ID M7TYL0_BOTF1 Unreviewed; 466 AA.
AC M7TYL0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative phosphatidylinositol n-acetylglucosaminyltransferase subunit c protein {ECO:0000313|EMBL:EMR86354.1};
GN ORFNames=BcDW1_4918 {ECO:0000313|EMBL:EMR86354.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR86354.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGC family.
CC {ECO:0000256|ARBA:ARBA00008321}.
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DR EMBL; KB707858; EMR86354.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TYL0; -.
DR STRING; 1290391.M7TYL0; -.
DR HOGENOM; CLU_024002_1_0_1; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR009450; Plno_GlcNAc_GPI2.
DR PANTHER; PTHR12982; PHOSPHATIDYLINOSITOL GLYCAN, CLASS C; 1.
DR PANTHER; PTHR12982:SF0; PHOSPHATIDYLINOSITOL N-ACETYLGLUCOSAMINYLTRANSFERASE SUBUNIT C; 1.
DR Pfam; PF06432; GPI2; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:EMR86354.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:EMR86354.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 123..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 51350 MW; CD27C192E93A8DC0 CRC64;
MVPPLAPQSA PPLNRSSTAP NITSARTVPY ERSHLAPEDA ISQASPPRRS SAAVNQLRMT
NGDAGRLRSR GRHADRTKSS TRRRKTTWKK LLWVKQSYPD NYTDQDTFLE HLQRNPRLQP
YDFWPLVADS TVIVQHVCSV IIFIVSFVGI YDKHVSPVSV VGWGSIATFL GWVLWDLWVG
QEESTRPAFP PPQPFSHSVS ATSSTPNLLA TAASGPRQSY SMSTTSLQST ASNLTQPPPI
RPVYTPHNSH LSHRTSLRLS TAKSALLIYF TLLGLSPILK SLTRSTSSDS IWAMSFFLFT
INIFFFDYAT PSPSSSSGYP PSNTKNKNIP ASLSTNAALM ASTVLASRLP STGQVFSLTL
FSIEVFGLFP VFRRYTRLHS LRGHLILTLL LVFGAGGGVG LVLPQSGRSA WDWKSGLIGV
VLGTLITGLA MGGCSWWLIG LQKYKNEIHG PWDPARPVIR RAWDDY
//
