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Database: UniProt
Entry: N1JJ05_BLUG1
LinkDB: N1JJ05_BLUG1
Original site: N1JJ05_BLUG1 
ID   N1JJ05_BLUG1            Unreviewed;       594 AA.
AC   N1JJ05;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   10-APR-2019, entry version 22.
DE   SubName: Full=Tripeptidyl-peptidase 1 {ECO:0000313|EMBL:CCU82207.1};
GN   ORFNames=BGHDH14_bgh03052 {ECO:0000313|EMBL:CCU82207.1};
OS   Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS   (Oidium monilioides f. sp. hordei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria.
OX   NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU82207.1, ECO:0000313|Proteomes:UP000015441};
RN   [1] {ECO:0000313|EMBL:CCU82207.1, ECO:0000313|Proteomes:UP000015441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DH14 {ECO:0000313|EMBL:CCU82207.1};
RX   PubMed=21148392; DOI=10.1126/science.1194573;
RA   Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M.,
RA   Stueber K., Ver Loren van Themaat E., Brown J.K.M., Butcher S.A.,
RA   Gurr S.J., Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J.,
RA   Ahmadinejad N., Ametz C., Barton G.R., Benjdia M., Bidzinski P.,
RA   Bindschedler L.V., Both M., Brewer M.T., Cadle-Davidson L.,
RA   Cadle-Davidson M.M., Collemare J., Cramer R., Frenkel O., Godfrey D.,
RA   Harriman J., Hoede C., King B.C., Klages S., Kleemann J., Knoll D.,
RA   Koti P.S., Kreplak J., Lopez-Ruiz F.J., Lu X., Maekawa T., Mahanil S.,
RA   Micali C., Milgroom M.G., Montana G., Noir S., O'Connell R.J.,
RA   Oberhaensli S., Parlange F., Pedersen C., Quesneville H.,
RA   Reinhardt R., Rott M., Sacristan S., Schmidt S.M., Schoen M.,
RA   Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA   Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T.,
RA   Panstruga R.;
RT   "Genome expansion and gene loss in powdery mildew fungi reveal
RT   tradeoffs in extreme parasitism.";
RL   Science 330:1543-1546(2010).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCU82207.1}.
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DR   EMBL; CAUH01006005; CCU82207.1; -; Genomic_DNA.
DR   STRING; 34373.CCU82207; -.
DR   MEROPS; S53.010; -.
DR   EnsemblFungi; BLGH_04817-mRNA-1; BLGH_04817-mRNA-1; BLGH_04817.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000015441; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   Gene3D; 3.40.50.200; -; 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; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000015441};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015441};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    594       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004107260.
FT   DOMAIN      222    593       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    302    302       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    306    306       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    507    507       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       549    549       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       550    550       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       571    571       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       573    573       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   594 AA;  65008 MW;  9DC8D03A1CE23CE3 CRC64;
     MELATAAVIL FFATACLGAY PQGQVDNCIS FGDYQVYEQL PVAPSPWTPR KIDHINQDQS
     FKLRIHLKNI NTDSFHQKVF DMSTPSHPSY GQHMTRKEVN SYLAPSSLSF QLVRQWLEEQ
     NVGNITIEND WFVVESTVRR VERLLHTNFE VYENTLTGKS VLRTLSYSLP SSLRAHIDII
     APTIKFSTPA AYRSTLVDWP AEEIHEDNAS LDGGVAAACN SSITLECIKD LYNLRQFSGS
     NSSKNQFALA GFLEEYAQHD DLNRFLTQYE PDAVGNDFST VLVNNGSNTQ QNETDKSLNM
     GEANLDIQYA FLAYPTPAMY ISTGGRPPET SKYEVDNEPY LEFLTYLLGI DQPPQTISIS
     YGDSEWSVPD SYARTVCDLF SQLAARGVSV LVASGDSGSG SNCNETHPGS LYYTPSFPAS
     CPFVTSVGST YHISPEVAVA FSGGGFSDIF PRPAYQDQAV TTYLDNADPS FTPYFNTSGR
     AYPDIAAQGV NFHVFVRGNN VLESGTSAST PIMAAIIALL NGDRIERGAP PLGLLNPWLY
     ENGQAAFTDI VGGKGSGCPQ ISGSGFRAST GWDPVTGLGT PDFEKLREQS SNSI
//
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