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Database: UniProt
Entry: A5DAE1_PICGU
LinkDB: A5DAE1_PICGU
Original site: A5DAE1_PICGU 
ID   A5DAE1_PICGU            Unreviewed;       538 AA.
AC   A5DAE1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 2.
DT   05-JUL-2017, entry version 52.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDK36148.2};
GN   ORFNames=PGUG_00246 {ECO:0000313|EMBL:EDK36148.2};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM
OS   1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK36148.2, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK36148.2, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
RA   Agrafioti I., Arnaud M.B., Bates S., Brown A.J., Brunke S.,
RA   Costanzo M.C., Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L.,
RA   Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R.,
RA   Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C.,
RA   Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.,
RA   Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.,
RA   Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M.,
RA   Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CH408155; EDK36148.2; -; Genomic_DNA.
DR   RefSeq; XP_001486869.1; XM_001486819.1.
DR   ProteinModelPortal; A5DAE1; -.
DR   STRING; 4929.A5DAE1; -.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EDK36148; EDK36148; PGUG_00246.
DR   GeneID; 5129325; -.
DR   KEGG; pgu:PGUG_00246; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   InParanoid; A5DAE1; -.
DR   KO; K01268; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   Complete proteome {ECO:0000313|Proteomes:UP000001997};
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:UP000001997};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   538 AA;  59032 MW;  182CA75967CD45FE CRC64;
     MWIRSATHAG VKRRTAPDNQ HKYISKMVTL QDRWERVDSW IGSAECSIQD MDDFDTETQD
     SSEAVFPLDE DDYYDAFCSE YMSFTNNNPT TCHAVQYMSE MLEARGFVYI PETRPIDEKT
     ARAIIKGGCF YTSRGGLSLV AFIIGGQWQP ENGIGAIGSH VDALTAKLKP CSIKPNVDGY
     QMLGVANYSG SLQKNWLDRD LGIGGGVIIK KNDKVSRKIV SSGSFPIARI PSLAEHFGAV
     ADGPYNKETQ MVPIIGYGEA KEASETEKSA PLYGKHPLPL LRYVATRAGC KLEEIVGVDL
     ELYDIQSACR GGLDNEFMFA PRIDDRLCSF AAINALLSSA SEIKNSTTLK QWNGLNMVLL
     ADNEEIGSGS RTGAKGKFLS TTLKRILSAR NLQLQHLSVT FANSLILSAD VTHALNPNFK
     SAYLDNHYPV PNKGLTIKMD ANGRVMTDSI GTAMMQKIAE KNNLQFQTFH VRNDMPSGST
     IGPILAVETG ARVVDVGLPQ LSMHSIRAMC GYKEAGLGIK AFEAFFRDRT TVARAVCI
//
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