ID A0A178Z5D8_9EURO Unreviewed; 870 AA.
AC A0A178Z5D8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=AYL99_10669 {ECO:0000313|EMBL:OAP54969.1};
OS Fonsecaea erecta.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP54969.1, ECO:0000313|Proteomes:UP000078343};
RN [1] {ECO:0000313|EMBL:OAP54969.1, ECO:0000313|Proteomes:UP000078343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP54969.1,
RC ECO:0000313|Proteomes:UP000078343};
RA Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA Attili D.S., Gorbushina A.;
RT "Draft genome of Fonsecaea erecta CBS 125763.";
RL Submitted (APR-2016) 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 -!- 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:OAP54969.1}.
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DR EMBL; LVYI01000012; OAP54969.1; -; Genomic_DNA.
DR RefSeq; XP_018688336.1; XM_018842175.1.
DR AlphaFoldDB; A0A178Z5D8; -.
DR STRING; 1367422.A0A178Z5D8; -.
DR GeneID; 30014837; -.
DR OrthoDB; 103959at2759; -.
DR Proteomes; UP000078343; 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 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:UP000078343}.
FT DOMAIN 77..285
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
FT REGION 44..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 94678 MW; 4741385C2ECE8438 CRC64;
MSASLNVIAL ISGGKDSLFS ILHCLDNGHK VVALANLYPG ARSSMTHGQG GDDASSSSSP
TTGLRREDES DEPEGEDLNS FMYQTVGHSV IPLYAECLGI PLYRREITGS AVQMGRYYDA
SVLDSSLLDE TEDLVPLLRE AMQAHPEANA LCSGAILSTY QRTRVESVAV RLGLTPLAYL
WQYPALPPPR GRGESLTGLL DDMSVAGCDA RIIKIASGGI KESLLWANVA DPRTQQRLVN
GLRPFFPDHE FWLRGAVLGE GGEYETLAVN GPRRLWKRRI VIAPENQSTF TGEGGVSYLR
LARPGTESNH EDASEARDEC LRLPQAFDPQ FQTVLNMVET QETLNAGRHA DRLDEKDPRW
PQHGLNYSLR PADCLASGHL SICNITWCDP SGDGRPNNAA GQMQGICDQL KSFLESKSSF
LNLPTGLTPS NIVSTTLLLK NMSNFGAVNP IYASLFRAGE PNPPARVTVA CSLPEHIEVS
LSVLLDLGPR ELRRGLHVQS RSYWAPANIG PYSQAICVPV NKQSESRVNV HDTGLVEVVH
MAGQIPLVPH TMELSHAGFP EQAVLSLQHM WRVGQERGVD MWPWGIAFLE SCTDTPARTK
YSCRIWRQTH LTGTRLTKVV ADEEGDEEDG GLDAWDLQHN RAATYQAATA QVTVGQHLHL
LPHPGVLLDD STSFTFLPPF IAAEVVSLPR NAPVEWWSMG ITNLPRRPAS RPRVSVVRRE
HAWVSLIKLT VLPPHGKAGT NIHLVTVLVR RGAGSGLSAV DSVRVETEVL DLIQADNGHE
MAAAAEVVHG TAFVALQDQE GWARISEGRL FKDLAVIPCN SLFGSSGIAP YAGPGNGDES
LLLDEDIEGT AASCSPLAVA MVMRIDQNSR
//
