ID   M0NDC4_9EURY            Unreviewed;       395 AA.
AC   M0NDC4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Periplasmic serine proteinase {ECO:0000313|EMBL:EMA55079.1};
GN   ORFNames=C450_03392 {ECO:0000313|EMBL:EMA55079.1};
OS   Halococcus salifodinae DSM 8989.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1227456 {ECO:0000313|EMBL:EMA55079.1, ECO:0000313|Proteomes:UP000011625};
RN   [1] {ECO:0000313|EMBL:EMA55079.1, ECO:0000313|Proteomes:UP000011625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8989 {ECO:0000313|EMBL:EMA55079.1,
RC   ECO:0000313|Proteomes:UP000011625};
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   -!- 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:EMA55079.1}.
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DR   EMBL; AOME01000015; EMA55079.1; -; Genomic_DNA.
DR   RefSeq; WP_005039999.1; NZ_AOME01000015.1.
DR   AlphaFoldDB; M0NDC4; -.
DR   STRING; 1227456.C450_03392; -.
DR   PATRIC; fig|1227456.3.peg.706; -.
DR   OrthoDB; 350578at2157; -.
DR   Proteomes; UP000011625; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
FT   DOMAIN          286..369
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   REGION          34..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   395 AA;  39673 MW;  0D2DEA2CA1C5C8C6 CRC64;
     MDDARTTRRA YLGALGTALA AGLAGCGGAL GDQTTTNSTT ASSTTRSTPA ETTADGPANA
     TAATADANAT GDTATATDGN ATAGDTPSPY TRVYRQTVGS VVLVSVTGGI GGGGQGSGFV
     FRNGYVVTNA HVVSNASTVE VRFSEGEWRS ASVVGTDPSS DLAVLDVRTP PDHATPLPLV
     EDQPAIGTEV VAIGNPYGLE GSVTSGLVSG VNRSIPAPNG YTIPDGIQTG APVNPGNSGG
     PLVNLDGEVV GVINSGGGDN LAFAISAALV DRVVPALIQN GEYDHAYMGV RLEPVTPRTA
     EQVGLDRPRG VVITRDPSGD GPSAGVLRRG DVIVGLGGQR IDTLQGLSSY LALQASPGDT
     IDVTVLRNGE RRTLSLTLGS RPEQPGAATQ STTTP
//