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DPH5_DICDI
ID   DPH5_DICDI              Reviewed;         273 AA.
AC   Q75JG8; Q552F4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Diphthine methyl ester synthase;
DE            EC=2.1.1.314;
DE   AltName: Full=Diphthamide biosynthesis methyltransferase;
GN   Name=dph5; ORFNames=DDB_G0276115;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000014; EAL69357.1; -; Genomic_DNA.
DR   RefSeq; XP_643259.1; XM_638167.1.
DR   AlphaFoldDB; Q75JG8; -.
DR   SMR; Q75JG8; -.
DR   STRING; 44689.DDB0238863; -.
DR   PaxDb; Q75JG8; -.
DR   EnsemblProtists; EAL69357; EAL69357; DDB_G0276115.
DR   GeneID; 8620302; -.
DR   KEGG; ddi:DDB_G0276115; -.
DR   dictyBase; DDB_G0276115; dph5.
DR   eggNOG; KOG3123; Eukaryota.
DR   HOGENOM; CLU_066040_1_0_1; -.
DR   InParanoid; Q75JG8; -.
DR   OMA; TAGDPMV; -.
DR   PhylomeDB; Q75JG8; -.
DR   Reactome; R-DDI-5358493; Synthesis of diphthamide-EEF2.
DR   UniPathway; UPA00559; -.
DR   PRO; PR:Q75JG8; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0004164; F:diphthine synthase activity; ISS:dictyBase.
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   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..273
FT                   /note="Diphthine methyl ester synthase"
FT                   /id="PRO_0000327700"
FT   BINDING         10
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         90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         115..116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   273 AA;  31016 MW;  E82B0AF6EDC7D6A2 CRC64;
     MVLYIIGLGL GDEKDVTIKG FEAIKKSSKI YLEAYTSLLG GSTSIEALEK FYEKKIIIAD
     REMVESGCEE MLKESTENDV SFLVVGDPFG ATTHTDLVIR AKELSIPVKV IHNASIMNAI
     GCCGLQLYSY GQTISMVFFT ETTKPDSWYD RVKINRVNGM HTLCLLDIKV KEQSIENMCR
     GRLIYEPPRF MTVNQCIEQL LEIEEIRKEK VYDQDTLCIG LSRVGQDDQQ IISGTMKELL
     DVDFGAPLHS FIICGDMHFI EKEYFETFRV KKN
 
 
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