ID A0A067TUM4_GALM3 Unreviewed; 697 AA.
AC A0A067TUM4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=GALMADRAFT_235897 {ECO:0000313|EMBL:KDR83614.1};
OS Galerina marginata (strain CBS 339.88).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR83614.1, ECO:0000313|Proteomes:UP000027222};
RN [1] {ECO:0000313|Proteomes:UP000027222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL142368; KDR83614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067TUM4; -.
DR STRING; 685588.A0A067TUM4; -.
DR HOGENOM; CLU_010289_2_1_1; -.
DR OrthoDB; 103959at2759; -.
DR Proteomes; UP000027222; 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; cd06155; eu_AANH_C_1; 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; 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:UP000027222}.
FT DOMAIN 1..239
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 697 AA; 75987 MW; ABB1637ACC7D9DF6 CRC64;
MKYLALLSGG KDSCYNLVHC AQNGHELVAA ASLGPEPGKE ELDSYLYQTV GQDAIEFVAR
ALEVPLYRRV ITGDAVEQGS EYGGRNANNA GGVAGDETED LYELLLTVQA HHPDVKGVSV
GAILSNYQRV RVEHVCRRLE LTPLCYLWQR NQGELLAEMI EAGMEAILIK VAGIGLTTSH
LGKTLAQMEP TLKKLNTLYG SHICGEGGEY ETLTLDCPLF KHRIKLIDTE TVIHSGSDFA
AVAYLRVKAA ELVPKPPKPT SAQAVSTPPL LEDEFKALQG AILQSQGRSE ARNLPSLHVG
SRAFHHPTGP VSSIGLRKGA WVVVANIQVS LLEGENDITI EEEVIRCFDT LAERLAEGGL
TLSQCCIINI FISSMDLFLR VNAVYSTFLG TSPPARACVG VDLPPGIRVR MEAMAFSEKT
PFDRQALHVQ GLSYWAPANI GPYSQAIAVG ERVFISGQIG LLPSQLALPS PRSLATELGL
ASQHVARVTS ALRDYSGGGW EGYTQLALYW MTQLDDLVHV KAGHIALQSS DYPTLFLVVK
ELPKDALVEK QVLLHTGRCP VIDEDDGEVL LQNSVPSYER GYSNIGDQGA LEWELSSFKE
DDSSCVIIFV KGDFRKGVTH FQELSSKMTS IVASALSIRY FYRPDTGTDM QYLCRRIFGE
NGAPAVTPVP CQMISSLSTD DWDLAFCVVT ASRTQNQ
//
