ID A0A0D3FBW5_9ORYZ Unreviewed; 1170 AA.
AC A0A0D3FBW5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART02G36790.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART02G36790.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART02G36790.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART02G36790.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0D3FBW5; -.
DR STRING; 65489.A0A0D3FBW5; -.
DR PaxDb; 65489-OBART02G36790-1; -.
DR EnsemblPlants; OBART02G36790.1; OBART02G36790.1; OBART02G36790.
DR Gramene; OBART02G36790.1; OBART02G36790.1; OBART02G36790.
DR eggNOG; KOG1164; Eukaryota.
DR eggNOG; KOG2316; Eukaryota.
DR eggNOG; KOG2317; Eukaryota.
DR HOGENOM; CLU_002930_0_0_1; -.
DR Proteomes; UP000026960; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017178; F:diphthine-ammonia ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 CDD; cd14125; STKc_CK1_delta_epsilon; 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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002761; Diphthami_syn_dom.
DR InterPro; IPR030662; DPH6/MJ0570.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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; PF00069; Pkinase; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55298; YjgF-like; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 301..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1170 AA; 129566 MW; E6B1542BE2237F02 CRC64;
MDHVVGGKFK LGKKIGSGSF GELFLAVNVQ TGEEVAVKLE NVKTKHPQLH YESKLYMLLQ
GGTGIPHLKW FGVEGEYNVM VIDLLGPSLE DLFNYCSRKF SLKTVLMLAD QMINRVEYMH
QKGFLHRDIK PDNFLMGLGR KANQVYIIDY GLAKKYRDLQ THKHIPYREN KNLTGTARYA
SVNTHLGVEQ SRRDDLESLG YVLMYFLRGS LPWQGLKAGT KKQKYDKISE KKMLTPVEVL
CKSYPSEFIS YFHYCRSLRF EDKPDYSYLK RLFRDLFIRE GYQFDYVFDW TILKYPQIGS
KPLMRPSERT SGAAGPSMEK MEKAPGEASG RRNPTGSLNQ SDNYAQRPSM SLKEIMHSTD
RSGERTVERP RTSSRTGSAS RRAVASSSRP GSSVEPMEQQ YSRTSRLFSS SGSRPSSTQR
VNPSVGETRA TSLSRAAVAR GSRDEPLHRS LELLSLGGVN EEIFLAWAPR THLRGPIVAL
ANLIPEDDAV DELDSYMYQT MKFDAISLIG LACREQGLKY NVTTGDEVED MFVLLSEVKR
QIPSITAVSS GAIASDYQRL RVESVCSRLG LVSLAYLWKQ DQTLLLDEMI RRGIVAIIVK
VAAMGLKPSA HLGKELAELK CHLLQLNESY GINVCGEGGE YETLTLDCPL FRNARIVLDD
FEVILHSPDS IAPVGILHPL KFHLEHKPNS FGTVGDSATA QENSSYLYEV DGAISHSDVE
KKQETLSPVT TVDACTNIDL CISKTGKKLF SIGCWIQDPC GTSEGLKTDL VAVLSRIENQ
LKEEGLGWMN VLYVHLFISS MKEFGLANEV YVSFITEQKC PLGVPSRSTV ELPLVQVGLG
HAYVEVLVTK EQVKRVLHVQ SISCWAPSCI GPYSQATLHG EILYMAGQLG LDPPTMKLCP
GGPTAELEFA LRNSEAVANA FGCSIFSSAI HFLVYCSAHL TSSEKEQVEH TLRSSYITSL
DCSNTGSYPT ILYVFASDLP KGAYVEIKPI LYVPSPTNDD GVPTREQEAG GSLPASSEAF
SAWSAQYSDL DDSCCQVHTI GGKICSAVVS VTNDIALKIC STTEQLYHSE EHLKALARFC
AFQLAKILID NGFSWDNLTM LRFYYSVEHP VTADVMSRVF SEAFAELEEG GVGSCTPDGV
PIFNIVPVSA SGCFTSLSDI ISCELLASKV
//