SYQ_DICDI
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 03-AUG-2022, entry version 133.
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 (Slime mold).
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};
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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.DDB0201644; -.
DR PaxDb; P14325; -.
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; -; 1.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 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_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR Pfam; PF04557; tRNA_synt_1c_R2; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00440; glnS; 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
