(data stored in ACNUC8465 zone)

SWISSPROT: Q6FK43_CANGA

ID   Q6FK43_CANGA            Unreviewed;       390 AA.
AC   Q6FK43;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   10-APR-2019, entry version 77.
DE   RecName: Full=GPI-anchor transamidase {ECO:0000256|RuleBase:RU365060};
DE            Short=GPI transamidase {ECO:0000256|RuleBase:RU365060};
DE            EC=3.-.-.- {ECO:0000256|RuleBase:RU365060};
GN   OrderedLocusNames=CAGL0M01298g {ECO:0000313|CGD:CAL0136869,
GN   ECO:0000313|EMBL:CAG62377.1};
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:CAG62377.1, 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   -!- FUNCTION: Mediates GPI anchoring in the endoplasmic reticulum, by
CC       replacing a protein's C-terminal GPI attachment signal peptide
CC       with a pre-assembled GPI. During this transamidation reaction, the
CC       GPI transamidase forms a carbonyl intermediate with the substrate
CC       protein. {ECO:0000256|RuleBase:RU365060}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-
CC       anchor biosynthesis. {ECO:0000256|RuleBase:RU365060}.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family.
CC       {ECO:0000256|RuleBase:RU365060}.
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DR   EMBL; CR380959; CAG62377.1; -; Genomic_DNA.
DR   RefSeq; XP_449401.1; XM_449401.1.
DR   STRING; 5478.XP_449401.1; -.
DR   MEROPS; C13.005; -.
DR   EnsemblFungi; CAG62377; CAG62377; CAGL0M01298g.
DR   GeneID; 2891170; -.
DR   KEGG; cgr:CAGL0M01298g; -.
DR   CGD; CAL0136869; CAGL0M01298g.
DR   EuPathDB; FungiDB:CAGL0M01298g; -.
DR   eggNOG; KOG1349; Eukaryota.
DR   eggNOG; COG5206; LUCA.
DR   HOGENOM; HOG000204398; -.
DR   InParanoid; Q6FK43; -.
DR   KO; K05290; -.
DR   OMA; DIACNPR; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0042765; C:GPI-anchor transamidase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003923; F:GPI-anchor transamidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016255; P:attachment of GPI anchor to protein; IEA:UniProtKB-UniRule.
DR   InterPro; IPR028361; GPI_transamidase.
DR   InterPro; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR12000; PTHR12000; 1.
DR   PANTHER; PTHR12000:SF1; PTHR12000:SF1; 1.
DR   Pfam; PF01650; Peptidase_C13; 1.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   3: Inferred from homology;
DR   PRODOM; Q6FK43.
DR   SWISS-2DPAGE; Q6FK43.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   GPI-anchor biosynthesis {ECO:0000256|RuleBase:RU365060};
KW   Hydrolase {ECO:0000256|RuleBase:RU365060};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU365060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Signal {ECO:0000256|RuleBase:RU365060};
KW   Thiol protease {ECO:0000256|RuleBase:RU365060};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     21       {ECO:0000256|RuleBase:RU365060}.
FT   CHAIN        22    390       GPI-anchor transamidase.
FT                                {ECO:0000256|RuleBase:RU365060}.
FT                                /FTId=PRO_5004274033.
FT   TRANSMEM    359    377       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   390 AA;  44441 MW;  DCF29F59B5D13A50 CRC64;
     MRIVLPCLLW LVTLACGVVN AEHTNNWAVL VSTSRFWFNY RHMANVLSMY RTVRRLGIPD
     SQIILMLSDD VACNSRNLFP GSVFNNKDHA IDLYGESVEV DYRGYEVTVE NFIRLLTDRW
     TEDQPKSKRL QTDENSNIFI YLTGHGGDDF LKFQDAEEIA SEDIADAFAQ MYEKKRYNEI
     FFMIDTCQAN TMYSKFYSPN VLAVGSSELD ESSYSHHSDV EIGVAVIDRF TYYSLEFLEQ
     IDKTSNLTLK DLFDSYTFEK VHSHVGVRSD LFKRNVSDVL ITDFFANVQN VIPDDNSGKT
     SGNNEDIIDL AIQKSQLASK KDKSSQTPKP KEPASSIYFR TASSLNKNIT DAKNNSNEGL
     MTVLLIILVM LGLYTTFKRT SKKETAKFSL
//

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