ID A0A498IFV1_MALDO Unreviewed; 1883 AA.
AC A0A498IFV1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=glutamate--tRNA ligase {ECO:0000256|ARBA:ARBA00012835};
DE EC=6.1.1.17 {ECO:0000256|ARBA:ARBA00012835};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030865};
GN ORFNames=DVH24_036421 {ECO:0000313|EMBL:RXH82080.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH82080.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH82080.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH82080.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory photoreceptor which exists in two forms that are
CC reversibly interconvertible by light: the Pr form that absorbs
CC maximally in the red region of the spectrum and the Pfr form that
CC absorbs maximally in the far-red region. Photoconversion of Pr to Pfr
CC induces an array of morphogenic responses, whereas reconversion of Pfr
CC to Pr cancels the induction of those responses. Pfr controls the
CC expression of a number of nuclear genes including those encoding the
CC small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B
CC binding protein, protochlorophyllide reductase, rRNA, etc. It also
CC controls the expression of its own gene(s) in a negative feedback
CC fashion. {ECO:0000256|ARBA:ARBA00002479}.
CC -!- SIMILARITY: Belongs to the phytochrome family.
CC {ECO:0000256|ARBA:ARBA00008235}.
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:RXH82080.1}.
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DR EMBL; RDQH01000338; RXH82080.1; -; Genomic_DNA.
DR STRING; 3750.A0A498IFV1; -.
DR Proteomes; UP000290289; Chromosome 12.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR CDD; cd00807; GlnRS_core; 1.
DR CDD; cd10289; GST_C_AaRS_like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR013516; Phyto_chromo_BS.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR049437; tRNA-synt_1c_C2.
DR NCBIfam; TIGR00463; gltX_arch; 1.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43097:SF5; GLUTAMATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS00245; PHYTOCHROME_1; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606}.
FT DOMAIN 218..391
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 618..688
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 748..803
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 902..1119
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1883 AA; 209886 MW; DFB9C186E6A7823E CRC64;
MSSSRPSNSS SNPGRSRHSS RIIAQTTVDA KIHADFEESG GSFDYSNSVR VGSSVGGDQQ
PRSDKVTTAY LHNIQKGKTI QPFGCLLALD EKTFKVIAYS ANAPEMLTTV SHAVPSVGES
PVLGIGTDIR TIFTAPSASA LHKALGFGEV SLLNPILVHC KTSGKPFYAI THRVTGSLII
DFEPVKPYEV PMTAAGALQS YKLAAKAIAR LQSLPSGSME RLCDTMVQEV FELTGYDRVM
TYKFHDDDHG EVVSELTKPG LEPYLGLHYP STDIPQAARF LFMKNKVRMI VNCGAKLVKV
FQDEKLPLDL TLCGSTLRAP HSCHLEYMKN MNSIASLVMA VVVNEGDDEV RDRDSVPPQK
RKRLWGLVVC HNTSPRFVAF PLRYACEFLT QVFAIHVNKE IEMEDQMVEK NILRTQTLLC
DMLLRDAPLG IMSQSPNVMD LVKCDGAALL YKNKVWRLGM TPNDFQLHDI ASWLSEDHMD
STGLSTDSLY DAGFPGALAL GDVVCGMAAV WITSKDVLFW LRSHTAAEIR WGGAKHETGE
KDDGSKMHPR SSFKAFLEVV KTRSLPWKDY EMDAIHSLQL ILRNAFKDVE TTLEANTKAI
NVRLSDLKLE GMEELEAVTS EMVRLIETAT VPILAVGVDG LVNGWNTKID ELTGLPVDEA
IGKHLLTLVE DSSTSVVKKM LDSALRGKEE QNIQFEIKTH GSRADLGPIS LVVNACASRD
IRENVVGVCF VAQDITGQKN VMDKFTRIEG DYKAIVQNPS PLIPPIFGTD EFGWCSEWNS
AMTKLTGWKR EEVMDKMLLG EVFGINMACC PLKSQESFVN LGVVLNHAMT GQVSEKLPFG
FCARSGKHIE CLLCVSKKLN SEGSVTGVFC FLQLASPELQ QALNVQRLSE QTAVKRLKEL
SYIRRQIRNP LAGIIFSRKM MEDTELGAEQ QRLLHTSAQC QHQLNKILDD SDLDTIIDGY
LDLEMVEFTL HEVLNAAVSQ VMIKSNAKSV RIVHNAAEDI MTETLYGDSL RLQQVIADFL
AVSVSFMPTG GQLTIEANLT KDRLGRSVQL VHLELRITHA GGGIPEGLLN QMFGNNGDIS
EEGISLLISS KLVKLMNGDV RYLREEGRST FMISVELAAA HKITLEQCVK KNNIKRNAAN
QATSPGAKST PWIQMMDIKA VSFAAENPPL AELLAAKLAG ISLPTDASLP PDSLYSLQFS
NGLKLHGKNV LLRYIGRIAK LYGDNPFEAG KIDEWLEYAP VLSQGSAFES ACKHLDDYLG
SSTFFANQSL SIADIAIWSG LAGTGKRWES LRNSKKYPNL SRWFNSLLAE YGDALNEVTA
TFIGKKGSGK PTATKTKGTQ ADQQLKSVNG DVSEKGKAGS KPTSEVDLPE AEVGKVRLRF
APEPSGYLHI GHSKAALLNQ YFAQRYKGQL IVRFDDTNPD KESNEFVDNL LKDIETLGIK
YETVTYTSDY FPQLMEMAEN LIRQGKAYVD DTPREEMKKE RMDGIESKCR NNSVEENLKL
WNEMIAGSKR GKECCVRGKL DMQDPNKSLR DPVYYRCNPT PHHRIGSKYN LYPTYDFACP
FVDSIEGITH ALRSSEYHDR NAQYYRVQED MGLRKVHIYE FSRLNMVYTL LSKRKLLWFV
QNEKVSGWDD PRFPTVQGIV RRGLKVEALI QFILEQGASK NLNLMEWDKL WTINKKIIDP
VCPRHTAVIE ERPVLLTLTN GPEKPFVRII PRHKKYEGAG EKATTYTRRI WLDHADAESI
KVDEEVTLMD WGNAIVKGIE KDTDGNLKLT GVLHPEGSVK TTKLKLTWLP ESDELVKLSL
MEFDHLITKK KLEEDEDFVD VVNPCTEKET AALGDSNMRN LKCGDILQLE RKGYFRCDVP
YLRPSKPVVL FAIPDGRQQT GSK
//
