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Database: UniProt
Entry: A0A2D3VM70_9PEZI
LinkDB: A0A2D3VM70_9PEZI
Original site: A0A2D3VM70_9PEZI 
ID   A0A2D3VM70_9PEZI        Unreviewed;       506 AA.
AC   A0A2D3VM70;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   10-APR-2019, entry version 7.
DE   SubName: Full=Probable Alkaline protease 2 {ECO:0000313|EMBL:CZT24889.1};
GN   ORFNames=RCC_10617 {ECO:0000313|EMBL:CZT24889.1};
OS   Ramularia collo-cygni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Ramularia.
OX   NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT24889.1, ECO:0000313|Proteomes:UP000225277};
RN   [1] {ECO:0000313|EMBL:CZT24889.1, ECO:0000313|Proteomes:UP000225277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URUG2 {ECO:0000313|EMBL:CZT24889.1,
RC   ECO:0000313|Proteomes:UP000225277};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|SAAS:SAAS01077246}.
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DR   EMBL; FJUY01000023; CZT24889.1; -; Genomic_DNA.
DR   OrthoDB; 921536at2759; -.
DR   Proteomes; UP000225277; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd04077; Peptidases_S8_PCSK9_Proteinase; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000225277};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01077244};
KW   Protease {ECO:0000256|SAAS:SAAS01099369, ECO:0000313|EMBL:CZT24889.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225277};
KW   Serine protease {ECO:0000256|SAAS:SAAS01099373};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     15       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        16    506       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5013756891.
FT   DOMAIN       42    135       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      175    421       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
SQ   SEQUENCE   506 AA;  54102 MW;  6DA54188E933AA11 CRC64;
     MKSFLGLTLP LLAAASPVMV ESIHNEAAPV ISSVNAKEIP DSYMIKFKSH VNSNSAAEHH
     DWVTDLHATT QKAKTDLKKR SQTPMVDDIF HGLKHTYNIA GSLMGYSGHF DEDTIEQIRR
     HPDVELIERD QEVHTLGSDD HETEKNSPWG LARISHRDSL SFGTFNKYLY TADGGEGVDV
     YVIDTGTNVE HVDFEGRAAW GKTIPQGDAD EDGNGHGTHC SGTVAGKKYG VAKKAHVKAV
     KVLRSNGSGX MSDVVKGVEY AATSHTSEVK KAKDGKRKGF KGSAANMSLG GGKSALLDQA
     VNAAVDAGIH FAVAAGNDNA DSCNYSPAAA ENAVTVGAST LADERAYFSN FGKCNDIFAP
     GLNIQSTWIG SKYAINTISG TSMASPHIAG LLAYLLSLQP AKSSAYAVAD ITPKKLKSHL
     LAISTVGALS DVPSNTENLL AWNGGGSSNF TDIVHKGGYK ATHADLPEKL SEKVSEKVDD
     FAQKIEDFEH KMEXDLKDFI SSLKSE
//
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