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Database: UniProt
Entry: A0A0D1ZE51_9EURO
LinkDB: A0A0D1ZE51_9EURO
Original site: A0A0D1ZE51_9EURO 
ID   A0A0D1ZE51_9EURO        Unreviewed;       512 AA.
AC   A0A0D1ZE51;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-NOV-2017, entry version 14.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIV92234.1};
GN   ORFNames=PV10_06692 {ECO:0000313|EMBL:KIV92234.1};
OS   Exophiala mesophila.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV92234.1, ECO:0000313|Proteomes:UP000054302};
RN   [1] {ECO:0000313|EMBL:KIV92234.1, ECO:0000313|Proteomes:UP000054302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV92234.1,
RC   ECO:0000313|Proteomes:UP000054302};
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 mesophila CBS40295.";
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; KN847523; KIV92234.1; -; Genomic_DNA.
DR   RefSeq; XP_016223808.1; XM_016371515.1.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; KIV92234; KIV92234; PV10_06692.
DR   GeneID; 27324537; -.
DR   Proteomes; UP000054302; 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:UP000054302};
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:UP000054302};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   512 AA;  55589 MW;  0A96E04165F8F80A CRC64;
     MVRKTSSGFF TSIHEDLPLH VARGYDRVYH QHSAYPQQVS RTRDEHPPVA PFSAEKYTQP
     YLDFMTNNPT IYHAVDAFTS DLAKAGYECL SERNLWKIKP GGKYYIKRNG SAFIAFAVGK
     DYKPGNGVGI VAGHIDALTA KLKPVPKLAT KAGFVQLGVA PYAGGLNFTW WDRDLGIGGR
     VLVKGKDGKI TEQLVKLNWP IARVPTLAPH FGAAAQGPFN PETNMVPIIG LDNSDITGKA
     HAPLNLPAGT FVAKQPERLV RAIAGELGIQ EYTDIVNWEL ELFDIQPAQL GGLDKEFIFA
     GRIDDKLCCF AAIQGLLASS DDDSPGIVKM VGCFDDEEIG SYLRQGARSN FMSSVIERIV
     ESSSDNYGPN LLSQTLANSF LVSSDVIHAV NPNFLGAYLE NHAPRLNIGV AVSADPNGHM
     TTDSVSTALL SRIAEKSGST LQVFQIRNDS RSGGTIGPMT SSKLGVRAID CGIPQLSMHS
     IRATTGSLDP GLGVQLYKGF FDHFQEVDQE FE
//
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