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Database: UniProt
Entry: A0A0V0SEP6_9BILA
LinkDB: A0A0V0SEP6_9BILA
Original site: A0A0V0SEP6_9BILA 
ID   A0A0V0SEP6_9BILA        Unreviewed;       807 AA.
AC   A0A0V0SEP6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
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:KRX24757.1};
GN   ORFNames=T07_493 {ECO:0000313|EMBL:KRX24757.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX24757.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX24757.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX24757.1};
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, ECO:0000256|RuleBase:RU363037}.
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:KRX24757.1}.
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DR   EMBL; JYDL01000016; KRX24757.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0SEP6; -.
DR   Proteomes; UP000054630; 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   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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363037};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363037};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363037};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363037};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT   DOMAIN          34..191
FT                   /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT                   RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04558"
FT   DOMAIN          195..282
FT                   /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT                   RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04557"
FT   DOMAIN          291..590
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          593..692
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   DOMAIN          708..784
FT                   /note="tRNA synthetases class I (E and Q) anti-codon
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF20974"
SQ   SEQUENCE   807 AA;  92726 MW;  B2DCFA1B6B048486 CRC64;
     MTIMEEKLSM SIDNSIEYGK FWKIQIRMAF ADNNQLLSAL GLSGEKIKET LRNETLTASL
     SNMADQALKI TNGKLSESQG KLLYQTATRL KKQCFQYAEL LIEEICTNRL ENDLQLSAAL
     QFLLSHAASD FDKAEFEQAC GIGVKVTEEQ IEDTVASVIK ANEEKLQLMR YKFPISSLIA
     EVRKVLPWAD GSKLKKEIDM QMLILLGPKT LDDMQSGKKI PSKVVPKEKL KAKETAKNEE
     SEFEGAATIE ELMKTKAHFH KPGENYKTEG YVVTPKTMDL LKRHLEITGG KVVTRFPPEP
     NGILHIGHAK AINIDFGYAK AHGGICYLRY DDTNPEKEEE RYFTAIREMV EWLGYTPYKV
     THSSDYFDQL YEYALELIRR GHAYVCHQKA EEVKGINPTP SPWRDRPIDE SLKLFEDMKN
     GMFDEGAATL RMKITLEEGK VDPVAYRIKY VPHHRTGNKW CIYPTYDYTH CLCDSIENIT
     HSLCTKEFQS RRSSYYWLCN ALDLYCPVQW EFARLNVHYA VISKRKIIKL VQENIIRDWD
     DPRLFTLTAL KRRGFPPQAI NNFVAKMGLT TALTAVDPMM LEACVRDVLN VTAPRHMAVL
     NPLKVRFANP VELPKMVEVP DFPNTLSDKS PGKHHVQFDS TIFIEADDFK EHADDKHFKR
     FTSTQAVGLK YVGLVMILQE IKKNHLGEFM ELIVKVEKLT EQNKPKCFIH WVAKPISCEV
     RLYERLFHHR NPEDSNEVPG GFLTDVNKDS LHVINDAYID ESLRRCAKVE SRFQFERVGF
     FVVDPDSTDT KLVFNRTVSL KEDVRKT
//
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