ID W7HQ27_9PEZI Unreviewed; 880 AA.
AC W7HQ27;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN ORFNames=DRE_04427 {ECO:0000313|EMBL:EWC46256.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC46256.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC46256.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC46256.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI
CC during GPI precursor assembly. {ECO:0000256|ARBA:ARBA00024708}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU363075}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363075}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGB
CC subfamily. {ECO:0000256|ARBA:ARBA00006065}.
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DR EMBL; KI966419; EWC46256.1; -; Genomic_DNA.
DR AlphaFoldDB; W7HQ27; -.
DR HOGENOM; CLU_327056_0_0_1; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000024837; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum 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 Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR22760:SF4; GPI MANNOSYLTRANSFERASE 3; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU363075};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363075};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW Reference proteome {ECO:0000313|Proteomes:UP000024837};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363075};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363075}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..880
FT /note="Mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004895527"
FT TRANSMEM 180..204
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 216..239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 269..291
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 303..319
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 325..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 353..371
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT DOMAIN 551..867
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 880 AA; 98173 MW; B264D69C39EA37AB CRC64;
MPSTFASSTA TVFLTVLGIR LLNALTLSTF FQPDEYFQSL EVAASWRPDS PSYVTWEWHH
GLRSVLYPRV FQAVYLVVDA VSHTLGLSPA VNAELLVVAP KVIGAVTAAV GDLYTGLLAR
KLWGDGAGNY ALLFSICSAW NWFCFTRTFS NCLETTLTVI GMSYWPWRSF NARDLSLASL
FAAISFTVRP TNGLISWAIG ALLLEKLPSL KGQATAVYQI GIISGAVLLV NAAIDYGFYN
RITFPFVEFY RLNVTQSISE FYGVSPWHYY YSQGMPLLLT GYLPLALFSL YKGLLSSNSS
VRHLTVLANF VPLAFMITKH KEVRFLYPLL PMFHALMAGV GLPALPRNWN RKWVVSAMVI
INLPIAYYTG YIHQRGVVDV VNWLRVEHYS DHQSQVERPS SAARIGFLMP CHSTPFGSHL
WNAALKSKAG EQTMSAWFLT CEPPVGLSIE ERKEYLDEAD QFYANATMWL AEKFGPPPMK
VDEAVVEPET LWPDKLITFE ATAELIKGYL LVEEKIGRIT NYLLRTNVQL GASYATGIKS
NELVAAGLIA SAKFVNADPG EVVLGGSSTQ LLHNLSSALV FPPGSEIIVT NCEHETNVAP
WLRLARLQGH TIKHWSLDSS KGWTLHFSDL EPLLSEKTAL VAFTNCSNIT GTIHDVKAIA
RSIKQKNPEI LVSVDGVAYA PHRPIDVKDL GIDFYVFSWY KVYGPHISLL YAAPRTSKYI
TPLAHFFNPQ ETLFDKLNLA GGNYELTAAL PKLVEFLTPE VWEEIAKQEE VLSKTMIDWL
STRRDATLYG TAESSSDKRV PVISFSIKGW GSKELVEGLE KQDQKYGIRW GHCYAKRLID
SFGLDKPDEG VVRVSLLFYN TVEEVEGLVK VLEQVLDTKK
//
