ID W9IYU6_FUSOX Unreviewed; 935 AA.
AC W9IYU6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=Diphthine--ammonia ligase {ECO:0000256|ARBA:ARBA00018426};
DE EC=6.3.1.14 {ECO:0000256|ARBA:ARBA00012089};
DE AltName: Full=Diphthamide synthase {ECO:0000256|ARBA:ARBA00029814};
DE AltName: Full=Diphthamide synthetase {ECO:0000256|ARBA:ARBA00031552};
GN ORFNames=FOYG_02951 {ECO:0000313|EMBL:EWY98475.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY98475.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY98475.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) 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};
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DR EMBL; JH717840; EWY98475.1; -; Genomic_DNA.
DR AlphaFoldDB; W9IYU6; -.
DR HOGENOM; CLU_010289_2_0_1; -.
DR OrthoDB; 103959at2759; -.
DR Proteomes; UP000030753; Unassembled WGS sequence.
DR GO; GO:0017178; F:diphthine-ammonia ligase activity; IEA:UniProtKB-EC.
DR CDD; cd01994; Alpha_ANH_like_IV; 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 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.
DR SUPFAM; SSF55298; YjgF-like; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030753}.
FT DOMAIN 210..414
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
FT REGION 133..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 935 AA; 101961 MW; 6706D46589F8874D CRC64;
MVGSPGAHRE TSLKHLLPNE LAWRYQHLLL HHTPHPNSPP NSAILHHIKC PLLIKKLSFR
PHFPASSCLP DWVQLPYSSA WSTATVLSAM SSEKLNVIAL ISGGKDSFFS LIHCLEHGHQ
IVALANLFPG PAPDSSSAIS GGQSPFRQED ATKAEPETNL QTPSDLSSPV GFQRIDPGTW
TPQPPDPATG DHDSLRQGQG SGESSDTDLN SFMYQTVGHE VLPLYADATG LPLYRLPITG
RAVRHERDYD ATANAQDKVQ ESDETESMLP LLQSIIARHP EANAVCAGAI LSTYQRTRVE
SIALRLGLVP LAYLWQYPVL PPPSAAISAD TQLLIDMANV GLEARIIKVA SAGLDENHLW
ERVSSETGSS RVKNALRKFG SAQDAAALGE GGEFETLVLD GPSSVFKKRI VVPEQGRRIV
REGGGCSWLM LGGARLEDKH DAAAKPAVRI PNLLDPHFKS VFGDLPQPLN ELKAAKASAI
SRRLTSLSQD AGTFTADSEV LRWSVLPDLG LGEMPIQDET IQVVEKIRDL ASGAGVRLSQ
VTSTIVVLRR MSDFPMVNGE YGKIFTRPNP PSRVTISCGD LLPAGVNIAI SLAAPTPKAI
RDRNGLHVQS RSYWAPANIG PYSQAIDVPV TAQDQPTGLR CISIAGQIPL IPATMLLPST
SEKSHELQIV LSLQHLWRVG QEMKIQWWTS SVAYFPRANS SEIQRSAQLA GYAWKQAHGS
PDEEGDGDNG PDLWDLKYNP AYMSLGNDDK TTRKTLPDWE ALTLRQQNEP ETCIPPMFAA
EVEELPRQAA VEWHAHNGLS KIEEASFLMC CLPELTLPGW KTWHSVVTTA SATVIYSTAA
YSHADRPHSA SLDSLKIDMC KIMQESLHQL HPHGPETVQS KLTLVYADAA QIVSIWNNLG
DKCDVALIPC RSIWSSDGQS VAIVGLFETI FIRES
//
