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Database: UniProt
Entry: A0A0G2DZH1_9EURO
LinkDB: A0A0G2DZH1_9EURO
Original site: A0A0G2DZH1_9EURO 
ID   A0A0G2DZH1_9EURO        Unreviewed;       519 AA.
AC   A0A0G2DZH1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-NOV-2017, entry version 10.
DE   SubName: Full=Putative vacuolar aspartyl aminopeptidase {ECO:0000313|EMBL:KKY16247.1};
GN   ORFNames=UCRPC4_g05973 {ECO:0000313|EMBL:KKY16247.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales;
OC   Phaeomoniellales incertae sedis; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY16247.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY16247.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY16247.1};
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.
RN   [2] {ECO:0000313|EMBL:KKY16247.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY16247.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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:KKY16247.1}.
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DR   EMBL; LCWF01000164; KKY16247.1; -; Genomic_DNA.
DR   EnsemblFungi; KKY16247; KKY16247; UCRPC4_g05973.
DR   Proteomes; UP000053317; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KKY16247.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053317};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   519 AA;  55973 MW;  CE10B5ED99ABDFA5 CRC64;
     MVRKTSSGLF ASTHDPSRES FFSNADSRRH ENINHLPSRS RPAPAREVRE RTFAPEDYTK
     PFLNFMTSNP TVFHAVAHFA KQLSGAGFEA LSERDLWTEK IQPGGKYYVT RNGSAFIAFS
     VGKDYQPGNG VGIVAGHIDA LTAKLKPVPK LPTKAGYVQL GVAPYAGALN STWWDRDLGI
     GGRVLVKDSK GKIETKLVKL DWPIARVPTL APHFGAAAQG PFNMETQVVP IIGLDNSDVL
     GTSSVSEEST KIPAGTFAAT QPERLVKAIA GEMGISDYSS IVNWELELFD TQPAQLGGLD
     KEFIFAGRID DKLCCYAAVE ALLASSDSTS SDIIKMTCCF DDEEIGSLLR QGARGNFLPS
     VLERICESLS TSCGPNLYSQ MLANSFLVSS DVIHAVNPNF LSAYLENHSP RLNVGIAVSA
     DPNGHMTTDS VSTAVLQRCA DKCGSKLQLF QIRNDSRSGG TIGPMTSSAL GIRAIDAGIP
     QLSMHSIRAT TGSLDPGLGV KIFKGFFDYY SEVDAEFVE
//
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