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Database: UniProt
Entry: A0A072PSD5_9EURO
LinkDB: A0A072PSD5_9EURO
Original site: A0A072PSD5_9EURO 
ID   A0A072PSD5_9EURO        Unreviewed;       622 AA.
AC   A0A072PSD5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   16-JAN-2019, entry version 17.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KEF62238.1};
GN   ORFNames=A1O9_00210 {ECO:0000313|EMBL:KEF62238.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF62238.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF62238.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF62238.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) 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:KEF62238.1}.
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DR   EMBL; AMGV01000001; KEF62238.1; -; Genomic_DNA.
DR   RefSeq; XP_013264828.1; XM_013409374.1.
DR   EnsemblFungi; KEF62238; KEF62238; A1O9_00210.
DR   GeneID; 25275162; -.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000027920; 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; 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; 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:UP000027920};
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:UP000027920};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    622       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001681902.
FT   DOMAIN      235    621       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    317    317       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    321    321       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    538    538       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       580    580       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       581    581       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       599    599       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       601    601       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   622 AA;  67869 MW;  91B38E68CCA061DC CRC64;
     MAAAARISTA LVASLSLLSC FQTSLANPIT RRTAFAVKDF HPTPRAWTNL GAAPSDHLIS
     LSIGLSQGRF SELERHLYEV SDPFHPRYGQ HLSAEEVHDL VKPSDETSDA VHDWLEGHGV
     RAHHLKYSPA KDWLYVTLPL SMIEEMLDTE YSVYEHRDGS TLVRTEGYSL PLYLHEHIST
     IQPTNSWARL DGHKKRNEVK RRTTQAAVVS DDWSPAPLVP LPDNTTVAAV CNFTSVTPDC
     IRTLYGTLDY TPKSAGVNKM GHTNYLDEAT NRSDISIFLG KYRPEAQAYA YEFEVISIDG
     GVIDNGTNVS EEGLDREANL DAEYMIGVGY PTPLTAWHTG GRDPSFMPDI NTPDNSDEPF
     LVWANYVIAQ QDIPQVISTS YGDDEQTVSQ AYAQAVCNQF AQLGARGVSL FFSSGDYGVG
     ADDTCYSNVD NSTYMFMPSF PADCPYVTAV GATTGYPESA AWRKLRSGAY FTSGAGFSNY
     FPQPKYQADA VDGYVAGLNG LYDGFYNKTG RAYPDLSCIG QVFPTIWNGS TLGLVGTSGS
     SPICAAVFAL LNDALITEGR PPIGFLNPWL YAHGHKLFTD VTNGTSAGCN TSGFPATQGW
     DAVTGWGTPY FPSLLEGFGL KK
//
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