(data stored in ACNUC10043 zone)

SWISSPROT: Q18DQ8_HALWD

ID   Q18DQ8_HALWD            Unreviewed;       379 AA.
AC   Q18DQ8;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   SubName: Full=M50 family metalloprotease {ECO:0000313|EMBL:CAJ51231.1};
DE            EC=3.4.24.- {ECO:0000313|EMBL:CAJ51231.1};
GN   OrderedLocusNames=HQ_1101A {ECO:0000313|EMBL:CAJ51231.1};
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ51231.1, ECO:0000313|Proteomes:UP000001975};
RN   [1] {ECO:0000313|EMBL:CAJ51231.1, ECO:0000313|Proteomes:UP000001975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA   Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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DR   EMBL; AM180088; CAJ51231.1; -; Genomic_DNA.
DR   RefSeq; WP_011570397.1; NC_008212.1.
DR   STRING; 362976.HQ_1101A; -.
DR   MEROPS; M50.A04; -.
DR   EnsemblBacteria; CAJ51231; CAJ51231; HQ_1101A.
DR   GeneID; 4192078; -.
DR   KEGG; hwa:HQ_1101A; -.
DR   eggNOG; arCOG00609; Archaea.
DR   eggNOG; COG0750; LUCA.
DR   HOGENOM; HOG000149148; -.
DR   OMA; DGGHVLY; -.
DR   BioCyc; HWAL362976:G1G1J-113-MONOMER; -.
DR   Proteomes; UP000001975; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   InterPro; IPR008915; Peptidase_M50.
DR   Pfam; PF02163; Peptidase_M50; 2.
PE   4: Predicted;
DR   PRODOM; Q18DQ8.
DR   SWISS-2DPAGE; Q18DQ8.
KW   Hydrolase {ECO:0000313|EMBL:CAJ51231.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000313|EMBL:CAJ51231.1};
KW   Protease {ECO:0000313|EMBL:CAJ51231.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001975};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        324..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          127..217
FT                   /note="Peptidase_M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
FT   DOMAIN          256..294
FT                   /note="Peptidase_M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   379 AA;  40993 MW;  BD29E0763F1D406F CRC64;
     MESLDPAVDP PVDALQSVFH LYETQRDGDR ILYYGESLVP EQMLIREAWP AFREAGYEIE
     VASTETREDV VVARPIDTSI DGIPWKNMLL FLATIVSTLL VGAITWYYIP PSDLLANPLT
     ILQALPFTAA ILGVLATHEL GHYVMGRYHG VNVSLPYVIP FIFPFGTLGA IIRMRGQMPD
     RRALFDIGVA GPLAGLTATV IVTVIGLTQS PIQIPARAME QSGQMIIFNN PPLLDIIATV
     IGEPTAYNDP RMSVSPIIIG GWVGMFFTVL NLLPVGQLDG GHILRAMLGT TQERVAALVP
     VSLIALSAYL HYGLGYAFNE SVGLWAFWGV LSAFVAFKGP ANPIDDAPLG IPRVLLGVLT
     FALGALCFLL VPIEVATVS
//

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