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Database: UniProt
Entry: W9YMU1_9EURO
LinkDB: W9YMU1_9EURO
Original site: W9YMU1_9EURO 
ID   W9YMU1_9EURO            Unreviewed;       507 AA.
AC   W9YMU1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EXJ93838.1};
GN   ORFNames=A1O1_02231 {ECO:0000313|EMBL:EXJ93838.1};
OS   Capronia coronata CBS 617.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ93838.1, ECO:0000313|Proteomes:UP000019484};
RN   [1] {ECO:0000313|EMBL:EXJ93838.1, ECO:0000313|Proteomes:UP000019484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ93838.1,
RC   ECO:0000313|Proteomes:UP000019484};
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 Capronia coronata CBS 617.96.";
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:EXJ93838.1}.
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DR   EMBL; AMWN01000002; EXJ93838.1; -; Genomic_DNA.
DR   RefSeq; XP_007721332.1; XM_007723142.1.
DR   EnsemblFungi; EXJ93838; EXJ93838; A1O1_02231.
DR   GeneID; 19157131; -.
DR   Proteomes; UP000019484; 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   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:UP000019484};
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:UP000019484};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   507 AA;  55078 MW;  5C145880A8988FB4 CRC64;
     MVRKTSSGFF TSIHEDLPLH VSRGYDRMVQ HTAYAPTPRD PIPQKTFSPE KYTQPYLDFM
     TNNPTIFHAV AAFTAQLEKA GYEYLSERTQ WKIQPGGKYY TKRNGSAFIA FAVGKDYKPG
     NGVGIVAGHI DALTAKLKPV PKLATKAGYI QLGVAPYAGG LNSTWWDRDL GIGGRVLVKT
     KDGKIEERLV KLDWPIARIP TLAPHFGAAA QGPFNLETNM VPIIGLDNSD ITGQKQSTLN
     LPAGTFVSTQ PERLVRAIAG QLGVEDYTSI VNWELELFDI QPAQVGGLDK EFIFAGRIDD
     KLCCFAAIEA LLASSDDASP GIIKMVGCFD DEEIGSYLRQ GARSNFMSSV IERICEASSD
     HCGPNLISQT LANSFLVSSD VIHAVNPNFL GAYLENHSPR LNVGVTVSAD SNGHMTTDSV
     STALLSRVAE KCGSTLQVFQ IRNDSRSGGT IGPMTSSKLG CRAIDCGIPQ LSMHSIRATT
     GSLDPGLGVK LYKGFFDYFE QVDTEFQ
//
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