ID   A0A1V6PW69_9EURO        Unreviewed;       763 AA.
AC   A0A1V6PW69;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-SEP-2023, entry version 20.
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=PENANT_c028G05466 {ECO:0000313|EMBL:OQD81264.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD81264.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQD81264.1}.
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DR   EMBL; MDYN01000028; OQD81264.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6PW69; -.
DR   STRING; 416450.A0A1V6PW69; -.
DR   OrthoDB; 103959at2759; -.
DR   Proteomes; UP000191672; 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   CDD; cd06156; eu_AANH_C_2; 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; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000191672}.
FT   DOMAIN          114..286
FT                   /note="Diphthamide synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01902"
FT   REGION          333..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   763 AA;  82125 MW;  70CD0A4F37E1640A CRC64;
     MAQPSPGLNV IALISGGKDS LYSILHCIRN GHQVVALANL YPEPSPSTTK ADNANDEEED
     IDSFMYQTIG HSIIPLYEEA LGIPLYREAI KGNAVDTSRI YKNTTTTTST STSTPEEADE
     TESLIPLLTR IKRAHPEANA VSAGAILSTY QRTRIENIAG RLGLTPLAWL WQYPILPAPE
     ARIADPLAVA QAGLLEDMAA VGCDARIIKV ASGGLDEGFL WEDVSGSANA GRRVRGRIGK
     AMGRFAGGED VRGAVLGEGG EYETLALNGP DFLWKGRIGV DAVDVRVGEG GVAFARVVGA
     RVEVKDGGDG VAPGDVRRPG LLDGVFEKAL ERDRDYEEGS EGASVVTGTS ASSPEWTACE
     PVHRQTGSSW TISNIVAPEA GPGTGEQMKG IADKVVQALT TASPAESGTR STDDIVFATV
     LLNSMGDFGS MNDVYVSLFN KPNPPARVTV ACGDRLPSNV KVMVSFVVDL CARDLRQGLH
     VQSRSYWAPA NIGPYSQAMS VPLQNNSRLV HIAGQIPLDP ASMEMAQKEQ SPFENYRLRA
     VLALQHLWRI GEATQVDWWL GVVAFLARGE QAAAQAQVAW RLWENMHALP NNEDEDDDEG
     PQLDAWDLKY GRRTEEVTSD AAALFLPKFT VLNSESATSI PPFLAVQVDE LPRGSDIEWQ
     GLGGRCEQVK LGTAEGPAYT TTMDGQYTYI SIEVEAGLSD DAWDDRLNLA IKTHSQNPSL
     SQAVLYTSYS LSEAWPGQVV PCRSIWGRGG RKLGAGIILQ QSH
//