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DPH51_CANAL
ID   DPH51_CANAL             Reviewed;         299 AA.
AC   Q59NX9; A0A1D8PNR9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Diphthine methyl ester synthase 1;
DE            EC=2.1.1.314;
DE   AltName: Full=Diphthamide biosynthesis methyltransferase 1;
GN   Name=DPH5; OrderedLocusNames=CAALFM_C503640WA; ORFNames=CaO19.6676;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the diphthine synthase family. {ECO:0000305}.
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DR   EMBL; CP017627; AOW29776.1; -; Genomic_DNA.
DR   RefSeq; XP_711428.2; XM_706336.2.
DR   RefSeq; XP_711434.2; XM_706342.2.
DR   AlphaFoldDB; Q59NX9; -.
DR   SMR; Q59NX9; -.
DR   STRING; 237561.Q59NX9; -.
DR   PRIDE; Q59NX9; -.
DR   GeneID; 3646984; -.
DR   GeneID; 3646990; -.
DR   KEGG; cal:CAALFM_C503640WA; -.
DR   KEGG; cal:CAALFM_C503700CA; -.
DR   VEuPathDB; FungiDB:C5_03640W_A; -.
DR   VEuPathDB; FungiDB:C5_03700C_A; -.
DR   eggNOG; KOG3123; Eukaryota.
DR   HOGENOM; CLU_066040_1_0_1; -.
DR   InParanoid; Q59NX9; -.
DR   OMA; TAGDPMV; -.
DR   OrthoDB; 1018517at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000000559; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..299
FT                   /note="Diphthine methyl ester synthase 1"
FT                   /id="PRO_0000156138"
FT   BINDING         9
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         113..114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   299 AA;  33899 MW;  302395C2370187EC CRC64;
     MLYLIGLGLS YESDITVRGL ETVKKCKRVY LEAYTSILMA ANQESLEKFY GREIILADRE
     LVETGSDDIL KDADKEDVAF LVVGDPFGAT THTDLVIRAR ELGIKVETIH NASVMNAVGA
     CGLQLYQFGQ TVSLVFFTDS WKPDSFYGKI MENRKIGLHT LLLLDIKVKE QSIENMARGR
     LIYEPPRYMD IATAAQQLLE IESIRQEQAY TPNTPCVAIS RLGSPTQTFK AGTLQELSEY
     DSGEPLHSLV MLGRQVHELE LEYLYQFVDD KEKFKKFVEQ DQEFFKPAPY VPPEDVDSE
 
 
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