ID   A0A024GDE8_9STRA        Unreviewed;       880 AA.
AC   A0A024GDE8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   08-NOV-2023, entry version 37.
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_056170 {ECO:0000313|EMBL:CCI44793.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI44793.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI44793.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI44793.1,
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:CCI44793.1}.
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DR   EMBL; CAIX01000079; CCI44793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024GDE8; -.
DR   STRING; 65357.A0A024GDE8; -.
DR   InParanoid; A0A024GDE8; -.
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          716..754
FT                   /note="TRASH"
FT                   /evidence="ECO:0000259|SMART:SM00746"
SQ   SEQUENCE   880 AA;  99821 MW;  A8AA2DF364B681CF CRC64;
     MKVVALVSGG KDSCFAMMEC VKYGHEIIGL AHLFPQENGS KSTAEIDSFM FQSVGSNLVE
     SIASCMDVPL WTAAIAGKPN TTDLMYNTAV DGDEVEDMYQ LLLQVKIVQK 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
//