ID A0A016VD04_9BILA Unreviewed; 213 AA.
AC A0A016VD04;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Diphthine--ammonia ligase {ECO:0000256|ARBA:ARBA00018426};
DE EC=6.3.1.14 {ECO:0000256|ARBA:ARBA00012089};
DE AltName: Full=ATP-binding domain-containing protein 4 {ECO:0000256|ARBA:ARBA00031202};
DE AltName: Full=Diphthamide synthase {ECO:0000256|ARBA:ARBA00029814};
DE AltName: Full=Diphthamide synthetase {ECO:0000256|ARBA:ARBA00031552};
DE AltName: Full=Protein DPH6 homolog {ECO:0000256|ARBA:ARBA00032849};
GN Name=Acey_s0012.g1819 {ECO:0000313|EMBL:EYC25315.1};
GN Synonyms=Acey-E01A2.5 {ECO:0000313|EMBL:EYC25315.1};
GN ORFNames=Y032_0012g1819 {ECO:0000313|EMBL:EYC25315.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC25315.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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 Evidence={ECO:0000256|ARBA:ARBA00001559};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156}.
CC -!- SIMILARITY: Belongs to the Diphthine--ammonia ligase family.
CC {ECO:0000256|ARBA:ARBA00008496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC25315.1}.
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DR EMBL; JARK01001348; EYC25315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016VD04; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0017178; F:diphthine-ammonia ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
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 SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT DOMAIN 30..168
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 213 AA; 24382 MW; 4B52D9F6F531A742 CRC64;
MIAEAMELPL YRREIKGKPL NQDFDYSPTA GDEVEDLYEL LKTVKEHHPS VQGVSAGAIL
SSYQKLRVED VCKRLNLTPL CYLWERDQKE LLREMISSGL DAVLVKVAAI GLDKKHLGMT
LSEVESTLDR LHSHYGVHPC GEGGEYETFV LDCPLFHKRI LIEESEVSAR LKKKREQKVQ
NHRKLARTTV THQDDPIAPV HYLRLSKLRL VDK
//
