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Database: UniProt
Entry: A0A0U1LIJ0_TALIS
LinkDB: A0A0U1LIJ0_TALIS
Original site: A0A0U1LIJ0_TALIS 
ID   A0A0U1LIJ0_TALIS        Unreviewed;       694 AA.
AC   A0A0U1LIJ0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Putative phosphatidylinositol N-acetylglucosaminyltransferase subunit C {ECO:0000313|EMBL:CRG82815.1};
GN   ORFNames=PISL3812_00161 {ECO:0000313|EMBL:CRG82815.1};
OS   Talaromyces islandicus (Penicillium islandicum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Islandici.
OX   NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG82815.1, ECO:0000313|Proteomes:UP000054383};
RN   [1] {ECO:0000313|EMBL:CRG82815.1, ECO:0000313|Proteomes:UP000054383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG82815.1};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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}.
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DR   EMBL; CVMT01000001; CRG82815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1LIJ0; -.
DR   STRING; 28573.A0A0U1LIJ0; -.
DR   OrthoDB; 205848at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000054383; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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; PF00704; Glyco_hydro_18; 1.
DR   Pfam; PF06432; GPI2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000313|EMBL:CRG82815.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054383};
KW   Transferase {ECO:0000313|EMBL:CRG82815.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        441..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        470..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        493..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          528..627
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|Pfam:PF00704"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..60
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   694 AA;  76148 MW;  547402C529EBAD56 CRC64;
     MLRETSRVLS SAEPATSEPP ASPFTLHQLS WSPYSIARGP MAPQPQTSPP PIPPPVPVET
     HPNRAGGLKP PLPQRVPPDP TRLAPEHAYY PHSQPRSWHD SSAQHRPIGG VVSTSSSVAV
     AALRPPPAVP GFETRKPDAR KSRDRRRKKR KGAWKKLMWV RQTYPDNYTD AETFLDHLQR
     NPRLRPYDFW PLVADSTVIV QHVCSVVIFV CCFVEIVQNR VSPVSVVGWG SIGTVLGWVL
     WDSWVWKEQS EAIKAAQIIE GAELDDGSSA SSASSNPGAS TSQSSSNVSN VHGLGLNIPR
     SSSEMHLRRR STELSTASLQ SANPNSPTLQ PTNIFYTCKE DGKSLLSTRN RQRLATVKSA
     VLIYCALLGL SPILKSLTKS TASDSIWALS CWLMIINIFS FDYGSGEGGM DATKFPASLS
     TNAALMASTV LASRLPSTTH VFSLTLFSIE VFGLFPVFRR HLKHVSWTGH LILTFGLVFA
     AGAGVGITLR GGWAAAIVGS FLGSILTALV MGSCSWWLLV CHSAVSLRYV IYVDEWDRAN
     LPSTEVTSGS THAIMAFAES ETFNNDGQFT PWGNVQYFRS PFLKDTEFMV SIGGWGDITG
     FSNAIKSKAS IQNYAENVAA MITSIGVESV GGQYYFDTIA HIFWMWDTPQ LMQRKFTDIV
     NKLKMGGVMA WSLGEDSYDW SHVNVLKAQV RMRA
//
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