ID A0A915AIM3_PARUN Unreviewed; 713 AA. AC A0A915AIM3; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 08-NOV-2023, entry version 5. DE RecName: Full=GPI mannosyltransferase 1 {ECO:0000256|ARBA:ARBA00013797}; DE EC=2.1.1.314 {ECO:0000256|ARBA:ARBA00011927}; DE AltName: Full=GPI mannosyltransferase I {ECO:0000256|ARBA:ARBA00032997}; DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class M protein {ECO:0000256|ARBA:ARBA00031139}; OS Parascaris univalens (Nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Parascaris. OX NCBI_TaxID=6257 {ECO:0000313|Proteomes:UP000887569, ECO:0000313|WBParaSite:PgR009X_g134_t03}; RN [1] {ECO:0000313|WBParaSite:PgR009X_g134_t01, ECO:0000313|WBParaSite:PgR009X_g134_t02} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (NOV-2022) to UniProtKB. 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. {ECO:0000256|ARBA:ARBA00025668}. CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that CC catalyzes four methylations of the modified target histidine residue in CC translation elongation factor 2 (EF-2), to form an intermediate called CC diphthine methyl ester. The four successive methylation reactions CC represent the second step of diphthamide biosynthesis. CC {ECO:0000256|ARBA:ARBA00004006}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation CC elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl CC ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:42652, Rhea:RHEA-COMP:9749, Rhea:RHEA- CC COMP:10173, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:73995, ChEBI:CHEBI:79005; EC=2.1.1.314; CC Evidence={ECO:0000256|ARBA:ARBA00000054}; CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}. CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis. CC {ECO:0000256|ARBA:ARBA00005156}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004477}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the PIGM family. CC {ECO:0000256|ARBA:ARBA00011071}. CC -!- SIMILARITY: Belongs to the diphthine synthase family. CC {ECO:0000256|ARBA:ARBA00006729}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR WBParaSite; PgR009X_g134_t01; PgR009X_g134_t01; PgR009X_g134. DR WBParaSite; PgR009X_g134_t02; PgR009X_g134_t02; PgR009X_g134. DR WBParaSite; PgR009X_g134_t03; PgR009X_g134_t03; PgR009X_g134. DR Proteomes; UP000887569; Unplaced. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro. DR GO; GO:0004164; F:diphthine synthase activity; IEA:InterPro. DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR CDD; cd11647; DHP5_DphB; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR035996; 4pyrrol_Methylase_sf. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR004551; Dphthn_synthase. DR InterPro; IPR007704; PIG-M. DR NCBIfam; TIGR00522; dph5; 1. DR PANTHER; PTHR10882:SF0; DIPHTHINE METHYL ESTER SYNTHASE; 1. DR PANTHER; PTHR10882; DIPHTHINE SYNTHASE; 1. DR Pfam; PF05007; Mannosyl_trans; 1. DR Pfam; PF00590; TP_methylase; 1. DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603}; KW Reference proteome {ECO:0000313|Proteomes:UP000887569}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 191..220 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 240..263 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 305..326 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 338..362 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 374..397 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 403..424 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 438..678 FT /note="Tetrapyrrole methylase" FT /evidence="ECO:0000259|Pfam:PF00590" SQ SEQUENCE 713 AA; 80760 MW; 626B9200657724A9 CRC64; MRKRGGIVST NVECTSDSDS ESGEERVVAW TTAKIFITAF LFRALLVCYG PVHDYLFDVN FTDVDYRVFT DAAAYVRRGR SPYERATYRY TPLLAWLLVP NTVWPEFGKM IFCVLDIAVG YDCYETATAP LLARKPSKRT HSRITREAKQ AIVIFWLANP LTAIISARGN ADVIVCAAVV HTLKLLLNNQ WLLAAVVHGL IAIQLKIYPL IYLPSIFLYI SNVRIATGYL DCCRKFLLNW KGFVFVLVSL MSFALSILVY FLLYGNRYIY ESLLYHISRT DTRHNFSPYF YSFYLLDGET TFSQLVGRIA FGPQAALILL ISVRFYDDLP FCWMLLTMAF IAFNKVCTSQ YFLWFISLLP IAQRSIEMSL KRSVVLSSMW VIAQAIWLLA AYFLEFWGVN SFLFIWLASL LFFSTNVFIV AQLITHYRDP FQSVVMVFYL VGLGLGDAED ITVKGLNTIK KCVRVYLEAY TSILSYALDK SKLERFYGKE VIMADRELVE QHSDELLAGA EVSDVCMLVV GDPFGATTHS SLVLRARDLH IPVKVIHNAS IINAVACCGL QLYSFGETVS IVMWTDSWQP DSYYDKIAAN RSRGLHTLCL LDIKVKEQSV DNLLRGREIY EPPRYMSCSE AAKQLLQIAE RKEKAGVQPA YSAETLCVGL ARIGWNNQKI VSCSLSEMVL VDMGEPLHSL VIVGEMHPVE IDMLKAFAVR SAS //