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Database: UniProt
Entry: Q8SQM4_ENCCU
LinkDB: Q8SQM4_ENCCU
Original site: Q8SQM4_ENCCU 
ID   Q8SQM4_ENCCU            Unreviewed;       408 AA.
AC   Q8SQM4;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=GPI-ANCHOR BIOSYNTHESIS PROTEIN {ECO:0000313|EMBL:CAD27091.1};
GN   OrderedLocusNames=ECU09_1210 {ECO:0000313|EMBL:CAD27091.1};
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD27091.1, ECO:0000313|Proteomes:UP000000819};
RN   [1] {ECO:0000313|EMBL:CAD27091.1, ECO:0000313|Proteomes:UP000000819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1 {ECO:0000313|EMBL:CAD27091.1,
RC   ECO:0000313|Proteomes:UP000000819};
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
CC   -!- FUNCTION: Catalytic subunit in the complex catalyzing the transfer of
CC       N-acetylglucosamine from UDP-N-acetylglucosamine to
CC       phosphatidylinositol, the first step of GPI biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003265}.
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DR   EMBL; AL590451; CAD27091.1; -; Genomic_DNA.
DR   RefSeq; XP_955672.1; XM_950579.1.
DR   AlphaFoldDB; Q8SQM4; -.
DR   STRING; 284813.Q8SQM4; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   VEuPathDB; MicrosporidiaDB:ECU09_1210; -.
DR   HOGENOM; CLU_009583_19_0_1; -.
DR   InParanoid; Q8SQM4; -.
DR   OMA; QCVLPTM; -.
DR   OrthoDB; 24420at2759; -.
DR   Proteomes; UP000000819; Chromosome IX.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR013234; PIGA_GPI_anchor_biosynthesis.
DR   PANTHER; PTHR45871; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL BIOSYNTHETIC PROTEIN; 1.
DR   PANTHER; PTHR45871:SF1; PHOSPHATIDYLINOSITOL N-ACETYLGLUCOSAMINYLTRANSFERASE SUBUNIT A; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF08288; PIGA; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000819};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        387..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          43..128
FT                   /note="PIGA GPI anchor biosynthesis"
FT                   /evidence="ECO:0000259|Pfam:PF08288"
FT   DOMAIN          184..336
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   408 AA;  46526 MW;  D00BD3EAA1FB79D0 CRC64;
     MKSLRIAMVS DFFYLLKGGV ETHIKYLSEE LIAMGHKVII ITHRAGNLVG CRMVGNIKVY
     FLDIPVLCRN TTFPSLYSNF PLFKEIFDNE EIEIVHGHQT MSNMCIEGLF HARTLNLKTV
     ITDHSIFEVG PFENIVVNAL CRLALKNIDR CICVSYTSKE NTHIRTMIPL ERIHVIPNAI
     VSDIFRPSEK KHSGGKVVVV VSRLVFRKGI DLLIGAIPLI CKGDRSVRIV IVGDGPMRDG
     IEQVLDENEL YDRVEIIHEV DHERVGEIMR RGDVFLNTSL TETFCITIVE AASCGLHVVS
     TNVGGIHEIL PPDMITFSRI TPEDIARKVL EVLGKSGHNP QDYNKRLKNV YSWERVARMT
     EKVYMEIEKT SLSYRDRRKL YQGVTGFLSR FMITIEYLFL FVLSLRNV
//
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