(data stored in SCRATCH zone)

SWISSPROT: Q6FJR5_CANGA

ID   Q6FJR5_CANGA            Unreviewed;       601 AA.
AC   Q6FJR5;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 93.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62505.1};
GN   Name=YPS1 {ECO:0000313|CGD:CAL0136285};
GN   OrderedLocusNames=CAGL0M04191g {ECO:0000313|CGD:CAL0136285,
GN   ECO:0000313|EMBL:CAG62505.1};
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:CAG62505.1, 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR380959; CAG62505.1; -; Genomic_DNA.
DR   RefSeq; XP_449529.1; XM_449529.1.
DR   ProteinModelPortal; Q6FJR5; -.
DR   STRING; 284593.XP_449529.1; -.
DR   MEROPS; A01.030; -.
DR   EnsemblFungi; CAG62505; CAG62505; CAGL0M04191g.
DR   KEGG; cgr:CAGL0M04191g; -.
DR   CGD; CAL0136285; YPS1.
DR   EuPathDB; FungiDB:CAGL0M04191g; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   eggNOG; ENOG410XNV7; LUCA.
DR   HOGENOM; HOG000248646; -.
DR   InParanoid; Q6FJR5; -.
DR   KO; K06009; -.
DR   OMA; LWITGSD; -.
DR   OrthoDB; EOG092C3KPP; -.
DR   PMAP-CutDB; Q6FJR5; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR   CDD; cd05474; SAP_like; 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; IPR033876; SAP-like.
DR   PANTHER; PTHR13683; PTHR13683; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 2.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJR5.
DR   SWISS-2DPAGE; Q6FJR5.
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}.
FT   DOMAIN       73    483       Peptidase A1. {ECO:0000259|PROSITE:
FT                                PS51767}.
FT   ACT_SITE     91     91       {ECO:0000256|PROSITE-ProRule:PRU01103}.
FT   ACT_SITE    378    378       {ECO:0000256|PROSITE-ProRule:PRU01103}.
SQ   SEQUENCE   601 AA;  63789 MW;  146156E87F7A086C CRC64;
     MKFSSLCMLA SVAAHSKAAK NVADLSYVKL DFDKYYGETF ETAKRGRSQA DIRVNKRANG
     YEEVQITNQN SFYSVTLEVG TPPQSVVVLV DTGSSDLWIT GSDNPYCRGS TGTSGKNMLL
     EAELKRALED ARDIAKERTT LAPRDDEHND GLLSWLTGSD GLLGGQGGTT ITLTDSAQPT
     AAGTSNGARA TINCAKYGTF DTSKSSTWHS NDTAFMIQYG DSTFASGTWG MDNLHLSDLN
     VTGLSFAVAN RTNSTVGVLG IGLPALEVTY SGRTAVSGQR PYQYDNFPLV LLRNGAIKSN
     SYSLFLNNAS AETGSVLFGA VDHSKYLGDL YTIPMVNTYA SQGYKNPIQF EVTLNGLGIS
     SSSDNTTITT TKIPALLDSG TTLTYLPQAL VTRIVQKLQA TYSNRAGYYV FSCPSQSDDT
     EVVFDFGGFH INAPITNFII GSSGDSCILG IMPQSGGGII LGDSFLNSAY VVYDLENYEI
     SMAQANYAGG QEDIEVISSS VPGAVRAPGF SSTWSTLATS FNTQGDIFTV QAAATVSGSA
     TNTGTGRATA TGNSNSTRST TSRSRTSATS TRSDSQKKND ASRTSFTSTL LFVAGLLVSF
     I
//

If you have problems or comments...

PBIL Back to PBIL home page