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Database: UniProt
Entry: A0A0G2H7I4_9PEZI
LinkDB: A0A0G2H7I4_9PEZI
Original site: A0A0G2H7I4_9PEZI 
ID   A0A0G2H7I4_9PEZI        Unreviewed;       615 AA.
AC   A0A0G2H7I4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-MAY-2019, entry version 15.
DE   SubName: Full=Putative tripeptidyl-peptidase 1 {ECO:0000313|EMBL:KKY24640.1};
GN   ORFNames=UCDDS831_g02258 {ECO:0000313|EMBL:KKY24640.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetes incertae sedis; Botryosphaeriales;
OC   Botryosphaeriaceae; Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY24640.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY24640.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY24640.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY24640.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY24640.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell
RT   wall degradation and secondary metabolism in the genomes of grapevine
RT   trunk pathogens.";
RL   Submitted (MAY-2015) 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:KKY24640.1}.
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DR   EMBL; LAQI01000056; KKY24640.1; -; Genomic_DNA.
DR   EnsemblFungi; KKY24640; KKY24640; UCDDS831_g02258.
DR   Proteomes; UP000034182; 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:UP000034182};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17    615       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002544961.
FT   DOMAIN      225    615       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    310    310       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    314    314       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    533    533       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       575    575       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       576    576       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       594    594       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       596    596       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   615 AA;  65873 MW;  54E5CFE8209BEB05 CRC64;
     MLGSHLLVLL AAAASASPLR ARSEYQVKEH FNVPRSWSRV GRAPSEHVVN LQIGLKQARF
     AELERHLYEV SDPRHERYGQ HLTADDVNDL VTPADGTLDL VHEWLEDNGI AKSHLEYSPA
     KDWIKVSLPV DHVEALLDTE YSVYQHATGG HIVRTPSWSL PRHLHDHVET IQPTNSFFRA
     APRRSNARPI IEDILQPLAH EKFISNQASS DAGAFDVSTV CNTTFVTPQC LRTYYGTVDY
     VPQVPGKNKI GLANYLNETS KRTDVKLFLQ QFRPDAASAA NNFTIEVING GDNTQTPNTA
     EQNADGKNME GNLDAETILG IGYPTPLIAY NTGGSPPFQP DANTDTNTNE PYLDWVQHVL
     GQSDVPQVVS TSYGDDEQTV PPSYAHTVCN MFAQLGARGV SLLFASGDAG VGDEGACISN
     NGTDAATFLP SFPDGCPYVT SVGATTGFSP ETAAYDVLGS GSVFTSGGGF SNYFAQPSYQ
     AEAVQNYSVA SLADGAYAGL YNASGRAYPD IAAQGQKFVV TWEGSNIRLD GTSASTPLAS
     AIISLVNDAL IAAGKSPLGF LNPWLYQGGW KAFNDVTNGS AAGCGVEGFV AAEGWDPVTG
     FGTPNFPAIL ESLGL
//
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