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Database: UniProt
Entry: A0A2H3EM51_9HELO
LinkDB: A0A2H3EM51_9HELO
Original site: A0A2H3EM51_9HELO 
ID   A0A2H3EM51_9HELO        Unreviewed;       656 AA.
AC   A0A2H3EM51;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   16-JAN-2019, entry version 5.
DE   SubName: Full=Alkaline serine protease {ECO:0000313|EMBL:PBP18115.1};
GN   ORFNames=BUE80_DR010990 {ECO:0000313|EMBL:PBP18115.1};
OS   Diplocarpon rosae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Diplocarpon.
OX   NCBI_TaxID=946125 {ECO:0000313|EMBL:PBP18115.1, ECO:0000313|Proteomes:UP000218527};
RN   [1] {ECO:0000313|EMBL:PBP18115.1, ECO:0000313|Proteomes:UP000218527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DortE4 {ECO:0000313|EMBL:PBP18115.1,
RC   ECO:0000313|Proteomes:UP000218527};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PBP18115.1, ECO:0000313|Proteomes:UP000218527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DortE4 {ECO:0000313|EMBL:PBP18115.1,
RC   ECO:0000313|Proteomes:UP000218527};
RA   Klein E., Featherston J., Rees J., Debener T.;
RT   "A draft genome sequence of the rose black spot fungus Diplocarpon
RT   rosae reveals a high degree of genome duplication.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PBP18115.1}.
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DR   EMBL; MVNX01000160; PBP18115.1; -; Genomic_DNA.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000218527; 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   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000218527};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW   ECO:0000313|EMBL:PBP18115.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218527};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   DOMAIN      239    656       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    319    319       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    323    323       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    574    574       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       615    615       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       616    616       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       634    634       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       636    636       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   656 AA;  71267 MW;  9810E8BEE12F5020 CRC64;
     MRLSSLVVVM TGGLAVEMIH GLMASPLSHS RPTQRAVPPS HSLHERHLPS WENQWTRKLK
     VPDTQILPMR IGLKQSNLGA GHDKLMAMST PGHESYGKHM TPVEIIEFFA PHHSSTDAVS
     AWLESSGISS HRFAASSNRQ WIQFDATAAE VEALLFADFY VREHSSGVHD ISTQEYHVPA
     HVREHVDYVT PGTRLRERKI KASRGDELSK RFESTVGARP LITQLPGFPN PNTSVCDVYV
     TAECTKVQYE LPDATKASPG NKLGIFQSLD VHYSRADLDV YYSTLYPHIP NGTYPEERLI
     DGAIDATEET AEFVPIHLES GLDFDSASPL IYPQGLVLFQ EDDEYYESTG SFNGFWNTFL
     DALDGSYCTS SASGETGDCT VEACLDPVYP DPDPGGYKGQ LQCGVYQPTN VISISYGVTE
     AALPDSYLKR QCNEWMKLAL QGVTVVMSSG DSGVGGGTCN GDSGKIFDPV FASTCPYILS
     VGSTEGDRFS RAQAPIPGAK LHELPRAAVQ AYWDQEQSGL GFTGYHHFVE NGDFRSVTRG
     VYHHGGRGYP DVAAVGDRQV VYSNGSWWLV GGTSLSAPVW GAVLTLVNEE RLAAGKSTVG
     FIHPILYQHP EAFTDVTVGS NPGCGGVGFP AAEGWDPVTG LGSPIFPVLL QVLMGI
//
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