ID A0A0V1LLX4_9BILA Unreviewed; 1869 AA.
AC A0A0V1LLX4;
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};
GN Name=ers-1 {ECO:0000313|EMBL:KRZ60504.1};
GN ORFNames=T02_7149 {ECO:0000313|EMBL:KRZ60504.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ60504.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ60504.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ60504.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ60504.1}.
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DR EMBL; JYDW01000028; KRZ60504.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1LLX4; -.
DR Proteomes; UP000054721; 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:KRZ60504.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1869
FT /note="glutamine--tRNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006881902"
FT DOMAIN 1096..1253
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04558"
FT DOMAIN 1257..1344
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04557"
FT DOMAIN 1353..1652
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 1655..1754
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 1770..1846
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 163..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1869 AA; 212261 MW; 209C678677AFBDE0 CRC64;
MIYFYSRHES CREVNVALLL FLDFHILCTA MDNESRADVE PSQRSKKLNV AIATESVECA
AVDRFVEACD PAEDPAPSFA KKVLLGFPEI ECDSGTESDE ELERIETNSI ASLAVSQTSD
YYASQPSWSV SSCLSRIDSP LCFTLSDQDL NCWENLSIST SPSQNLEDAR ESSSASNCAV
GQSDPQLPTH HYHTRQQLQR LKREILNNEM PTKSSYGADE VDSNDGEVDL YQRTAFVPFK
KCRGLLEPLQ SGLRSNGSKT ATMNNRLSSK SDILESVTAA AMRRTAPIKL IIPPPLKLES
AESRQHHSFD ETVGSLSTNG CRKRVRSDEG DQPQTSTGYF RARPCLNFEK MREKMVKPNR
KKPSIATGAE GAAKAKMKLR LLEEFDLNKL DFGSIDDEQL DLFLCWENLS ISTSTSQNLE
DARESSSASN CAVGQSDPQL PTHHYHTRQQ LQRLKREILN NHMPTKSCYG ADEVDSNDGE
VDLYQRTAFV PFKKCHGRLE QQQTSDHSKH TEMKLIILPP FKLETDKSRQ QHSMDETVGS
LSTNGYRKRV YDQMKKMKYW PHTVHFIANC VCICLRSSIQ YLVTISFMSG VSDDVDDEFW
NDSNVSSFCF DDFPSDTAKI IEEIGAELNK LDLNSTDDEE LGLFGGDHLT SSFNDEMSSV
SNSQTPSDLR SISSETTEQR TTPLSVQATQ PDSDDYKRLQ AECSRLRSKW TELQCRLKQE
KYFAPDFEET IGRLATGEIY IFQYYRRLSD KKQLLKTAID FGDGDAICCV VLFLERTLSP
VVFRQLLLEF PPAVSHYIFY LKQLSMNDKL SELLLSLGLV EQLAAVEVSR ICSEKNAESK
IALLRKALAG GVFADPSLNE ERMFLNSYAD LLEHQLPIDA ADNSARVEGG LKNENSVVDS
SVLETLMYCC RLHYELPSNS LASPLSIRNK FGLTEQQFDW IAIKALAERQ QWAEIQKLLL
RKGLFGKQKL KLPISCEQLL NVLYSNGATA SVSSKHSSND ITIYIDLFSD NQRKLMLAKK
YKCHALVIKI LIGLKDRLEL LKYMATLSPS SVELSTAETA LTNSIILENS NVIVLLRIKK
LHFLIHNFRM AFADNNQLLS ALGLSGEKIK ETLRNETLTA SLSNMANQAL KITNGKLSES
QGKLLYQTAT RLKKQCFQYA ELLIEEICNN RLENDLQLSA ALQFLLSHAA SDFDKAEFEQ
ACGIGVKVTE EQIEDTVASV IKANEEKLQL MRYKFPISSL IAEVRKVLPW ADGSKLKKEI
DMQMLILLGP KTLDDMQSGK KIPSKVMPKE KLKAKEIAKN EESEFEGAAT IEELMKTKAH
FHKPGENYKT EGYVVTPKTM DLLKRHLEIT GGKVVTRFPP EPNGILHIGH AKAINIDFGY
AKAHGGICYL RYDDTNPEKE EERYFTAIRE MVEWLGYTPY KVTHSSDYFD QLYEYALELI
RRGHAYVCHQ KAEEVKGINP TPSPWRDRPI NESLKLFEDM KNGMFDEGAA TLRMKITLEE
GKVDPVAYRI KYVPHHRTGN KWCIYPTYDY THCLCDSIEN ITHSLCTKEF QSRRSSYYWL
CNALDLYCPV QWEFARLNVH YAVISKRKII KLVQENIIRD WDDPRLFTLT ALKRRGFPPQ
AINNFVAKMG LTTALTAVDP MMLEACVRDV LNVTAPRHMA VLNPLKVRFA NPVELPKMVE
VPDFPNTLSD KSKGKHHVQF DSTIFIEADD FKEHADDKHF KRFTSTQAVG LKYVGLVMIL
QEIKKNHLGE FMELIVKVEK LTEQNKPKCF IHWVAKPISC EVRLYERLFH HRNPEDSNEV
PGGFLTDVNK DSLHVINDAY IDESLRRCAK VESRFQFERV GFFVVDPDST DTKLVFNRTV
SLKEDVRKT
//
