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Database: UniProt
Entry: A0A0G2HIA7_9PEZI
LinkDB: A0A0G2HIA7_9PEZI
Original site: A0A0G2HIA7_9PEZI 
ID   A0A0G2HIA7_9PEZI        Unreviewed;       573 AA.
AC   A0A0G2HIA7;
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:KKY28125.1};
GN   ORFNames=UCDDS831_g00490 {ECO:0000313|EMBL:KKY28125.1};
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:KKY28125.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY28125.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY28125.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY28125.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY28125.1};
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   -!- 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:KKY28125.1}.
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DR   EMBL; LAQI01000012; KKY28125.1; -; Genomic_DNA.
DR   EnsemblFungi; KKY28125; KKY28125; UCDDS831_g00490.
DR   Proteomes; UP000034182; 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   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:KKY28125.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034182};
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:UP000034182};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   573 AA;  61546 MW;  2A13611026032741 CRC64;
     MTKNPPTLRQ KQPKFPSSHS MQPPAASTTS SWEPAEHRAW PANGAFLEPT QGDTLFGSSL
     FSGNVAPAVP PKVPETPRPA VATPKHQTAS ARRQLKPQDY TKPFCDFLTE NPTVFHAVEA
     VAQDLKAQGY KKLSERDVWK LDAGGKYFVE RNGSSLIAFA VGEAYEPGNG AAILAGHIDA
     LTAKLKPIPK LRTKAGYEQL GVAPYAGALN STWWDRDLGI GGRVLVKEES GKIASKLVKL
     DWPIARIPTL APHFGAAAQG PFNKETQMVP IIGLDNSDIL GQQKNEDDAE FKPALLGGEG
     TFTSTQPERL VKVIAKELGI TDYSTIVNWE LELFDTQPAQ VGGIDKEFIF AGRVDDKLCS
     WAAVQALLNS SSAETSATDT SSSSILKVVG LFDDEEIGSL LRQGARGNFL PSVINRVVDS
     FAGFPTPTLL SQTFANSFIV SSDVIHAVNP NFLNAYLENH SPRLNVGLVV SADSNGHMTT
     DAVSTALLQR VADKAGQRLQ VFQIRNDSRS GGTVGPMMSA ATGIRAIDAG IPQLSMHSIR
     ATTGSLDPGL GVAIFQGFLD HYEAVDQEFR DTV
//
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