ID A0A1M7TD81_FERGO Unreviewed; 683 AA.
AC A0A1M7TD81;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Serine protease, subtilisin family {ECO:0000313|EMBL:SHN68627.1};
GN ORFNames=SAMN02745226_01855 {ECO:0000313|EMBL:SHN68627.1};
OS Fervidobacterium gondwanense DSM 13020.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=1121883 {ECO:0000313|EMBL:SHN68627.1, ECO:0000313|Proteomes:UP000184207};
RN [1] {ECO:0000313|EMBL:SHN68627.1, ECO:0000313|Proteomes:UP000184207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13020 {ECO:0000313|EMBL:SHN68627.1,
RC ECO:0000313|Proteomes:UP000184207};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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 ECO:0000256|RuleBase:RU003355}.
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DR EMBL; FRDJ01000014; SHN68627.1; -; Genomic_DNA.
DR RefSeq; WP_072760817.1; NZ_FRDJ01000014.1.
DR AlphaFoldDB; A0A1M7TD81; -.
DR STRING; 1121883.SAMN02745226_01855; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000184207; 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; 2.60.40.1800; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
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 InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
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 192..462
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 239
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 414
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 683 AA; 75003 MW; A7FC863F4D2F9B51 CRC64;
MKSKLLLSNK KYTFNLKSLL WKSKLVFVFL IIGLVISIAT SCTNSRSGRI DNGSTSDLSE
NLSLTNDDYF PDRVLVGYED EDDLDKIAEL IEGRLLLNIP QIRVASFKVE KVEKVLQIFQ
DEESIQKVKI RYAEPVYKRS IIPYSVGQGY SNQKVVLNYT IYENYTSESL DFYLWGLRAI
DVKKVWNDGY DGTGIIVAVL DTGVDGTHPD LQGQVTRGYR PIINQEIPEG TDSSYGGSHG
THVAGTIAAK KDGKGLVGVA PRVKIMPVVL FDIGGWYVGD DYAAKGIIWA VDHGAKVLSN
SWGGAGYSQT LKDAFDYALA HGVVVVAAAG NSKSSQSFQY PANYPGVIQV GAVEYLGNKY
DIADFSSGSP MLSVSAPGVN IISTMPQKTS VGYDKRSFQI AENSGYYGFM SGTSMATPHV
SGFVALLLQE YPNAKPWQIR RLLENGAIDI GEPGIDERSG YGMINQRSVS SELPDNGGLN
LDVEVTDAYG DWKIPSVSVS LIGTSNTDRR VRYFSKTNGD GVAKFLNIDT GKYDVIISGP
DSRENSEGLS NVVYRKAEER VYYANRSFTN DSSITFNFSS QARIKFKNVS GNEFLILQSK
DGSTSTTIEL LSNQIDISHL SGRYFIKFGY PSPVLHNTTV NATITLNGYD IRLSGYITAG
STLTTLYDAY GRNSHWTFFG KTE
//