ID   A0A084QTT9_STAC4        Unreviewed;       805 AA.
AC   A0A084QTT9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   28-JUN-2023, entry version 31.
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=S40285_00262 {ECO:0000313|EMBL:KFA67374.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA67374.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA67374.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA67374.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
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; KL660192; KFA67374.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084QTT9; -.
DR   STRING; 1283841.A0A084QTT9; -.
DR   HOGENOM; CLU_010289_2_0_1; -.
DR   InParanoid; A0A084QTT9; -.
DR   OMA; HCRLAQS; -.
DR   OrthoDB; 103959at2759; -.
DR   Proteomes; UP000028524; 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; 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; 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:UP000028524}.
FT   DOMAIN          77..285
FT                   /note="Diphthamide synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01902"
FT   REGION          52..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   805 AA;  86860 MW;  156C353728122AE2 CRC64;
     MASDGLKVVA LVSGGKDSFF SLLHCIHHGH DVVALANLFP ASGPDQSFEV DYIDPNAPAP
     TSPTDQGTGT APASDLNSFM YQTVGHEIVP LYAAATGLPL YRQPIQGGAE THERDYDHAA
     GSRASSLQDE AESMLSLLQA VKAHHPDANA VCAGAILSTY QRTRVESIAL RLGLVPLAYL
     WKYPVLPPPS VPADEAQLLR DMAAAQLQAR IIKVASAGLD ETHLWEHITS DVGAARIKRA
     LARFGTGEGA VLGEGGEFET VVVDGPAHLF KKRICVPAEE KKVVAEEGGT SWLMLRGAYL
     EDKHTDTAEP LPKALRIPEL LDARFRNVLE GLQLENNETN FVEQASPSAL LKGTAPLCSD
     RTEMRHLTVL ANPGTHDGTI QAEIVSVVDE IRHLMSSASL NPSDITTATI ILRDMADFPG
     LNAEYGKLFR KPNPPSRVTI SCGPLLPDGH NIVVYLTLPS LPDNSSRNGL HVQSRSYWAP
     ANIGPYSQAT DVPVISGGQQ TGLRCIFVAG QIPLIPATML LPPPSDTSLQ LQIVLSLQHL
     WRISAQMKIQ YFTSAVAYFA RSSSSDEMQQ NAKHAGLAWK LVHADTLEDD EDADDGLDPW
     DLKYNPQYAS LSSSGPETAA ISMPDLSILT LQQRNRTESH IPPFFAAEVE SLPRDSAVEW
     HGHIGLSGAS QGSAELCYYP NIDAMGWAAN HVLVRTSDGI FIHTALHCPN SDDGGFTSWN
     MLEEALKTAY RGALQGLGVK ATDDNSTNHP YLLYVDASKL KFAWSKYEEG YASVPFAIIP
     CRSLWSHAGK GIGCVALYKT IVGGA
//