ID Q16W05_AEDAE Unreviewed; 741 AA.
AC Q16W05;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 24-JAN-2024, entry version 104.
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 ORFNames=AAEL009372 {ECO:0000313|EMBL:EAT38760.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT38760.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT38760.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38760.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT38760.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38760.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EAT38760.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT38760.1};
RG VectorBase;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CH477578; EAT38760.1; -; Genomic_DNA.
DR RefSeq; XP_001653809.1; XM_001653759.1.
DR RefSeq; XP_001653810.1; XM_001653760.1.
DR AlphaFoldDB; Q16W05; -.
DR SMR; Q16W05; -.
DR STRING; 7159.Q16W05; -.
DR VEuPathDB; VectorBase:AAEL009372; -.
DR eggNOG; KOG2316; Eukaryota.
DR eggNOG; KOG2317; Eukaryota.
DR OMA; HCRLAQS; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000682892; 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 CDD; cd06155; eu_AANH_C_1; 1.
DR CDD; cd06156; eu_AANH_C_2; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.1490.10; putative n-type atp pyrophosphatase, domain 2; 1.
DR Gene3D; 3.30.1330.40; RutC-like; 2.
DR InterPro; IPR002761; Diphthami_syn_dom.
DR InterPro; IPR030662; DPH6/MJ0570.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
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 Pfam; PF01042; Ribonuc_L-PSP; 2.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55298; YjgF-like; 2.
PE 3: Inferred from homology;
FT DOMAIN 1..223
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 741 AA; 83711 MW; BBBE7A01D0E48781 CRC64;
MRVVALVSGG KDSTYNMMQV TAEGHQVIAL ANLHPKDKDE LDSYMYQTVG HQGIEKLAQA
MELPLYRRIT RGNSINTKGN YEPTEDDEVE DLYELLRQVK EERNVEAVAV GAILSDYQRV
RVENVCNRLQ LISLAYLWRR DQTELLQEMI DCQVYAIIIK VAALGLIPDR HLGKSLKEMQ
PHLLNMKDKY GLNVCGEGGE YETFTLDCPL FKSRIVVDDV QTVISSADPV CPVGYLNFTK
LRLVPKERTE TVVVKNSLDF IADLNESSYS DLSDPDLSET ELELIEKVTN AKQRRSEQCH
GAETSSQAME IALKTLEDLI TSNSFTLRQI CYITLYVRDM NEYSYLNAIY SEKFGFTNPP
TRVCVECPLP ENCHVVLEAV AFNSEKSSKY GLLTDYSILH YYLSAVSELE HKRHTMHVQG
ISHWAPANIG TYSQSTKVGH ITYISGQIAL VPGSMTIVEG GIKQQCKLTL RHVSRIAKAM
HAQGQLRDVV QGICFVTHPS YIYEARRQWE RRTANAIMDY IVVPALPRGA LVEWQVWAHT
HNDKFDYEET GCSIGDYSIS IRRRWNYENN CASVVCYVST GLATSTTKLA ELSDDFLQHH
NQLAQSISRE QIHDTIAYVL RKLLQDYPVG NSPTNESGSS SSDEQNNHNS HHHHPHYYHQ
VSHHRTTDGA EPTADSGKPT VHLRIFYQVS AIGSVQSLVE AIESFLSLPS NTVRIAYTVV
PACHLQNFST FISICGLRHH E
//
