ID A0A1N6YZV1_9EURY Unreviewed; 448 AA.
AC A0A1N6YZV1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Subtilase family protein {ECO:0000313|EMBL:SIR20049.1};
GN ORFNames=SAMN05421858_1802 {ECO:0000313|EMBL:SIR20049.1};
OS Haladaptatus litoreus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haladaptataceae; Haladaptatus.
OX NCBI_TaxID=553468 {ECO:0000313|EMBL:SIR20049.1, ECO:0000313|Proteomes:UP000186914};
RN [1] {ECO:0000313|Proteomes:UP000186914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7737 {ECO:0000313|Proteomes:UP000186914};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; FTNO01000001; SIR20049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6YZV1; -.
DR OrthoDB; 341609at2157; -.
DR Proteomes; UP000186914; 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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR006311; TAT_signal.
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; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
DR PROSITE; PS51318; TAT; 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:UP000186914};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 126..428
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 389
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 448 AA; 47216 MW; F3EB651B7BABE106 CRC64;
MSKDTTRRSF LKSAGVALSG LALTTQSVSA SSSEDRYIVD LESASEDVLS GLTVVHRLDQ
FGIAVVEGDE SQVQGTRYST DVEMELNQAE IEDNGDGDEP GPHKLSQLQW DKQAQGISGI
HGTTRGEGTR VSVIDSGALE THPDLAGVLN TDLSKNFTGD GGDYNPIISD HGTHVSGIIA
GDDTNGSGIF GTAPGTDLVA LRVFTGPFAT FGDIIAAMVF SADIESDVAN MSLGAYPLPD
NADTELLRES IERATDYANE QGTLMVAAAG NDGINLDTDG DVISLPNEAD NVMSISATGP
IGYRWNDPGN GRRIRNYHAA FNHIDEPTTT PAPYTNYGEE AIDISAPGGN AIPSEPEGEN
WQYDMVLSTI FEWGDDGMVP AHGWKAGTSM AAPQVSATAA LVKSVNPDAT PAQLRDHLEA
TAEDVGQPTY SGKGHLDTRA AVETDIDN
//
