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Database: UniProt
Entry: A0A0M8MXJ5_9HYPO
LinkDB: A0A0M8MXJ5_9HYPO
Original site: A0A0M8MXJ5_9HYPO 
ID   A0A0M8MXJ5_9HYPO        Unreviewed;       553 AA.
AC   A0A0M8MXJ5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   SubName: Full=Vacuolar aminopeptidase 1 {ECO:0000313|EMBL:KOS18857.1};
GN   ORFNames=ESCO_000672 {ECO:0000313|EMBL:KOS18857.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS18857.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS18857.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease
RT   agent of ant agriculture.";
RL   Submitted (JUL-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:KOS18857.1}.
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DR   EMBL; LGSR01000020; KOS18857.1; -; Genomic_DNA.
DR   EnsemblFungi; KOS18857; KOS18857; ESCO_000672.
DR   Proteomes; UP000053831; 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:KOS18857.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053831};
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:UP000053831};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   553 AA;  59744 MW;  05266C02516A6991 CRC64;
     MTRIISGHMS AQRSVVSLRQ HASSRPASRS PPPLDPPTAS QMGPQTTSAQ PSSKFFVLAD
     MEGRAPRDNR ACPSCIAKLS PVEIGQVNWH LDEENPCKLC QFAAVKPEAF TKPFCDFLHE
     NPTVFHTLPP RDSWAGKIKA GGKYWLSRNG SSLIAFAVGK SYRTGNGISM IAGHIDALTA
     RLKPISTKPN RAGYVELGVA PYAGALSPTW WDRDLSIGGR VIVRDPHTGK TKSKLVKIDW
     PIAKIPTLAP HFGVGMMGSN NAETQAVPVI GLESPEDAAN ATPLAAPGSF VNTQPPRLVK
     LIAKQLSIAN LDSIVNWELE LFDSQPATTF GLDKELITAG RIDDKLCSWS ALMGLLASDD
     REDDGYIRLA AFFDDEEIGS LLRQGARGNF LPSTIERLLE SLNPQTYGPG LFGQTMAKSF
     LLSADVSHAG NPNFLAEYMP EHIPRLNVGL VLCEDSNGHM TTDAVSSTIM HRVAELSGSV
     LQDFQIRNDS RSGGTVGPML SSALGVRAAD AGLPQLSMHS IRATTGALDP GLGVKIFKGF
     YDHWEKIDNE WEA
//
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