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Database: UniProt
Entry: A0A151W449_HYPMA
LinkDB: A0A151W449_HYPMA
Original site: A0A151W449_HYPMA 
ID   A0A151W449_HYPMA        Unreviewed;       473 AA.
AC   A0A151W449;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   07-JUN-2017, entry version 7.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KYQ42632.1};
GN   Name=dapA {ECO:0000313|EMBL:KYQ42632.1};
GN   ORFNames=Hypma_03737 {ECO:0000313|EMBL:KYQ42632.1};
OS   Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Lyophyllaceae;
OC   Hypsizygus.
OX   NCBI_TaxID=39966 {ECO:0000313|EMBL:KYQ42632.1, ECO:0000313|Proteomes:UP000076154};
RN   [1] {ECO:0000313|EMBL:KYQ42632.1, ECO:0000313|Proteomes:UP000076154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=51987-8 {ECO:0000313|EMBL:KYQ42632.1,
RC   ECO:0000313|Proteomes:UP000076154};
RA   Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT   "Whole genome sequencing of Hypsizygus marmoreus 51987-8.";
RL   Submitted (MAR-2016) 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:KYQ42632.1}.
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DR   EMBL; LUEZ01000006; KYQ42632.1; -; Genomic_DNA.
DR   EnsemblFungi; KYQ42632; KYQ42632; Hypma_03737.
DR   Proteomes; UP000076154; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblFungi.
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:KYQ42632.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076154};
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:UP000076154};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   473 AA;  51383 MW;  F9D5AE4B794BC144 CRC64;
     MMLYPNGPEA AVRFLKFVNA SPTPFHAVDN AAARLEKAGF QKLREKDDWE KDVKAGGKYY
     FTRNQAALVA FTIPAEWKHG AGLSIVATHV DSPNLKVRPI SKRTTSGYLQ VGVETYGGGI
     WHSWLDRDLS LAGRAVIAEQ GGGFRSKLIK IDRPLLRIPT LAIHLDRNVN DSFKFNQETE
     FVPILGLIES QLNSPKDGAN GKEEKPDTAK ASSIQANHHS ELLALLASEL SVAPEEIHDF
     ELSLFDTQPS TLGGINGEFI FSPRMDNLVL SFCAVEAIAE SASAQTFPGL EGNVNCIALF
     NHEEIGSVST SGAESSLIPS LLNRLSPTPA SLAQSISRSF LISADMGHAL HPNYTSKFED
     QHKPVMNGGI VIKTNAKQRY ASDAITSFIV KQLVERKGGK VQEFEVRNDM ACGSTVGPML
     SKIGIRTVDV GNAMLSMHSI RETAGSHDVQ NAIDLFTSFF EGFAVLDKGL TVD
//
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