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Database: UniProt
Entry: F7W9K1_SORMK
LinkDB: F7W9K1_SORMK
Original site: F7W9K1_SORMK 
ID   F7W9K1_SORMK            Unreviewed;       527 AA.
AC   F7W9K1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=phosphatidylinositol N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00012420};
DE            EC=2.4.1.198 {ECO:0000256|ARBA:ARBA00012420};
DE   AltName: Full=GlcNAc-PI synthesis protein {ECO:0000256|ARBA:ARBA00032160};
GN   ORFNames=SMAC_12075 {ECO:0000313|EMBL:CCC13992.1};
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC13992.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC13992.1, ECO:0000313|Proteomes:UP000001881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC   {ECO:0000313|Proteomes:UP000001881};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:CCC13992.1};
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA   Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCC13992.1}.
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DR   EMBL; CABT02000053; CCC13992.1; -; Genomic_DNA.
DR   RefSeq; XP_003351143.1; XM_003351095.1.
DR   AlphaFoldDB; F7W9K1; -.
DR   STRING; 771870.F7W9K1; -.
DR   GeneID; 10808768; -.
DR   KEGG; smp:SMAC_12075; -.
DR   VEuPathDB; FungiDB:SMAC_12075; -.
DR   eggNOG; KOG1111; Eukaryota.
DR   HOGENOM; CLU_009583_19_2_1; -.
DR   InParanoid; F7W9K1; -.
DR   OMA; QCVLPTM; -.
DR   OrthoDB; 24420at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
DR   GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IEA:InterPro.
DR   GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03796; GT4_PIG-A-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR039507; PIG-A/GPI3.
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   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001881};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        441..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..133
FT                   /note="PIGA GPI anchor biosynthesis"
FT                   /evidence="ECO:0000259|Pfam:PF08288"
FT   DOMAIN          207..344
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   REGION          177..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..200
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  58308 MW;  31F57693F4C06BB1 CRC64;
     MAPTYRIAMV CDFFFPQPGG IESHIYQLST KLIDRGHKVI IITHAYEGRT GVRYLTNGLK
     VYHVPFLVIY RSATFPTVFS FFPIFRNIVL RERIDIVHGH ASLSSLCHEA ILHARTMGLR
     TVFTDHSLFG FADAASILTN KLLKNTVLRA SLDPLMVSVI PNAVVAENFR PLGYPTSSPP
     SSISSPVPGG LPPNPSSLTP PRRILGPHDP ITIVVISRLF YNKGTDLLTA AIPRILAAHP
     NTRFIIAGSG PKAIDLEQMI EQNVLQDRVE MLGPVRHSEV RDVMVRGHIY LHPSLTEAFG
     TVIVEAASCG LYVVCTQVGG IPEVLPSHMT VFAKPEEDDL VAATGKAIAA LRRNEVRTEL
     FHEQVKNMYS WTNVAERTER VYNGISGAIS EAEFYGLNTS QNRNGTGITS TTTATASTAA
     KGVQSFALID RLKRYYGCGV WAGKLFCVLV IIDYLIFLFL ELVFPRERID ICPDWPRKDR
     KKLMMMMGTG GGSDGNNARG GRRAEGGGLE WGDVEDYRRR SRPSRLR
//
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