ID C1G7K1_PARBD Unreviewed; 837 AA.
AC C1G7K1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 24-JAN-2024, entry version 58.
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=PADG_03156 {ECO:0000313|EMBL:EEH47058.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH47058.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH47058.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH47058.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275959; EEH47058.2; -; Genomic_DNA.
DR RefSeq; XP_010758286.1; XM_010759984.1.
DR AlphaFoldDB; C1G7K1; -.
DR STRING; 502780.C1G7K1; -.
DR GeneID; 22582518; -.
DR KEGG; pbn:PADG_03156; -.
DR VEuPathDB; FungiDB:PADG_03156; -.
DR eggNOG; KOG2316; Eukaryota.
DR eggNOG; KOG2317; Eukaryota.
DR HOGENOM; CLU_010289_2_0_1; -.
DR InParanoid; C1G7K1; -.
DR OMA; HCRLAQS; -.
DR OrthoDB; 103959at2759; -.
DR Proteomes; UP000001628; 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 PANTHER; PTHR12196:SF2; DIPHTHINE--AMMONIA LIGASE; 1.
DR PANTHER; PTHR12196; DOMAIN OF UNKNOWN FUNCTION 71 DUF71 -CONTAINING PROTEIN; 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:UP000001628}.
FT REGION 72..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 91037 MW; 63C0EAD05F4558EC CRC64;
MSQQLNIIAL ISGGKDSLYS LLHCLKNGHK VVALANMHPP LRPKPGPNYA AYFATGTLDA
GDQDGCVVQK GRVGQEEGNS NEDDAQQEQE DEEEEEEDLE SYMYQTVGHS IIPLYESALD
IPLYRAPIQG TALNTSRDYH TPTSPPPSSQ PSTPIPESAD ETESLFHLLK HVMKHHPTAN
AVCAGAILST YQRTRVENIA SRLGLIPLAW LWMYPTLPPP AERAKTPRNS PAAVAGLLED
MAACGCEARI VKIASGGLDV DDLWANVAGG DGHGGGSVVR ERLVKGMGRF VGEGEVHGAV
LGEGGEYETI ALDGPGVLWR KKIVVRSVER RIGEGGVAAA RITGARCVPK EGGGEGGLGL
VRVPQVFDAE FKGLLSDMVL RLKQYDDFQE EELQNRMLRG DDEVWKADIS QTQGENVWTI
SNVSVPEVGA GAANQMKAIV QKLEDITRQS ATRDIVFATI LLRSMDDFAL INPIYASLFT
NPNPPARVTV ACGDSLPPGV DVIASFVIDM LPREGRLGLH VQSRSYWAPA NVGPYSQAQC
IPLHKGAKID RDGGVIYVAG QIPLDPGSMD LYNPLPTQES SGWFSPFVSR TILSLQHLWR
IGKVMEADWW LGGVAFLAGD EKIPSKAKVA WDIWEHMNRD PSSSNAGDDK GDGGDGAPEF
DAWDLKYGNH RDLGHSSSNG TKKNLPNFDI VRGSIFTPPF FAVQVDALPR ASDIEWQGLG
TRTDTLAIYE KTQPGKHWII SHLQGAGFGS FYYIGIQCGD QPDRDLEGHV QDAMDAVKAR
ENDTQSGNID HINFTIYTSH SLSESVWQQG QIVPCKSLWG QRGKKLAAGI VVHVRLK
//
