ID A0A0V1D7B6_TRIBR Unreviewed; 1808 AA.
AC A0A0V1D7B6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030466};
DE Flags: Fragment;
GN Name=ers-1 {ECO:0000313|EMBL:KRY57355.1};
GN ORFNames=T03_16604 {ECO:0000313|EMBL:KRY57355.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY57355.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY57355.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY57355.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000948};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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:KRY57355.1}.
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DR EMBL; JYDI01000032; KRY57355.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1D7B6; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00807; GlnRS_core; 1.
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 Gene3D; 1.10.150.780; Vps16, C-terminal region; 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 InterPro; IPR038132; Vps16_C_sf.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRY57355.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 1036..1192
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04558"
FT DOMAIN 1196..1283
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04557"
FT DOMAIN 1292..1591
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 1594..1693
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 1709..1785
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 169..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY57355.1"
SQ SEQUENCE 1808 AA; 204729 MW; 170E20A858E7472F CRC64;
LSANCIVRNF QIRHESCREV NVALLLFLDF HILCTAMDNE SRADVEPSQR SKKLNVAIAT
ESVECAAVDR FVEACDPAED PAPSFAKKVL LGFPEIECDS GTESDEELER IETNSIASLA
VSQTSDYYAS QPSWSVSSCL SRIDSPLCFT LSDQDLNCWE NLSISTSPSQ NLEDARESSS
ASNCAVGQSD PQLPTHHYHT RQQLQRLKRE ILNNEMPTKS CYGADEVDSN DGEVDLYQRT
AFVPFKKCRG LLEPLQSGLR SNGSKTATMN NTLSSKSDIL ESVTAAAMRR TAPIKLIIPP
PLKLESAESR QHHSFDETVG SLSTNGCRKR VRSDEGDQPQ TSTGYFRARP CLNFEKMREK
MVKPNRKKPS IATGAEGLEQ RVPIAVFWQF LVPVTEHCQF CLLSTGPNWE NLSISTSPSQ
NLEDARESSS ASNCAVGQSD PQLPTHHYHT RQQLQRLKRE ILNNEMPIKS CYGADEVDSN
DGEVDLYQRT AFVPFKKCHG RLEQQQTSDH SKHTEMKLII LPPFKLETDK SRQQHSMDET
VGSLSTNGYS FMSGVSDDVD DEFWNDSNVS SFCFDDFPSD TAKIIEEIGA ELNKLDLNST
DDEELGLFGG DHLTSSFNDE MSSVSNSQTP SDLRSISSET TEQRTTPLSV QATQPDSDDY
KRLQAECSRL RSKWTELQCR LKQEKYFAPD FEETIGRLAT GEIYIFQYYR RLSDKKQLLK
TAIDFGDGDA ICCVVLFLER TLSPVVFRQL LLEFPPAVSH YIFYLKQLSM NDKLSELLLS
LGLVEQLAAV EVSRICSEKN AESKIALLRK ALAGGVFADP SLNEERMFLN SYADLLEHQL
PIDAADNSAR VEGGLKNENS VVDSSVLETL MYCCRLHYEL PSNSLASPLS IRNKFGLTEQ
QFDWIAIKAL AERQQWAEIQ KLLLRKGLFG KQKLKLPISC EQLLNVLYSN GATASVSRRR
MLMLILKVSV QDITIYIDLF SDNQRKLMLA KKYKCHALVI KILIGLKDRL ELLKYMATLS
PSSVELSTAE TALTNSLLSA LGLSGEKIKE TLRNETLTAS LSNMANQALK ITNGKLSESQ
GKLLYQTATR LKKQCFQYAG LLIEEICNNR LENDLQLSAA LQFLLSHAAS DFDKAEFEQA
CGIGVKVTEE QIEDTVASVI KANEEKLQLI RYKFPISSLI AEVRKVLPWA DGSKLKKEID
MQMLILLGPK TLDDMQSGKK IPSKVMPKEK LKAKEIAKNE ESEFEGAATI EELMKTKAHF
HKPGENYKTE GYVVTPKTMD LLKRHLEITG GKVVTRFPPE PNGILHIGHA KAINIDFGYA
KAHGGICYLR YDDTNPEKEE ERYFTAIREM VEWLGYTPYK VTHSSDYFDQ LYEYALELIR
RGHAYVCHQK AEEVKGINPT PSPWRDRPID ESLKLFEDMK NGMFDEGEAT LRMKITLEEG
KVDPVAYRIK YVPHHRTGNK WCIYPTYDYT HCLCDSIENI THSLCTKEFQ SRRSSYYWLC
NALDLYCPVQ WEFARLNVHY AVISKRKIIK LVQENIIRDW DDPRLFTLTA LKRRGFPPQA
INNFVAKMGL TTALTAVDPM MLEACVRDVL NVTAPRHMAV LNPLKVRFAN PVELPKMVEV
PDFPNTLSDK STGKHHVQFD STIFIEADDF KEHADDKHFK RFTSTQAVGL KYVGLVMILQ
EIKKNHLGEF MELIVKVEKL TEQNKPKCFI HWVAKPISCE VRLYERLFHH RNPEDSNEVP
GGFLTDVNKD SLHVINDAYI DESLRRCAKV ESRFQFERVG FFVVDPDSTD TKLVFNRTVS
LKEDVRKA
//