ID A0A1E5UVA9_9POAL Unreviewed; 699 AA.
AC A0A1E5UVA9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=diphthine methyl ester synthase {ECO:0000256|ARBA:ARBA00011927};
DE EC=2.1.1.314 {ECO:0000256|ARBA:ARBA00011927};
GN ORFNames=BAE44_0022161 {ECO:0000313|EMBL:OEL16819.1};
OS Dichanthelium oligosanthes.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Dichantheliinae; Dichanthelium.
OX NCBI_TaxID=888268 {ECO:0000313|EMBL:OEL16819.1, ECO:0000313|Proteomes:UP000095767};
RN [1] {ECO:0000313|EMBL:OEL16819.1, ECO:0000313|Proteomes:UP000095767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Kellogg 1175 {ECO:0000313|Proteomes:UP000095767};
RC TISSUE=Leaf {ECO:0000313|EMBL:OEL16819.1};
RA Studer A.J., Schnable J.C., Brutnell T.P.;
RT "The draft genome of Dichanthelium oligosanthes: A C3 panicoid grass
RT species.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156}.
CC -!- SIMILARITY: Belongs to the diphthine synthase family.
CC {ECO:0000256|ARBA:ARBA00006729}.
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:OEL16819.1}.
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 EMBL; LWDX02061890; OEL16819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5UVA9; -.
DR STRING; 888268.A0A1E5UVA9; -.
DR OrthoDB; 1093496at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000095767; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004164; F:diphthine synthase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR CDD; cd11647; DHP5_DphB; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00522; dph5; 1.
DR PANTHER; PTHR10882:SF0; DIPHTHINE METHYL ESTER SYNTHASE; 1.
DR PANTHER; PTHR10882; DIPHTHINE SYNTHASE; 1.
DR Pfam; PF13460; NAD_binding_10; 1.
DR Pfam; PF00590; TP_methylase; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000095767};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 203..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 220..300
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF13460"
FT DOMAIN 333..487
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT DOMAIN 513..603
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 76271 MW; 706C370069128DA9 CRC64;
MMEVACFSPV LSPLVSVPSC GRGPRGRAAL LRLRPPSAAS LGPLACGAVV GRGRWRLAAA
AEPQAMQEQP ARTEVSDEAG RAGASEASSK LLLVVGGTGG VGQLVVASLL SRNIKSRLLL
RDPEKAVSLF GKQDESVLQV HLELQHSVFL PRCSREKENT IFSDLSESDS CKSADTEYIF
HDRYPCLSPR YFCTPLRPML HRILIFVLKK LWYAFFSIMN LFGVLKYKKM GEDFVRNSGI
PFTIIRPGRL TDGPYTSYDL NTLLKATAGE RRAVVIGKGD KLVGEVSRLV VAEACIQALD
IESTEGQIYE INSVKGEGPG TDPEKWKELF SSMLYIVGLG LGDERGVTVR GLDAVRRCAR
VYMEAYTALL TLGADGDPSP RLAKLEKLYG KEVTVAGRGM IEEERGDQVL REAAASDVAF
LVVGYPFGSD EGFRRSAHTD LVVRAKKLGV EVKVIDGASV LNAVGVCGLQ LHRYGAAITI
PFLPETYTSD YFYQAIVNNR WLGLHTLCLL AAMLYIVGLG LGDERDITVR GLDAVRSCSK
VYMEAYTSLL SLGLDPAALA NLEKLYGKEI TVADREMVEE RVDQVLLEAA DTDVAFLVVG
DPFGGKKVYE PPRFMTVNTA ISQLLEVEEA RGGSDRLLPA YGKDTLCIGV ARLGSDDQKI
VAGPMEKLLD VDFGPPLHCL IIVGETHPVE EEMLEFYKM
//
