ID A0A1J1IFH5_9DIPT Unreviewed; 739 AA.
AC A0A1J1IFH5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=CLUMA_CG012131 {ECO:0000313|EMBL:CRK99013.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK99013.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK99013.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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; CVRI01000048; CRK99013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1IFH5; -.
DR STRING; 568069.A0A1J1IFH5; -.
DR OrthoDB; 103959at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000183832; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000183832}.
FT DOMAIN 1..222
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 739 AA; 84150 MW; F2310F99541DDBCB CRC64;
MKVVALVSGG KDSTFNMLCC QSEGHEIVAL ANLHPADKDE LDSFMYQTVG HMGIEMLAEA
MELPLYRKTT SGLTTQKGKI YEPTEDDEVE DLYELLKQVK DEMQIEAVSV GAIFSDYQRV
RCENVCSRLN LTSLAYLWRR DQGELLQEMI DCQLEAIIIK VASLGLTPER HLGKSIRDMQ
GHLLKMHDKY GVNICGEGGE YETFTLDCPL FKKRIVIDDH QVIISSSDPV CPVGYINFTK
LHLEAKEPSD FKEYVIKNSL DFINELNSSS YSDLSDPDLT DTELEFIEKE NFAKHSGMPS
SHSGSLAGNF SRSQSMNMTK NNSLEQETLE EMKFEYEQNR LENQPHVVSN SKGWHWISSI
QGEGETTKDG VEKAMNQLEE IILEHSMKLN DICYITIYVR DISEYSILND VYIQRFNFQN
PPTRVCVETC LPHGCHIIME AVAFKTGHVK ETDYKRHTMH VQGISHWAPA NIGPYSQSTK
IGEITYISGQ IGLIPGNMKV ISGGIKQECK LILRHINRIA KAMNSHGQLR DVVQGICFVT
HPSYISEARR QWERRTANAI MDYIVVPGLP RKALVEWQVW IHTHNNKFEY EETGCSVGNQ
YVISIRRRWN YENNCAAIIC YVSTGQTSSS TKLTDMTDEM KQRHETLMTS LNESHLDEIM
QYNLSKIMQG YPKTTENVPA IHFRIFYQVM NPSPANLIIK TMKSFKDATK TANIAFTVIP
SCYLQNYGTF ISICGVRHE
//