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DPH5_ASPFU
ID   DPH5_ASPFU              Reviewed;         285 AA.
AC   Q6MY91; Q4WS48;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Diphthine methyl ester synthase;
DE            EC=2.1.1.314;
DE   AltName: Full=Diphthamide biosynthesis methyltransferase;
GN   Name=dph5; ORFNames=AfA31E11.010c, AFUA_1G14020;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA   Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA   Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S.,
RA   O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A.,
RA   Salzberg S.L., Saunders D., Seeger K., Sharp S., Warren T., Denning D.W.,
RA   Barrell B.G., Hall N.;
RT   "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT   region encompassing the nitrate assimilation gene cluster.";
RL   Fungal Genet. Biol. 41:443-453(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the diphthine synthase family. {ECO:0000305}.
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DR   EMBL; BX649607; CAF32112.1; -; Genomic_DNA.
DR   EMBL; AAHF01000004; EAL90734.1; -; Genomic_DNA.
DR   RefSeq; XP_752772.1; XM_747679.1.
DR   AlphaFoldDB; Q6MY91; -.
DR   SMR; Q6MY91; -.
DR   STRING; 746128.CADAFUBP00001329; -.
DR   EnsemblFungi; EAL90734; EAL90734; AFUA_1G14020.
DR   GeneID; 3509777; -.
DR   KEGG; afm:AFUA_1G14020; -.
DR   VEuPathDB; FungiDB:Afu1g14020; -.
DR   eggNOG; KOG3123; Eukaryota.
DR   HOGENOM; CLU_066040_1_0_1; -.
DR   InParanoid; Q6MY91; -.
DR   OMA; TAGDPMV; -.
DR   OrthoDB; 1018517at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000002530; Chromosome 1.
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..285
FT                   /note="Diphthine methyl ester synthase"
FT                   /id="PRO_0000156137"
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         221
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   285 AA;  31490 MW;  3B39977F72174678 CRC64;
     MLYLVGLGLA DETDITVKGL EVVKRAERVY LEAYTSILLV SKEKLEAFYG RPVIEADREL
     VETGSDEILA GADKADVAFL VVGDPFGATT HTDLVLRARE MGIESKVIPN ASIMSGIGCT
     GLQLYNFGQT VSMVFFTENW KPTSYYDRVK ENVQLGLHTL VLLDIKVKEQ SYENMARGRR
     IFEPPRYMTV AQCASQMLET EEERKEGVFG PDSLAVGAAR VGGPDQKLVV GTLKELSEVD
     MGPPLHSLVL LGRKAHDLER LYIREFAVDK ATFDASWNKG YGATS
 
 
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