ID A0A1V6TWV3_9EURO Unreviewed; 762 AA.
AC A0A1V6TWV3;
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=PENFLA_c003G00511 {ECO:0000313|EMBL:OQE30299.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE30299.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
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:OQE30299.1}.
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DR EMBL; MLQL01000003; OQE30299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TWV3; -.
DR STRING; 254877.A0A1V6TWV3; -.
DR OrthoDB; 103959at2759; -.
DR Proteomes; UP000191342; 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:UP000191342}.
FT DOMAIN 12..283
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 762 AA; 83322 MW; 6601A26F5ECA0E57 CRC64;
MSAAQPSAPG LNVIALISGG KDSLYSILHC IRNGHKVVAL ANLYPEPQNK TSTNPKHLRH
DEEDDIDSFM YQTIGHNIIP LYETALQIPL YRQPITGGAV DTSRIYGTKP SEKDETESLV
PLLQRIKKAH PEANAVSAGA ILSTYQRTRI ENVANRLGLV PLAWLWMYPS LPAPPARSAD
TLAIRQAGLL EDMAAARCDA RIIKVASGGL DEGFLWENVS GAGSGGRMMR RYLVKAMSRF
AAAEDIRGAV LGEGGEYETL ALDGPGFLWK QRIEVGSREE KVGEGGVAFV RLRGARCTAK
SVWEIGDGIA PSDIRRPGLL DAVFEGVLGS ALDFSGSRDD SKSRAMTSTA RSPDWPVCEP
VHRLSGSTWT ISNIVAPEAG PGAGEQMKAI AHKVQKVFKS FSHPKSGSRS TDDIVFATVL
LNSMADFGSM NDIYVSLFKK PNPPARVTVA CGDRLPSNVK VMVTFVVDLG ARDRRQGLHV
QSRSYWAPAN IGPYSQALSV PLQNASRIVY IAGQIPLDPG SMDLAQVEGP GSWAENYRLR
AVLALQHLWR IGEAMQVNWW LGAVAFLARG EHANTQAQVA WRLWERMHAL PDNEDEDDDD
GPQLDAWDIK YGRRTEELTD APVPSLPQFT ALVVSHTSIP PFLAVQVDEL PRGSDIEWQG
LGGRCEQVKL DIKGGTSSTT MDNQYKYTNI EIDAGSSDET LKQILRSVNE AYRRDSSLSQ
AVLYTTYPVP EPLWPVQVVP CRSVWGREGR RLSAGVVLQQ LS
//