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Database: UniProt
Entry: A0A1V4JID3_PATFA
LinkDB: A0A1V4JID3_PATFA
Original site: A0A1V4JID3_PATFA 
ID   A0A1V4JID3_PATFA        Unreviewed;       823 AA.
AC   A0A1V4JID3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, 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=QARS {ECO:0000313|EMBL:OPJ71963.1};
GN   ORFNames=AV530_009298 {ECO:0000313|EMBL:OPJ71963.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ71963.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ71963.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ71963.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ71963.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) 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:OPJ71963.1}.
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DR   EMBL; LSYS01007300; OPJ71963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4JID3; -.
DR   STRING; 372326.A0A1V4JID3; -.
DR   Proteomes; UP000190648; 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:UP000190648}.
FT   DOMAIN          8..165
FT                   /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT                   RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04558"
FT   DOMAIN          168..256
FT                   /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT                   RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04557"
FT   DOMAIN          265..564
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          567..667
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   DOMAIN          679..754
FT                   /note="tRNA synthetases class I (E and Q) anti-codon
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF20974"
FT   REGION          187..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   823 AA;  92698 MW;  6AA44CB6724F19C6 CRC64;
     MAAEEAEEAL GLFIGIGLSE AKARETLRNG ALSALLRQAV LQARSALGPA LDKATGTLLY
     NAAARLRDPK HLGFLVGYIV RREILTDLQL SAALEYVRTH PLEPLDTADF EQACGVGVCV
     TPEQIEEAVE AVISEHRAEL LAERYRFNMG LLMGEARSRL RWADGKTIKN EVDLQVLHLL
     GPKTEADLEK KPKAAKARPA PAEKQKAAVV ENGEVGTETR SLLEQLRGEA LKFHKPGENY
     KTEGYVVTPN TMALLKQHLA VTGGQVRTRF PPEPNGILHI GHAKAINFNF GYAKANGGVC
     FLRYDDTNPE KEEEKYFTAI REMVEWLGYQ PYAVTHASDY FDQLYTWALE LIRRGHAYVC
     HQKVEEIKGH NPPPSPWRDR PVEESLLLFE DMRKGKFGEG EATLRMKLIM EDGKMDPVAY
     RVKFTPHHRT GDKWCIYPTY DYTHCLCDSI EHITHSLCTK EFQARRSSYF WLCNALDVYC
     PVQWEYGRLN LLYTVVSKRK IIRLVETGAV RDWDDPRLFT LTALRRRGFP PEAINNFCAR
     VGVTVAQATM EPHLLEACVR EVLNEQAPRA MAVLEPLKVT ITNFPALKAL EVLVPNFPAD
     ESRGFHKVPL QPTIYIEETD FREEVDKGYK RLAPGQPVGL RHAGYIIAVQ NIIKDASGHV
     IELEVTCTKS DVAEKPKAFI HWVSEPLVCE VRLYERLFLH KNPEDPSEVP GGFLSDLNPD
     SLRVARNALV DSSVLSARPF DKFQFERLGY FSVDPDSEEG KLVFNRTVTL KEDPGKVGAG
     PGAVLSRDLE AALSRERYKS KSSGQEQQKY MQHGDWNPKE LAI
//
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