ID   DPH6_BOVIN              Reviewed;         267 AA.
AC   Q2HJF5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Diphthine--ammonia ligase;
DE            EC=6.3.1.14;
DE   AltName: Full=ATP-binding domain-containing protein 4;
DE   AltName: Full=Diphthamide synthase;
DE   AltName: Full=Diphthamide synthetase;
DE   AltName: Full=Protein DPH6 homolog;
GN   Name=DPH6; Synonyms=ATPBD4;
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].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Amidase that catalyzes the last step of diphthamide
CC       biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists
CC       in the conversion of an L-histidine residue in the translation
CC       elongation factor eEF-2 (EEF2) to diphthamide (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + diphthine-[translation elongation factor 2] + NH4(+) =
CC         AMP + diphosphate + diphthamide-[translation elongation factor 2] +
CC         H(+); Xref=Rhea:RHEA:19753, Rhea:RHEA-COMP:10172, Rhea:RHEA-
CC         COMP:10174, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82696,
CC         ChEBI:CHEBI:456215; EC=6.3.1.14;
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC   -!- SIMILARITY: Belongs to the Diphthine--ammonia ligase family.
CC       {ECO:0000305}.
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DR   EMBL; BC105462; AAI05463.1; -; mRNA.
DR   RefSeq; NP_001070484.1; NM_001077016.1.
DR   AlphaFoldDB; Q2HJF5; -.
DR   SMR; Q2HJF5; -.
DR   STRING; 9913.ENSBTAP00000051676; -.
DR   PaxDb; Q2HJF5; -.
DR   PRIDE; Q2HJF5; -.
DR   Ensembl; ENSBTAT00000055382; ENSBTAP00000051676; ENSBTAG00000001364.
DR   GeneID; 767944; -.
DR   KEGG; bta:767944; -.
DR   CTD; 89978; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001364; -.
DR   VGNC; VGNC:28181; DPH6.
DR   eggNOG; KOG2316; Eukaryota.
DR   GeneTree; ENSGT00420000029820; -.
DR   HOGENOM; CLU_010289_0_1_1; -.
DR   InParanoid; Q2HJF5; -.
DR   OMA; NYALYWA; -.
DR   OrthoDB; 1126213at2759; -.
DR   TreeFam; TF313566; -.
DR   Reactome; R-BTA-5358493; Synthesis of diphthamide-EEF2.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000001364; Expressed in oocyte and 108 other tissues.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017178; F:diphthine-ammonia ligase activity; IBA:GO_Central.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IBA:GO_Central.
DR   CDD; cd01994; Alpha_ANH_like_IV; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR002761; Diphthami_syn_dom.
DR   InterPro; IPR030662; DPH6/MJ0570.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR12196; PTHR12196; 1.
DR   Pfam; PF01902; Diphthami_syn_2; 1.
DR   PIRSF; PIRSF039123; Diphthamide_synthase; 1.
DR   TIGRFAMs; TIGR00290; MJ0570_dom; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..267
FT                   /note="Diphthine--ammonia ligase"
FT                   /id="PRO_0000282396"
FT   MOD_RES         97
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQ28"
SQ   SEQUENCE   267 AA;  29860 MW;  AA38E463F4A819E3 CRC64;
     MRVAALISGG KDSCYNMMQC VAAGHQIVAL ANLRPAENQV GSDELDSYMY QTVGHHAIDL
     YAEAMALPLY RRTIRGKSVD TGPVYTKCEG DEVEDLYELL KLVKEKEEVE GISVGAILSD
     YQRVRVENVC KRLNLQPLAY LWQRNQEDLL QEMISSNIQA IIIKVAALGL DPDKHLGKPL
     DQMEPYLLEL SKKYGVHVCG EGGEYETFTL DCPLFKKKII VDSSEVVTHS ADAFAPVAYL
     RFLELHLEDK VSPVPDNCRT SNDIHNS