GenomeNet

Database: UniProt
Entry: A0A0D9Z7H2_9ORYZ
LinkDB: A0A0D9Z7H2_9ORYZ
Original site: A0A0D9Z7H2_9ORYZ 
ID   A0A0D9Z7H2_9ORYZ        Unreviewed;       274 AA.
AC   A0A0D9Z7H2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=diphthine methyl ester synthase {ECO:0000256|ARBA:ARBA00011927};
DE            EC=2.1.1.314 {ECO:0000256|ARBA:ARBA00011927};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM03G18160.2};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM03G18160.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM03G18160.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   ---------------------------------------------------------------------------
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   AlphaFoldDB; A0A0D9Z7H2; -.
DR   EnsemblPlants; OGLUM03G18160.2; OGLUM03G18160.2; OGLUM03G18160.
DR   Gramene; OGLUM03G18160.2; OGLUM03G18160.2; OGLUM03G18160.
DR   HOGENOM; CLU_066040_1_0_1; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
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   HAMAP; MF_01084; Diphthine_synth; 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   NCBIfam; TIGR00522; dph5; 1.
DR   PANTHER; PTHR10882:SF0; DIPHTHINE METHYL ESTER SYNTHASE; 1.
DR   PANTHER; PTHR10882; DIPHTHINE SYNTHASE; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036432; Diphthine_synth; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRSR:PIRSR036432-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..241
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   BINDING         9
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT   BINDING         89
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT   BINDING         117..118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT   BINDING         168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT   BINDING         251
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
SQ   SEQUENCE   274 AA;  30393 MW;  7C9C8C213B50D58A CRC64;
     MLYIVGLGLG DERDITVRGL DAVRRCAKVY MEAYTSLLSL GLDPSALSNL EKMYGKEITV
     ADREMVEERA DQMLREAADA DVAFLVVGDP FGATTHTDLV VRAKNMGVEV KVIHNASVMN
     AVGVCGLQLY RYGETISIPF FTETWRPDSF YEKIQNNRRL GLHTLCLLDI HVKEPTLESL
     CRGKKVYEPP RFMSVNTAIS QLLEVEELRG GSAYGADSLC IGVARLGSDD QKIVAGPMKK
     LLDVDFGPPL HCLIIVGETH PVEEEMIEFH MIKS
//
DBGET integrated database retrieval system