ID A0A024GEN5_9STRA Unreviewed; 860 AA.
AC A0A024GEN5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 08-NOV-2023, entry version 38.
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=BN9_056210 {ECO:0000313|EMBL:CCI44797.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI44797.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI44797.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI44797.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) 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 -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC {ECO:0000256|ARBA:ARBA00005647}.
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:CCI44797.1}.
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DR EMBL; CAIX01000079; CCI44797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GEN5; -.
DR STRING; 65357.A0A024GEN5; -.
DR InParanoid; A0A024GEN5; -.
DR OrthoDB; 103959at2759; -.
DR Proteomes; UP000053237; 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; cd00472; Ribosomal_L24e_L24; 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; 2.30.170.20; Ribosomal protein L24e; 1.
DR Gene3D; 3.30.1330.40; RutC-like; 2.
DR InterPro; IPR002761; Diphthami_syn_dom.
DR InterPro; IPR030662; DPH6/MJ0570.
DR InterPro; IPR038630; L24e/L24_sf.
DR InterPro; IPR000988; Ribosomal_eL24-rel.
DR InterPro; IPR023442; Ribosomal_eL24_CS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR011017; TRASH_dom.
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 Pfam; PF01246; Ribosomal_L24e; 1.
DR SMART; SM00746; TRASH; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF55298; YjgF-like; 2.
DR PROSITE; PS01073; RIBOSOMAL_L24E; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT DOMAIN 696..734
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
SQ SEQUENCE 860 AA; 97755 MW; E4AC7A0AE819F948 CRC64;
MECVKYGHEI IGLAHLFPQE NGSKSTAEID SFMFQSVGSN LVESIASCMD VPLWTAAIAG
KPNTTDLMYN TAVDGDEVED MYQLLLQVKK EVPDLEGVCS GAILSSYQRN RVENVCHRLQ
LTSLTYLWQQ DQQELLERMI QNRVHAIIIK VAAIGLDPTR HLGKSLQEIQ PELLRLKEKY
QLNVCGEGGE YETLTLDCPL FRKRIVINSS RIVMHSDDFC APVAYLVIEE SSLEDKYLLN
PLLKPPISSN DPQSPDEIQD IRQLESAHSD DITAATTFRD QIHVRGLVSR LPISSIQEDM
SDIFNQLRDI LQERQACLQD ICFIHLYLQN MNTFAAVNHE YSNHIFTWQP PSRSCVECKD
LTVKVLLDCF AVRGSGAARI DPTQSVVQVL HVRSISAWAP SCIGPYSQAT TVHRSLILLA
GQIPLNPATM QLIGGNYQEQ SRQCIQNANA VLRVLDSNVK NVISAIVYVV PNLQNDSDYV
PTFPPLQGNV LQCELRSEHS DFQTPVLLIY VSKLPRESLV EVELTALTRT AFDTLCPNTL
QLEEKCNPYT FWYQIVTISR AVCLILAAVK CTERVAKDID YVVSSLIEKI DDAILQAQLF
WNQVLHLRIF YQRYNTIDQT KLVSALRISC KKKGLTVPAI SLIPVSGIQN KAFLAIQVTA
LDIDILDTKM WLMDRVALCL NQSISTQRNA MRIHTCYFCS SPVYPGHGIT FVRNDSKIFR
FCRSKCHKNF NRKRNPRKVK WTKSFRKAAG KEMALDTTYD FEKQRNRVVK YDRDLMNATI
HAMQRVQDIK QRRDQDFHKN RMKTGKVNER VRDLRELEQN ISLIQPAVAS KVNVQVNLNN
AKERNAAQQE SKQSSMLVDQ
//
