ID B7P2M4_IXOSC Unreviewed; 288 AA.
AC B7P2M4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=diphthine methyl ester synthase {ECO:0000256|ARBA:ARBA00011927};
DE EC=2.1.1.314 {ECO:0000256|ARBA:ARBA00011927};
GN Name=8023702 {ECO:0000313|EnsemblMetazoa:ISCW015932-PA};
GN ORFNames=IscW_ISCW015932 {ECO:0000313|EMBL:EEC00846.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC00846.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC00846.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW015932-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW015932-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 EMBL; ABJB010019535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB011109336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS623090; EEC00846.1; -; Genomic_DNA.
DR RefSeq; XP_002402579.1; XM_002402535.1.
DR AlphaFoldDB; B7P2M4; -.
DR STRING; 6945.B7P2M4; -.
DR PaxDb; 6945-B7P2M4; -.
DR EnsemblMetazoa; ISCW015932-RA; ISCW015932-PA; ISCW015932.
DR GeneID; 8023702; -.
DR KEGG; isc:IscW_ISCW015932; -.
DR VEuPathDB; VectorBase:ISCI015932; -.
DR VEuPathDB; VectorBase:ISCP_037203; -.
DR VEuPathDB; VectorBase:ISCW015932; -.
DR HOGENOM; CLU_066040_1_0_1; -.
DR InParanoid; B7P2M4; -.
DR OMA; TAGDPMV; -.
DR OrthoDB; 1093496at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000001555; 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 1: Evidence at protein level;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EEC00846.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B7P2M4};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR036432-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEC00846.1}.
FT DOMAIN 1..178
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 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 112..113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
SQ SEQUENCE 288 AA; 32060 MW; 2385F73A1F4C5C9A CRC64;
MLYLVGLGLG DVKDITLRGL EIVKKCSKVY LESYTSVLSA GQSQLEKFYG KELILADREM
VEQGSEEMLQ AAKNEDVAFL VVGDPLGATT HSDLMLRAHE LGVQTRLVHN ASILTAVGCC
GLQLYSFGET VSIVLWTESW KPHSYYDKIA ANRRRGLHTL CLLDIKMKEK TVENIIKGRD
IYEPPRFMTA SEAADQLLQI LETKKEEGIP EGELAYSENS MCIGLARVGT ETQQVVCASL
RDMSSCDLGG PLHSLIVPGK LHPMELEMLK LFVVDQAWFD EVCRRSTE
//
