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Database: UniProt
Entry: A0A437A534_9PEZI
LinkDB: A0A437A534_9PEZI
Original site: A0A437A534_9PEZI 
ID   A0A437A534_9PEZI        Unreviewed;       438 AA.
AC   A0A437A534;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   02-APR-2025, entry version 22.
DE   RecName: Full=GPI mannosyltransferase 1 {ECO:0000256|ARBA:ARBA00013797, ECO:0000256|RuleBase:RU365064};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU365064};
DE   AltName: Full=GPI mannosyltransferase I {ECO:0000256|RuleBase:RU365064};
GN   ORFNames=DFL_004457 {ECO:0000313|EMBL:RVD86167.1};
OS   Arthrobotrys flagrans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Arthrobotrys.
OX   NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD86167.1, ECO:0000313|Proteomes:UP000283090};
RN   [1] {ECO:0000313|EMBL:RVD86167.1, ECO:0000313|Proteomes:UP000283090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD86167.1,
RC   ECO:0000313|Proteomes:UP000283090};
RA   Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT   "Intercellular communication is required for trap formation in the
RT   nematode-trapping fungus Duddingtonia flagrans.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-
CC       acyl-PI during GPI precursor assembly. Required for cell wall
CC       integrity. {ECO:0000256|ARBA:ARBA00025399,
CC       ECO:0000256|RuleBase:RU365064}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC       ECO:0000256|RuleBase:RU365064}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU365064}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU365064}.
CC   -!- SIMILARITY: Belongs to the PIGM family. {ECO:0000256|ARBA:ARBA00011071,
CC       ECO:0000256|RuleBase:RU365064}.
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:RVD86167.1}.
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DR   EMBL; SAEB01000006; RVD86167.1; -; Genomic_DNA.
DR   RefSeq; XP_067491711.1; XM_067633554.1.
DR   AlphaFoldDB; A0A437A534; -.
DR   STRING; 97331.A0A437A534; -.
DR   GeneID; 93586768; -.
DR   VEuPathDB; FungiDB:DFL_004457; -.
DR   OrthoDB; 1741594at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000283090; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IEA:TreeGrafter.
DR   GO; GO:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR007704; PIG-M.
DR   PANTHER; PTHR12886:SF0; GPI MANNOSYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR12886; PIG-M MANNOSYLTRANSFERASE; 1.
DR   Pfam; PF05007; Mannosyl_trans; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU365064};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU365064};
KW   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW   ECO:0000256|RuleBase:RU365064};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365064};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283090};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365064};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU365064};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU365064}.
FT   TRANSMEM        23..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        148..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        182..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        226..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        302..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        331..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        367..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
SQ   SEQUENCE   438 AA;  49728 MW;  6625D3559E42C791 CRC64;
     MLTVNFHDGF AILIIILRLH THISVTSLLV LSSLLRLVFL LYGLYQDATS VFKYTDIDYL
     VFTDAARYVS NFSSPYLRAT YRYTPLLSWL LLPSTFEPQS LWFSFGKLLF AAGDILAGYL
     IIQVLQIYGF KATRAMKYAS LWLLNPMVAT ISTRGSSEGL LGVIVIALLW SVEKRRVVLS
     GAILGFAVHF KIYPFIYAPS ILLWMQPPNQ PDLISKIKGF ITKDRLVFSI TAFTTFMGLN
     VGMYAVYGHP FIVHTFLHHL TRLDHRHNFS PYNTLLYLKS SPFTPDPLYP AITLSNLTIE
     RLAFLPQLLI SSILLPLFAQ KDLPSTMFAQ TFAFVTFNKV VTSQYFMWYL VLLPFYLGRS
     RFLRRKVVGV VALGLWVVTQ GLWLGQAYHL EFEGENKFWP GLWSAAAAFF LVNCWILGVV
     VEDIGGMGVI SEKVVVSR
//
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