ID M1W6J1_CLAP2 Unreviewed; 869 AA.
AC M1W6J1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=CPUR_01377 {ECO:0000313|EMBL:CCE27903.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE27903.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE27903.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE27903.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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 -!- 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:CCE27903.1}.
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DR EMBL; CAGA01000006; CCE27903.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W6J1; -.
DR STRING; 1111077.M1W6J1; -.
DR VEuPathDB; FungiDB:CPUR_01377; -.
DR eggNOG; KOG2316; Eukaryota.
DR eggNOG; KOG2317; Eukaryota.
DR HOGENOM; CLU_010289_2_0_1; -.
DR OrthoDB; 103959at2759; -.
DR PhylomeDB; M1W6J1; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0017178; F:diphthine-ammonia ligase activity; IEA:UniProtKB-EC.
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 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 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; 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:UP000016801}.
FT DOMAIN 91..295
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
FT REGION 621..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..772
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 94917 MW; 7774A343B6612CC5 CRC64;
MSAERLNVIA LISGGKDSFY SLLHCIHHGH HIVALANLFP AEAGKHGSGD GTGRETGLRI
ILPSQKQDEL AANCVPNGNN HNEESANKDL NSFMYQTVGH EVISLYAEAT GLPLYRQPIL
GGAVKHERDY DYNSSKLPSS SSSPDETESM LSLLRAVKAH HPEANALCSG AILSTYQRTR
VESVALRLGL TPLSYLWKYP ILPPGPDVHL ADEAQLLRDM ADAGLDARII KVASAGLEEK
HLWERVTSEK GVSRIKASLR RFGFTEGATL GEGGEFETLV LDGPDVLFQK RICVPDHGRV
VVSEGGGSSW LMLRGAYLED KALAVPRSPD DVAIRIREPA LLHSKFQVIA SRLSERDLLP
CEPARSDWGV SGLGGNLSAW ANYSWDDDSN KTHIRRSFVA DPQALGTSIQ CETISIVENI
RAFLSSEDLD PRNVSSVIVL LRDMGDFPQI NEEYGKLFQR ANPPSRITIS CGDLLPKGHS
IVVHMTMPVA DAAKVPNFRN GLHVQSRSYW APANIGPYSQ AIETAITAGG RPTTLRTVHV
AGQIPLVPDY MTLPMVSTPE TTAQQQIVLS LQHLWRIGTE MNIQCWTSAV AYFTRRRQPC
ESSMRECALL AGQAWRMAHS SPFEDEDEDE NDEDQPNGPD LWDLKHDAQY QSLGNSSSSA
SAPPPLPDWS IYTLRQQNEA AESCIAPVFS AEIESLPRGS LVEWHAHSGS KGIEAGSVHV
LHCGGLEAGR WRGWHCVVRA GDYVVLQTTL AYVQQDDDAA AAEDDDDDEE DDGAGSKHAG
TTVPSAEELR EAYRDSLQGL LPRECDPETG NSEPYLVYVD ASTTSGQGET WLEKGVSGQL
AVVPCYSLWG TSAERLSIVA LYERVLVRG
//
