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Database: UniProt
Entry: A0A0P1BHJ8_9BASI
LinkDB: A0A0P1BHJ8_9BASI
Original site: A0A0P1BHJ8_9BASI 
ID   A0A0P1BHJ8_9BASI        Unreviewed;       504 AA.
AC   A0A0P1BHJ8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:CEH15683.1};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH15683.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH15683.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CCYA01000272; CEH15683.1; -; Genomic_DNA.
DR   EnsemblFungi; CEH15683; CEH15683; CEH15683.
DR   Proteomes; UP000054845; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
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:CEH15683.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054845};
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:UP000054845};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   504 AA;  54957 MW;  85124706D0A5E2DA CRC64;
     MSPTPGSGYS LPSIVSSINS SLETSPAQAF LKYSDASPTP FHATAVSAAL LEKDGFVRLK
     EQDAWDGKIE AGGKYFFTRN QSAIVAFGVG KQFQPGVSGV HLVGAHTDSP NFHIKPVSKR
     TKEGYLQCGV ETYGGGLWST WFDRDLSLAG RVIVATTASQ NAFQSRLVKV DRTLLRIPTL
     AIHLNRSAND AFKFNQETEM VPILGLADKA KEALNAPATT DEDGITGEPR MQEKHHSMLL
     ELLAGELGVQ VEQIQDFELS LYDTQKATIG GLNDEFIHAA RLDNQMSCFC ATTALIEATR
     GGSLSNSSSI QAIALFDNEE VGSVSTHGAE SNMLSSTVRR LGSMSILGLE SIKNDDHLHP
     TNYERSISKS FLISSDMAHG FHPNYSSFYE DNHRPKINGG VVIKTNAKQR YASTAPTTFL
     IRRIAKLASV PLQEFEVRND MPCGSTIGPM MSKTGIRTVD LGSPQLSMHS IRETSGTKDV
     KYKIDLFAAF FRDFDKVDSE LVVD
//
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