ID   DPH6_RAT                Reviewed;         267 AA.
AC   Q5M9F5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 86.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC087148; AAH87148.1; -; mRNA.
DR   RefSeq; NP_001014203.1; NM_001014181.1.
DR   AlphaFoldDB; Q5M9F5; -.
DR   SMR; Q5M9F5; -.
DR   STRING; 10116.ENSRNOP00000053362; -.
DR   PhosphoSitePlus; Q5M9F5; -.
DR   Ensembl; ENSRNOT00000107739.1; ENSRNOP00000076614.1; ENSRNOG00000037356.5.
DR   Ensembl; ENSRNOT00055005137; ENSRNOP00055003826; ENSRNOG00055003283.
DR   Ensembl; ENSRNOT00060036142; ENSRNOP00060029721; ENSRNOG00060020496.
DR   Ensembl; ENSRNOT00065026600; ENSRNOP00065020870; ENSRNOG00065015904.
DR   GeneID; 362191; -.
DR   KEGG; rno:362191; -.
DR   UCSC; RGD:1310006; rat.
DR   AGR; RGD:1310006; -.
DR   CTD; 89978; -.
DR   RGD; 1310006; Dph6.
DR   GeneTree; ENSGT00420000029820; -.
DR   InParanoid; Q5M9F5; -.
DR   OrthoDB; 103959at2759; -.
DR   PhylomeDB; Q5M9F5; -.
DR   Reactome; R-RNO-5358493; Synthesis of diphthamide-EEF2.
DR   UniPathway; UPA00559; -.
DR   PRO; PR:Q5M9F5; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017178; F:diphthine-ammonia ligase activity; ISO:RGD.
DR   GO; GO:0017183; P:protein histidyl modification to diphthamide; IBA:GO_Central.
DR   CDD; cd01994; Alpha_ANH_like_IV; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.90.1490.10; putative n-type atp pyrophosphatase, domain 2; 1.
DR   InterPro; IPR002761; Diphthami_syn_dom.
DR   InterPro; IPR030662; DPH6/MJ0570.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00290; MJ0570_dom; 1.
DR   PANTHER; PTHR12196:SF2; DIPHTHINE--AMMONIA LIGASE; 1.
DR   PANTHER; PTHR12196; DOMAIN OF UNKNOWN FUNCTION 71 DUF71 -CONTAINING PROTEIN; 1.
DR   Pfam; PF01902; Diphthami_syn_2; 1.
DR   PIRSF; PIRSF039123; Diphthamide_synthase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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_0000282399"
FT   MOD_RES         97
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQ28"
SQ   SEQUENCE   267 AA;  29984 MW;  C9AD123BF8DFB06D CRC64;
     MRVAALISGG KDSCYNMMRC IAEGHQIVAL ANLRPDDNQV ESDELDSYMY QTVGHHAIDL
     YAEAMALPLY RRTIRGRSLE TGRVYTRCEG DEVEDLYELL KLVKEKEEIE GVSVGAILSD
     YQRVRVENVC KRLNLQPLAY LWQRNQEDLL REMIASNIEA IIIKVAALGL DPDKHLGKTL
     GEMEPYLLEL SKKYGVHVCG EGGEYETFTL DCPLFKKKIV VDTSEAVIHS ADAFAPVAYL
     RLSGLHLEEK VSSVPGDDET TSYIHNS
//