ID A0A0L8IF99_OCTBM Unreviewed; 822 AA.
AC A0A0L8IF99;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 ORFNames=OCBIM_22012309mg {ECO:0000313|EMBL:KOF99685.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF99685.1};
RN [1] {ECO:0000313|EMBL:KOF99685.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF99685.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF99685.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ415907; KOF99685.1; -; Genomic_DNA.
DR RefSeq; XP_014773405.1; XM_014917919.1.
DR AlphaFoldDB; A0A0L8IF99; -.
DR STRING; 37653.A0A0L8IF99; -.
DR EnsemblMetazoa; Ocbimv22012309m; Ocbimv22012309m.p; Ocbimv22012309m.g.
DR EnsemblMetazoa; XM_014917919.1; XP_014773405.1; LOC106871445.
DR GeneID; 106871445; -.
DR KEGG; obi:106871445; -.
DR OMA; TWCIYPM; -.
DR OrthoDB; 934at2759; -.
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}.
FT DOMAIN 39..199
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04558"
FT DOMAIN 202..302
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04557"
FT DOMAIN 312..610
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 613..713
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 724..799
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 220..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 822 AA; 93896 MW; AD237266FD5B2FC1 CRC64;
MAVAVELPRV ITSAFNKFRF YYFLFVLLRQ LDSDMASTEL LSLFTSIGLS EQKAKETCKN
AALSNTLRQC IENVQKLSGN SSIDKDVGKL LYNLSTKLKS QIYNKIPLLV EYIGKNKITS
DLQLDSALSY LLSNPTDPVD IKTFEESCGV GVSVTSDQVE TAVEKVIANY RDELLEKRYH
FNTGILMSEV RKALKWADGK TIKNEVDMQI LDLLGPKTDV DKAKPSKAKQ SKQTENIRTK
STTSVNQENK KTVNALENFV RADGEVKSFM DLVGSSVKFH KVGENFKTDG YVIMPRTMEL
LKQHLKETNS TVYTRFPPEP NGILHIGHAK AINFNFGYAR AMGGKCYLRY DDTNPEKEEE
KFFRGIREMV EWLGYKPWKI TYASDNFGKL YDLAVDLIKR GHAYVCHMKA EDLKGHNVVD
SPWRERPIEE SLILFEDMRK GKINEGDATL RMKTTLEEGK KDPVAYRIKF TPHHRSGNDW
CIYPTYDYTH CLCDSIENIS HSLCTKEFQA RRSSYYWLCN VLELYCPVQW EYARLNLHYA
VVSKRKIAKL IEKGYVKDWD DPRLFTLTAL RRRGFPPEAI NLFCAKVGVT MAQTVIDPAL
LESCVRDVLN VKAPRAMAVL NPLPVKIINF PAGHSGKVSV PNYPADPNKG EHSVPFCEQI
FIERDDFKEV TDKNYKRLAP TQPVGLRHAG FTIEVAEVVK DSSGFITELH VKCHKTTEDK
PKAFIHWVSK PVSCEVRLYD KLFFHRNPED TSEVPDGYLS DVNRDSLKVI SNAFVDTSVL
KAETYKQFQF ERTGYFSVDR DSKPDHLVFN QTVTLKEDPN KN
//
