ID SYQ_DICDI Reviewed; 779 AA. AC P14325; Q54HF7; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 2. DT 24-JAN-2024, entry version 138. DE RecName: Full=Probable glutamine--tRNA ligase; DE EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897}; DE AltName: Full=Glutaminyl-tRNA synthetase; DE Short=GlnRS; DE AltName: Full=Vegetative-specific protein H4; GN Name=glnS; Synonyms=cinA, H4; ORFNames=DDB_G0289481; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-288. RC STRAIN=AX3; RX PubMed=2602140; DOI=10.1093/nar/17.23.9679; RA Singleton C.K., Manning S.S., Ken R.; RT "Primary structure and regulation of vegetative specific genes of RT Dictyostelium discoideum."; RL Nucleic Acids Res. 17:9679-9692(1989). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L- CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662, CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521, CC ChEBI:CHEBI:456215; EC=6.1.1.18; CC Evidence={ECO:0000250|UniProtKB:P47897}; CC -!- DEVELOPMENTAL STAGE: This protein is expressed in growing cells and CC deactivated upon the initiation of development. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA33446.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAFI02000141; EAL62672.1; -; Genomic_DNA. DR EMBL; X15388; CAA33446.1; ALT_FRAME; Genomic_DNA. DR PIR; S07563; S07563. DR RefSeq; XP_636180.1; XM_631088.1. DR AlphaFoldDB; P14325; -. DR SMR; P14325; -. DR STRING; 44689.P14325; -. DR PaxDb; 44689-DDB0201644; -. DR EnsemblProtists; EAL62672; EAL62672; DDB_G0289481. DR GeneID; 8627167; -. DR KEGG; ddi:DDB_G0289481; -. DR dictyBase; DDB_G0289481; glnS. DR eggNOG; KOG1148; Eukaryota. DR HOGENOM; CLU_001882_2_3_1; -. DR InParanoid; P14325; -. DR OMA; FAWRIMG; -. DR PhylomeDB; P14325; -. DR PRO; PR:P14325; -. DR Proteomes; UP000002195; Chromosome 5. DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004819; F:glutamine-tRNA ligase activity; ISS:dictyBase. DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; ISS:dictyBase. DR Gene3D; 1.10.10.2420; -; 1. DR Gene3D; 1.10.8.1290; Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1, domain 1; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004514; Gln-tRNA-synth. DR InterPro; IPR007638; Gln-tRNA-synth_Ib_RNA-bd_2. DR InterPro; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N. DR InterPro; IPR042558; Gln-tRNA-synth_Ib_RNA-bd_N_1. DR InterPro; IPR042559; Gln-tRNA-synth_Ib_RNA-bd_N_2. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd. 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; TIGR00440; glnS; 1. DR PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1. DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 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 Pfam; PF04558; tRNA_synt_1c_R1; 1. DR Pfam; PF04557; tRNA_synt_1c_R2; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 2: Evidence at transcript level; KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1..779 FT /note="Probable glutamine--tRNA ligase" FT /id="PRO_0000195862" FT BINDING 268..270 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00962" FT BINDING 274..280 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00962" FT BINDING 300 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00962" FT BINDING 440 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00962" FT BINDING 459 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00962" FT BINDING 488..489 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00962" FT BINDING 496..498 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00962" FT CONFLICT 219 FT /note="L -> F (in Ref. 2; CAA33446)" FT /evidence="ECO:0000305" SQ SEQUENCE 779 AA; 88426 MW; 2249628C92988AD1 CRC64; MSTKPTINKD ELVTLFSQIG LDSSKAKETT NNATLSSNLQ EIIKEAGAES GCEKSVGLLL YTLATKYPAN AMKHRATLVD YIANKKSVNS INLQACLDYL RRTANEELNV AEFEQSCGVG VVITREQVAQ AVSDYINKNK SDLLEKRYQF NIGGILMEIK NSLKWANAKD IKEEVDAAIL SLLGPKTDAD KAPPAKPVKP TTPTAVATTT AATTTTGDLS PIIPAELKPA KEEIKFPDPS DNIQNTPKLL ADHLKTTGGK IVTRFPPEPN GYLHIGHAKA MHLNFGYAKK NGGKCYLRFD DTNPEKENQE YIDSIIDSVK WLGHEPCEIT YSSSQFDTLY EMANELIRRG YAYVCHQTAS EISEGREKMT DSPYRNRTVE ENLKLFEDMR LGKFEEGKAI LRMKGDMKHP NPCMRDLIAY RIKYHHHPMS GDKWCIYPSY DYTHCLVDSI ENITHSLCTL EFEIRRLTYN WLIDVLGLYR PVVWEYARLN LTHTVLSKRK IITLVQNKIV NGWDDPRLST LNAFRRKGYT PEAINLLCDT IGVTRTNGTT ISYELLELCC RQDLDGKATR AMAVFDPIKV VITNYPEDKS EEINAPNIPS KPEKGTHKID FSRIVYIERS DFRMEDNKDF FGLAPGKEIL LKYAYNIKCE KVIQDADGKV TELHVTYDKD NSSKKLKTIH WVSSVAGTEP MKAEVRLYEH LFKDSEIGDD WLNNINPNSL RIIPNAFIDK TVLASKEYDR YQFERVGYFV VDKDTTSDKM VFNRTVSLKE NKEKSKSRN //