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Database: UniProt
Entry: A0A0G2HV34_9PEZI
LinkDB: A0A0G2HV34_9PEZI
Original site: A0A0G2HV34_9PEZI 
ID   A0A0G2HV34_9PEZI        Unreviewed;       479 AA.
AC   A0A0G2HV34;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   SubName: Full=Putative aspartyl aminopeptidase {ECO:0000313|EMBL:KKY38638.1};
GN   ORFNames=UCDDA912_g01331 {ECO:0000313|EMBL:KKY38638.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Diaporthales; Diaporthaceae;
OC   Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY38638.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY38638.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY38638.1};
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:KKY38638.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY38638.1};
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:KKY38638.1}.
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DR   EMBL; LCUC01000052; KKY38638.1; -; Genomic_DNA.
DR   EnsemblFungi; KKY38638; KKY38638; UCDDA912_g01331.
DR   Proteomes; UP000034680; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF02127; Peptidase_M18; 2.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KKY38638.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034680};
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:UP000034680};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   479 AA;  52224 MW;  ED6C619B852F8127 CRC64;
     MAPPKSAQEF VDFVNASPTP YHAVASSVKL LEAAGFKGIK ERDNWSSDLQ PGGKYYLTRN
     GSSIVAFAIG KKWAPGISKK TNAGFLQVGV ETYGGGIWHS WFDRDLSVAG RVLVKDSSGN
     FVQKLIKVDK PILRIPTLAI HLDRSANFDP NKETELFPIC GLAAAELNRT GVSEKEAKEE
     GPAEAEGGGE FQPLKAMTQR HHPYLLEIIA QHAGVETDGV IDFELVLYDT QKSCFGGLND
     EFIFSPRLDN LGMTYCSVLG LIESVKLRGA LDSESSIRLI TCFDHEEIGS TSAHGANSNL
     LPAVLRRLSV LPRGNFSESA SEKSYEQVNP DNIATAFEQT LSTSFFVSAD MAHSVNPNYQ
     QKYESNHQPE MNKGTVIKIN ANQRYATNSP GIVLLQEVAK KAGVPLQLFV VRNDSSCGST
     IGPMLSAKMG VRTLDLGNPQ LSMHSIRETG GTYDVEHGIK LFESFLSNYT ALESKILVD
//
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