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Database: UniProt
Entry: A0A072PQ16_9EURO
LinkDB: A0A072PQ16_9EURO
Original site: A0A072PQ16_9EURO 
ID   A0A072PQ16_9EURO        Unreviewed;       508 AA.
AC   A0A072PQ16;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   07-JUN-2017, entry version 12.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KEF61787.1};
GN   ORFNames=A1O9_03357 {ECO:0000313|EMBL:KEF61787.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF61787.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF61787.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF61787.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) 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:KEF61787.1}.
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DR   EMBL; AMGV01000002; KEF61787.1; -; Genomic_DNA.
DR   RefSeq; XP_013264377.1; XM_013408923.1.
DR   EnsemblFungi; KEF61787; KEF61787; A1O9_03357.
DR   GeneID; 25278293; -.
DR   Proteomes; UP000027920; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KEF61787.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000027920};
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:UP000027920};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   508 AA;  55604 MW;  8D6C7F5161B5340C CRC64;
     MAPVSIKVAA NDFLDFVNAS PTPFHAVKSV KERLSKVGFK EIKEKESWSS ALRPGGKYFL
     TRNGSTVVAF AIGKKWKPGN PISMIGAHTD SPCLRIKPVS KKQGDGFLQV GVETYGGGLW
     HTWFDRDLGL AGRVMVREKD GDVVQKLVHI DKPILRIPTL AVHLDRQETF SFNKETQLFP
     IAGLVSAELK RQDEKKSKVS SDEAEEENKP FTPLKALTSR HHPHIVELIA ADATVAPESV
     VDFELVLYDT QKAVLGGLSD EFIFSARLDN LNQTYCATMG LINSLRSSSA LDDETSIRLV
     ACFDHEEIGS MTAQGAFSVM LPAIIRRLSV LPSSIFAGEG SEESYDHAAE PEFSTAYEQS
     LSSSFLLSAD MAHSVNPNYG AKYESDHRPE MNQGPVIKIN ANARYATNSP GIVLLQEVAR
     KAAKIIDSDP EGVPLQLFVV RNDSSCGSTI GPMLSAHLGA RTLDLGNPQL SMHSCRETGG
     ADDVHHAIRL FSSFFQHYSS MEKTILVD
//
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