ID A0A1E5RTW3_HANUV Unreviewed; 702 AA.
AC A0A1E5RTW3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
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=AWRI3580_g1096 {ECO:0000313|EMBL:OEJ90321.1};
OS Hanseniaspora uvarum (Yeast) (Kloeckera apiculata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=29833 {ECO:0000313|EMBL:OEJ90321.1, ECO:0000313|Proteomes:UP000095358};
RN [1] {ECO:0000313|Proteomes:UP000095358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3580 {ECO:0000313|Proteomes:UP000095358};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
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:OEJ90321.1}.
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DR EMBL; LPNN01000003; OEJ90321.1; -; Genomic_DNA.
DR STRING; 29833.A0A1E5RTW3; -.
DR VEuPathDB; FungiDB:AWRI3580_g1096; -.
DR OrthoDB; 103959at2759; -.
DR Proteomes; UP000095358; 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 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; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:OEJ90321.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095358}.
FT DOMAIN 1..223
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 702 AA; 81122 MW; 7A12FEF9AA65D607 CRC64;
MKFVGLISGG KDSHYNILHC IKNGHSLTCL ANLRPSDKSQ QELNSFMFQT CGHDLLSKYN
LVTSIPIEFH DIHEHTSEVT TLTYEATXKT DEIEMLFNFL KSIKEKYDIE AVSVGAILSS
YQRNRVEDVC NRLNLKVLSY LWQRDQNDLM REMCDFEEKT KMPFDAKIIK TAAIGLNAED
LGKSLSEVYP KMLKLNKMYD VHICGEGGEF ETIVLDSPIF DKGYFKLKNV NVINNNAEND
DVYSCMLDVE VLTRERKLDN LKDMLIDMEQ PGILSSKWLS VENQIKKENF NISTEVMAVA
NETPIAQDYE MNVCKVGGLL HIQNIQPTNP SSDLDAQCSQ VFKQLFDVLK NHNISKRQIL
TTTLILKDMS NFQHINRNYI KFFNKIGALP PSRACLGSKL IKCDMQLSVI LSLDDKLEKD
GLHVQGISYW NPCNIGPYSQ FIYPKVKGNN NKXGYMAGQI PLISKSMILV NKFEELNSYD
RKDWIRDVVL TFKNYDFLKN TINIKNNLLT TIYISKEYTS LSLRDKIEVV KYIWDITCNP
YKVDIDYDTI DNHKFYYEKE NFDEYDDLDI ENLCIVEVDQ LPAHAPIEMG GVVCQTLDSR
IDDGEEDLPE LIKSQKGIDL LSDDNLRYNY STKSFNSTDD FLDFMHLEHK YPFQGTVYYI
PESIGNKEFF EFENLEYFGV NYAFDYKGQQ HAIIIHQKKI NI
//
