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Database: UniProt
Entry: A0A0D2CUI5_9EURO
LinkDB: A0A0D2CUI5_9EURO
Original site: A0A0D2CUI5_9EURO 
ID   A0A0D2CUI5_9EURO        Unreviewed;       507 AA.
AC   A0A0D2CUI5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW53747.1};
GN   ORFNames=PV05_06161 {ECO:0000313|EMBL:KIW53747.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW53747.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW53747.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW53747.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) 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; KN847320; KIW53747.1; -; Genomic_DNA.
DR   RefSeq; XP_013314331.1; XM_013458877.1.
DR   EnsemblFungi; KIW53747; KIW53747; PV05_06161.
DR   GeneID; 25328069; -.
DR   Proteomes; UP000054342; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000054342};
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:UP000054342};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   507 AA;  54928 MW;  55D115D3EB51D387 CRC64;
     MVRKTSSGFF TSIHEDLPLH VSRGYDRMVQ HTASTLASRP PSPQKRFSPE KYTQPYLDFM
     TNNPTIFHAV DAFTTQLEEA GYVYLSERTT WEIKPGGKYY TKRNGSAFIA FAVGKEYKAG
     NGMGIVAGHI DALTAKVKPV PKLPTKAGYV QLGVAPYAGG MNMTWWDRDL GIGGRVLVKG
     KDGKIKEELV KLDWPIARIP TLAPHFGAAA SGPFNLETNM VPIVGIDNSD LSGKQESSLN
     LPAGTFVASQ PERLVRAIAG KLGVEEYTSI VNWELELFDV QPAQLGGLDK EFIFAGRIDD
     KLCCFAAIEA LLASSDDASP GIVKMVGCFD DEEIGSYLRQ GARSNFMSSV IERIAENFSS
     SCGPNLVSQT LANSFLVSSD VIHAVNPNFL GAYLENHSPR LNVGVSVSAD SNGHMTTDSA
     STALLSRIAE KCGSTLQVFQ IRNDSRSGGT IGPMTSSKLG CRAIDCGIPQ LSMHSIRATT
     GSLDPGLGVK LYKGFFDYYE EVDKEFQ
//
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