ID M0MB31_HALMO Unreviewed; 349 AA.
AC M0MB31;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Subtilisin-like serine protease {ECO:0000313|EMBL:EMA42961.1};
GN ORFNames=C448_09992 {ECO:0000313|EMBL:EMA42961.1};
OS Halococcus morrhuae DSM 1307.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=931277 {ECO:0000313|EMBL:EMA42961.1, ECO:0000313|Proteomes:UP000011568};
RN [1] {ECO:0000313|EMBL:EMA42961.1, ECO:0000313|Proteomes:UP000011568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1307 {ECO:0000313|EMBL:EMA42961.1,
RC ECO:0000313|Proteomes:UP000011568};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA42961.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOMC01000123; EMA42961.1; -; Genomic_DNA.
DR RefSeq; WP_004054321.1; NZ_AOMC01000123.1.
DR AlphaFoldDB; M0MB31; -.
DR STRING; 931277.C448_09992; -.
DR PATRIC; fig|931277.6.peg.1950; -.
DR eggNOG; arCOG00702; Archaea.
DR OrthoDB; 27270at2157; -.
DR Proteomes; UP000011568; 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; 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:UP000011568};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 96..318
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 327..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 293
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 349 AA; 37175 MW; E44FDB7E6FBFEB50 CRC64;
MNDRIVFTRE PAAFLREMEC NVVETYDFGT SGAAYIECEA DHESTIADDD RVLDLEPNMT
VEPDLEPAAV SEDPAAVATI EDVRELHDVP TDDATGEGLT VVAMDSGIDP EHPVFEDKSI
EQVDVTGSGE GDAVGHGTAV LGQITRLAPD ASLVALRIFG EEGQTKNNVI MRAYEWLHTN
VEEYDVVNMS WGSSETSNAI NRTHDELVEK GIRDVVSAGN SGEKSGSPAT AERAFSIAAC
TEDGAIAEFS SYNPDRDNPD VAAIGKDNRL AQASGTAMGT ELDGPWVKAS GTSFSSPEVA
GMVAKYLTVD PETAPEPIMR EFEAAARDIP EQPRDGAGLA DYAATVNGE
//
