DPH5_BOVIN
ID DPH5_BOVIN Reviewed; 285 AA.
AC Q5E982; Q2HJ50;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Diphthine methyl ester synthase;
DE EC=2.1.1.314;
DE AltName: Full=Diphthamide biosynthesis methyltransferase;
GN Name=DPH5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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:0000250|UniProtKB:P32469}.
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:0000250|UniProtKB:P32469};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- SIMILARITY: Belongs to the diphthine synthase family. {ECO:0000305}.
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DR EMBL; BT021038; AAX09055.1; -; mRNA.
DR EMBL; BC113310; AAI13311.1; -; mRNA.
DR RefSeq; NP_001070289.1; NM_001076821.1.
DR RefSeq; XP_005204150.1; XM_005204093.3.
DR RefSeq; XP_005204151.1; XM_005204094.3.
DR RefSeq; XP_005204152.1; XM_005204095.3.
DR RefSeq; XP_005204153.1; XM_005204096.3.
DR AlphaFoldDB; Q5E982; -.
DR SMR; Q5E982; -.
DR STRING; 9913.ENSBTAP00000025327; -.
DR PaxDb; Q5E982; -.
DR PRIDE; Q5E982; -.
DR Ensembl; ENSBTAT00000025326; ENSBTAP00000025326; ENSBTAG00000019029.
DR Ensembl; ENSBTAT00000025327; ENSBTAP00000025327; ENSBTAG00000019029.
DR GeneID; 508904; -.
DR KEGG; bta:508904; -.
DR CTD; 51611; -.
DR VEuPathDB; HostDB:ENSBTAG00000019029; -.
DR VGNC; VGNC:28180; DPH5.
DR eggNOG; KOG3123; Eukaryota.
DR GeneTree; ENSGT00390000010568; -.
DR HOGENOM; CLU_066040_1_0_1; -.
DR InParanoid; Q5E982; -.
DR OMA; TAGDPMV; -.
DR OrthoDB; 1018517at2759; -.
DR TreeFam; TF105603; -.
DR Reactome; R-BTA-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000019029; Expressed in oocyte and 109 other tissues.
DR GO; GO:0004164; F:diphthine synthase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR CDD; cd11647; DHP5_DphB; 1.
DR Gene3D; 3.30.950.10; -; 1.
DR Gene3D; 3.40.1010.10; -; 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 PANTHER; PTHR10882; PTHR10882; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036432; Diphthine_synth; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR TIGRFAMs; TIGR00522; dph5; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..285
FT /note="Diphthine methyl ester synthase"
FT /id="PRO_0000156132"
FT BINDING 9
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 112..113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2P9"
SQ SEQUENCE 285 AA; 31662 MW; 64165AB6BB61D4D1 CRC64;
MLYMIGLGLG DAKDITVKGL EVVRRCSRVY LETYTSVLTV GKEVLEEFYE RKLILADREE
VEQEADNILK DADISDVAFL VVGDPFGATT HSDLILRATK LGIPYRVIHN ASIMNAVGCC
GLQLYKFGET VSIVFWTDTW RPESFFDKVK KNRQNGMHTL CLLDIKVKEQ SLENLIKGRK
IYEPPRYMSV NQAAQQLLEI VQNQRIRGEE PAVTEETLCV GLARVGAEDQ KIAAGTLQQM
STVDLGGPLH SLIITGGSLH PLEMEMLSLF TIPENSSEAQ SIGGL
