum methylthiophilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC Methanofastidiosum.
OX NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC46662.1, ECO:0000313|Proteomes:UP000075398};
RN [1] {ECO:0000313|EMBL:KYC46662.1, ECO:0000313|Proteomes:UP000075398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U1lsi0528_Bin055 {ECO:0000313|EMBL:KYC46662.1};
RX PubMed=26943620;
RA Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT fastidious methyl-reducing methanogen.";
RL ISME J. 0:0-0(2016).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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:KYC46662.1}.
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DR EMBL; LNGC01000181; KYC46662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150IP87; -.
DR Proteomes; UP000075398; 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 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; 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 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; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 142..437
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 185
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 390
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 471 AA; 50662 MW; 27434A2A88903C71 CRC64;
MKKALGAYIV FILLMSAVPI LGEATNYDKM DKAVRAKVES GLSNIDLIIE FYELDDSSRA
LIPKEKIINE FIELNSIHAI LNANEIKNIS SSEYVKNIWG NVGGLTLFDT ITFSSEDQIV
INGFMGADTI KASPLYNIGY KGNGVTVAVL DTGILETHVE FPEGKILYQY DFVNKDVVAD
DLDGHGTFVS GIISGQAYTT ADWAGYYNFV NTTPTNTMGV SPGSKLVILK IIENNQGKLS
DYFEACNWLI SNKNIYNIRV VNMSAGWDVD SMILSGWPLD GTDPASMAAN SVVDKGIVWV
NAAGNGGPSL DTIGAPARAK NVITVANAID RTVVLDTPIA ITRAPISIAN DSSRGGGYSG
LKPDISAPGT QILSSFIGND YDYGLASGTS FASPFVAGSV AILIQRHPNW TPYQVKIALM
RTATPISGAS AYEQGAGIVN LNGAFSYRQD FERTSVIGKV MEILKKNKEN N
//
