ID G7WJY9_METH6 Unreviewed; 956 AA.
AC G7WJY9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN OrderedLocusNames=Mhar_0037 {ECO:0000313|EMBL:AET63430.1};
OS Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET63430.1, ECO:0000313|Proteomes:UP000005877};
RN [1] {ECO:0000313|EMBL:AET63430.1, ECO:0000313|Proteomes:UP000005877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6Ac {ECO:0000313|EMBL:AET63430.1,
RC ECO:0000313|Proteomes:UP000005877};
RX PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT "The genome characteristics and predicted function of methyl-group
RT oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT spp.";
RL PLoS ONE 7:E36756-E36756(2012).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP003117; AET63430.1; -; Genomic_DNA.
DR RefSeq; WP_014585619.1; NC_017527.1.
DR AlphaFoldDB; G7WJY9; -.
DR STRING; 1110509.Mhar_0037; -.
DR GeneID; 12509206; -.
DR KEGG; mhi:Mhar_0037; -.
DR PATRIC; fig|1110509.7.peg.39; -.
DR HOGENOM; CLU_308524_0_0_2; -.
DR Proteomes; UP000005877; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1350.20; -; 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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
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|PROSITE-ProRule:PRU01240};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Reference proteome {ECO:0000313|Proteomes:UP000005877};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240}.
FT DOMAIN 494..755
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 500
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 544
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 722
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 956 AA; 104400 MW; 000DD60DDB16659B CRC64;
MKTEGLLIRS ILIIILGLSL GASLEVGLAR EFGGPLTAVR MAGWTIDDGN LTGYGASWAG
YNESCEEGDL NLSFKLKNLT GEMRVNINID GSNRYSIGFT NTPSLAIDAP AAFVGLIPSA
DYTLSTFIFK YVGETEAPEK FAGNSIPYDP TKEHQVSIIS REGHIQVYIE RIEEAEKTVI
REIDGEMMEG KISALQQVID YADPDPLPPG IIDFETLEGA YVELYDLVLT CRPNQPPTVT
SLGPDPTALR VDRDAIWTAS ASDPEGDPVF YCFWLRGPST GDDWVLQQNW SAEAKWEWRP
SQRGVYRIGA YATDGRHSAD EIFYSKGSWK DDLVYVEERP LVLGEEDSFQ RPDPEELVDG
TADGIDWGGK VPINHVLVVV DERFSFEEAT GIAEDLAKGL NGSVVGQFET ILMFQIKTNR
TTARGDSIEG LIRDIATARE DPSIELAFPN QQIYRESSLS DSVYAEENCK GYEMVRVQES
WDRVNESGVR LFPVKVAVID DGIYRWENCC EFDNATINTT VGGDAFAPAV LEEPLPGFEI
AGSHGTGIMN ILAADPDDGG LVGIASQPLG NKLMINLYNI YPPDDNMSFS TDAFLSLKYA
LENGSTIISC SWGNDRANNA LNVAYKKFFK NISNIAPERL FVCSAGNGGV TTRHSDYKHA
PGGIEISNMI TVGNVMNDRT PAPDSNQNIK DFFEVTLAAP GAQAVWGRND SGDIKNNSGG
TSMAAPHVTA AAAMMRSIYP SLEAKDMKDI LRDTGDITPD DPDELVGRVL NIDGSIDNVL
ENLPETLKDE TRAPLHVEIP RIDGVVTRHT TPKGTNWSLD LTLSDGSGEA KAELKLTQHE
TVISGNGNLY FLPEEDIDGS ASPRSKCPRD DIFGDVAEAF LGNALPTPSQ QPVEARGSFE
ETNLQLSIVS LNDMVRYEMT LSVIGSQITG TFKSYDGRGM ARSRGVCYGS LKKEDI
//