ID A0A151ID52_9HYME Unreviewed; 711 AA.
AC A0A151ID52;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=ALC62_10944 {ECO:0000313|EMBL:KYM98334.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYM98334.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYM98334.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYM98334.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM98334.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) 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; KQ977985; KYM98334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151ID52; -.
DR STRING; 456900.A0A151ID52; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000078542; 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:UP000078542}.
FT DOMAIN 1..231
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
FT REGION 294..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 80267 MW; 2202CEE394149E3C CRC64;
MKVVALISGG KDSCFNMMQC VAAGHEIVAL ANLFPVEKGV NTLLPDDLDS FMFQTVGHQG
VKYIAQAIGL PIYRYPTFGK ANVQDKYYYP TDSDEVEDLF KLLSTVKERE NIEAVSSGAI
FSDYQRIRVE NVCNRLGLIS LSYLWRRDQD ELLNEMIQSS VNAILIKVAA LGLEIKHLGK
SIFEMQPHLI KIKEKYGVNI CGEGGEYETF TLDCPLFAKS IVIDEYESIV NSRDDVAPVG
YLGFTKIHLE DKDNGELEKL SLSERLKNVL IKSPQDYIAE IIGPELHDGC NLSEDENDEH
ACESNSLKAS NSGQFHPPSP MEILYEEEDC PDAPVVNRNQ TGWFWFGGII GKHPDVTPAI
EEALEKLSTL IQNENLCPSD IVAITLYIKD MSNYKAINEV YVSWLGKRNP PVRVCVQCPL
NVHVALDATA YKENQESGDK WTYKRHTLYV QSISHWAPAN IGPYSQAVRV DDVILVAGQI
PLIPGNMNLL DMNIKRQCRL TLRHIDRIVK AMDAKLRDIV QGICFLTHSS YIEDARKEWE
RRTRNAIVDY VVVPNLPRGA QVEWCVWAHR DNNRFEYEET GKCVANFRIA IRRRWNYENN
VSAIVCYMST GSSNSTGNLT TEASLPSMEL NANELSEAFD YLLCKLRKGS QSANPTCNLR
IFYKVGSFLG PNFLHNVLSK FSTQNLVITI IPATHLHNFS TLLSIYGIRH E
//
