(data stored in SCRATCH zone)

SWISSPROT: Q6FK02_CANGA

ID   Q6FK02_CANGA            Unreviewed;       415 AA.
AC   Q6FK02;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 90.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62418.1};
GN   Name=PEP4 {ECO:0000313|CGD:CAL0137063};
GN   OrderedLocusNames=CAGL0M02211g {ECO:0000313|CGD:CAL0137063,
GN   ECO:0000313|EMBL:CAG62418.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62418.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01103,
CC       ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00692226}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01103}.
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DR   EMBL; CR380959; CAG62418.1; -; Genomic_DNA.
DR   RefSeq; XP_449442.1; XM_449442.1.
DR   ProteinModelPortal; Q6FK02; -.
DR   STRING; 284593.XP_449442.1; -.
DR   MEROPS; A01.018; -.
DR   EnsemblFungi; CAG62418; CAG62418; CAGL0M02211g.
DR   KEGG; cgr:CAGL0M02211g; -.
DR   CGD; CAL0137063; PEP4.
DR   EuPathDB; FungiDB:CAGL0M02211g; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   eggNOG; ENOG410XNV7; LUCA.
DR   HOGENOM; HOG000197681; -.
DR   InParanoid; Q6FK02; -.
DR   KO; K01381; -.
DR   OMA; WNGQYTV; -.
DR   OrthoDB; EOG092C33N0; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0043234; C:protein complex; IEA:EnsemblFungi.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0097718; F:disordered domain specific binding; IEA:EnsemblFungi.
DR   GO; GO:0070492; F:oligosaccharide binding; IEA:EnsemblFungi.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblFungi.
DR   GO; GO:0032258; P:CVT pathway; IEA:EnsemblFungi.
DR   GO; GO:0016237; P:lysosomal microautophagy; IEA:EnsemblFungi.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:EnsemblFungi.
DR   CDD; cd05488; Proteinase_A_fungi; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom.
DR   InterPro; IPR033819; Saccharopepsin.
DR   PANTHER; PTHR13683; PTHR13683; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FK02.
DR   SWISS-2DPAGE; Q6FK02.
KW   Aspartyl protease {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629219};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629231};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01103,
KW   ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS00629201};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    415       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004274031.
FT   DOMAIN       91    409       Peptidase A1. {ECO:0000259|PROSITE:
FT                                PS51767}.
FT   ACT_SITE    109    109       {ECO:0000256|PROSITE-ProRule:PRU01103}.
FT   ACT_SITE    301    301       {ECO:0000256|PROSITE-ProRule:PRU01103}.
SQ   SEQUENCE   415 AA;  45378 MW;  97FE8960CDEA9851 CRC64;
     MRLSLSVLMP LALMLLGDYA DAKVFQAELK KEKLTKEMLE LGFEAHVQQL GHKYVSQYEK
     ANPGTVLPRD HLFYPDQVHN VPLSNYMDAQ YFADISLGTP PQKFKVILDT GSSNLWVPSV
     DCGSLACFLH NKYDHSQSST YIKDGRPLSI SYGSGSIEGY ISEDNLQIGD LTIQNQKFGE
     TTSEPGLAFA FGKFDGILGL AYDTIAQDDI TPPFYSAIQQ HLLDESKFSF YLKSVNDPAA
     EGGSASDGGV FTLGGVDSSK FKGDLIPLHV RRQAYWEVPL NAIKLGDQST GKLENTGAAI
     DTGTSLITLP SDMAEIINAQ IGAKKGWTGQ YTLECSTRAK LPDLTFTLDG HDFVLSPFEY
     TLEVSGSCIS VITPMDFPEP IGRMAILGDA FLRRYYSVFD LDANVVSLAE AVHSA
//

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