ID U6L872_9EIME Unreviewed; 938 AA.
AC U6L872;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 13-SEP-2023, entry version 25.
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=EBH_0027460 {ECO:0000313|EMBL:CDJ46381.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ46381.1};
RN [1] {ECO:0000313|EMBL:CDJ46381.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ46381.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ46381.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ46381.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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};
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DR EMBL; HG710369; CDJ46381.1; -; Genomic_DNA.
DR AlphaFoldDB; U6L872; -.
DR EnsemblProtists; CDJ46381; CDJ46381; EBH_0027460.
DR VEuPathDB; ToxoDB:EBH_0027460; -.
DR OrthoDB; 103959at2759; -.
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 InterPro; IPR002761; Diphthami_syn_dom.
DR InterPro; IPR030662; DPH6/MJ0570.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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 SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 4: Predicted;
FT DOMAIN 4..203
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
FT REGION 396..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 103308 MW; 55FBE90428893025 CRC64;
MQKKAVALVS GGKDSVYAIH CARQAGFSII AVATLLPRDN AAETDSYMYQ SVATNLGVAI
AECLGVPHYS AHVKGRPVNT ETLQYTFDSD DEVHDLLLLL KRVTHEHPEI EAVTCGAILS
EYQRRRLEYI CGCARLLPVC LLWNREQKSL LKNMIDWGLH AVVVKTASMG LSKQHLGRSV
SDLLPHFLEL NRQFDFHVCG EGTTRFPFHC NLETLNAHRP FQEKEIREKE KKCYASSGRR
SPTAESGGEY ETVTLDCPLF TTGSIAVSDW EQICHSDDAV APVWLQCPVH WKVVPKKPTT
FRPPGELSST LNVLEWLRTK PYQDLIDAAV KDWGVDTNDR DSAPATPLCG EGTHCRIGPH
SICPSNKNCR WTLRSPASCS GGILTGDVCV SCSKESGEVE GDTSSPPEGS SAPPDPDLMS
SWLGEQLSKT LHSGVRTSIV EAVCQVCCPD YMRVPEKVFE RLGIRPVVQT VVVAPLPLGV
KLRLRIVVSH SEGSTVSSAL YLKPFTDDSV LHVHSVNLWV PPCSERDWRA ADRIHLCNAC
QGVRCELASE SSLRVSQLFL RGCDGRLPFT CDFPDEVNGP VLIPSRWRGE EYRRRKPAFY
TALQTVNAFV SLQYTRHLCY AGGANRGFPH DDCQPFIDEV ELGEACSAKP QDIDSASLHV
PQMKTPHFMP LCIVVFVNPK EGKEATRTNF DKKLGVVKQL LHSLIGRSSP RSDNSFSGDD
GASQSIVVVA EAPSLPKDAR VLMLPMWDIS PRVGDRECSQ TCSAKQMRQQ GEKYTVTIAV
VERCLTGTKD TETPVAGGCD NTICSVVVCL SFQRRHDYTG HYTLEDFVEQ LSITLTQWLS
VHPVGGDFAS SSSADTEGSV TVQGRGRMRE VCVFYCPSYL RLLQTDSESF EAICQQRIEA
GCCKNAAASS DILPIITFFP VLNLAGGLLE IVAHTLCA
//
