ID A0A1J9RB33_9PEZI Unreviewed; 585 AA.
AC A0A1J9RB33;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Phosphatidylinositol:udp-c transferase pig-c {ECO:0000313|EMBL:OJD37354.1};
GN ORFNames=BKCO1_7000119 {ECO:0000313|EMBL:OJD37354.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD37354.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD37354.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD37354.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OJD37354.1}.
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DR EMBL; MNUE01000007; OJD37354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9RB33; -.
DR STRING; 236234.A0A1J9RB33; -.
DR OrthoDB; 205848at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW Transferase {ECO:0000313|EMBL:OJD37354.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT REGION 1..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 61363 MW; 8114461F8A47FBDA CRC64;
MKAYRWKLGS LNRPSDAVPQ QGQGHLLTSR RSKQRWPGHP PTMHQTQGTS SFAGDNASAL
PCATSLSLHQ MPTTTPSSLA NDDDEDRRAS RASRVSSLST PRVSPPTTAI ANGEDVSPTS
APPPPRQQQS LATATATAAS KPASNNNKPH HKSPPSRSHR SHQSDDHHDH HHSFPPAAAG
IPDPSRLAPE DAIFPPPPRI SPQAAASRRA LVRSFEGEAE AEQHQQRQRQ QLAVTGGSGG
LGAANNNSSN NNAGGGTGTG TATTTTGGVG GRGSGGNAVG GSGGGGSESS SAAGRIMEQR
RKRERDRGRS GSRRRKGAWK KLLWVKQSYP DNYTDEETFL DHLQRNPRLQ PYEFWPLVGD
STVIVQHVMS VAIWCSCFSG IVQARVTPFM VVCTGSALTV LGWLLWDFWV SEEEDAERTA
DAVAHVITAA EAAKNEGAPA EEVASSASSA SSAAAAGQGS SGLGLLIPNA NAPGARTGHS
RGGSLASVVS NGSAVSAIST GHPTGDPTFA AAYQSPHGEP MSPRNQRRWA TIKSAVLIYC
VLLGLSPILK SLTKSTTSDS IWAMTSFLTI INISFFDYGG GVGAK
//
