ID A0A0V0YAS6_TRIPS Unreviewed; 1286 AA.
AC A0A0V0YAS6;
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=vipas39 {ECO:0000313|EMBL:KRX97359.1};
GN ORFNames=T4E_4372 {ECO:0000313|EMBL:KRX97359.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX97359.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX97359.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX97359.1};
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:KRX97359.1}.
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DR EMBL; JYDU01000032; KRX97359.1; -; Genomic_DNA.
DR EMBL; JYDU01000032; KRX97362.1; -; Genomic_DNA.
DR Proteomes; UP000054815; 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:KRX97359.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815}.
FT DOMAIN 513..670
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04558"
FT DOMAIN 674..761
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04557"
FT DOMAIN 770..1069
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 1072..1173
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 1187..1263
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 72..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1286 AA; 147287 MW; A4D6711807EFAD58 CRC64;
MVHFMSGVSV DVDDEFWNDS NVSSFCFDDF PSDTAKIIEE IGAELNKLDL NSIDDEELCL
FCGDHLTSSF NDEASSVSNS QTPSDLRSIS SETTEQRTTP LSVQATQPDS DDYKRLQAEC
SRLRSKWTEL QCRLKQEKYY APDFEETIGR LATGEIYIFQ YYRRLSDKKK LLKTAIDFGD
GDAICCVVLF LERTLSPVVF RQLLLEFPPA VSHYIFYLKQ LSMHDKLSEL LLYVYYYYAN
LYNRRKNHFV RSLGLVEQLA AVEVSRICSE KNAESKIALL RKALAGGVFS DQSLNEERIF
LNSYADLLEH QLPIDAADNN ARVEGNLKNE VSVVDSSVLE TLMYCCRLHY ELPSNSLASP
LSIRNKFGLT EQQFDWIAIR ALAERQQWSE IQKLLLRKGL FGKQKLKLPI SCEQLLNVLY
SNGATASDIT IYIDLFSDNQ RKLMLAKKYK CHALVIKILI GLKDRLELLK YMATLSPSSV
ELSTAETALT NSTEQAIFIF VFSFSCMAFA NHNQLLSALG LSEDKIKETL RNETLTASLS
NIANQALKIT DGKLSESQGK LLYQTATRLK KQCMQHADLL IEEICNNRLE NDLQLSAALQ
FLLSHAASDF NKAQFEQACG IGVKVTEEQI EDTVASVIKA NEEKLQLMRY KFPISSLIAE
VRKVLPWADG SKLKKEIDMQ MLILLGPKTL DDMQSGKKIP SKVMPKEKLK TKEIARNEES
EFEGAATIEE LMKTKAHFHK PGENYKTEGY VVTPKTMDLL KRHLQITGGK VVTRFPPEPN
GILHIGHAKA INIDFGYAKA HGGICYLRYD DTNPEKEEER YFTAIREMVE WLGYTPYKVT
HSSDYFDQLY EYALELIRRG YAYVCHQKAE EVKGINPTPS PWRDRPIEES LKLFEDMKNG
MFDEGAATLR MKITLEEGKV DPVAYRIKYV PHHRTGNKWC IYPTYDYTHC LCDSIENITH
SLCTKEFQSR RSSYYWLCNA LDLYCPVQWE FARLNVHYAV ISKRKIIKLV QENFIRDWDD
PRLFTLTALK RRGFPPQAIN NFVAKMGLTT ALTSVDPMML EACVRDVLNV TAPRHMAVLK
PLKVRIANLV ELPKTVEVPD FPNTLSDKST GKHHVQFDST IFIEADDFKE HADDKHFKRF
TSTQTVGLKY VGLVLILQEI KKNQMGEFVE LIVKVEKLTE QNKPKCFIHW VAKPISCEVR
LYERLFHHRN PEDSNEVPGG FLTDINKNSL HVINDAYIDE SLRRCAKVES RFQFERVGFF
VVDPDSTDTK LVFNRTVSLK EDVRKT
//
