ID C5LFD6_PERM5 Unreviewed; 659 AA.
AC C5LFD6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
GN ORFNames=Pmar_PMAR014969 {ECO:0000313|EMBL:EER04568.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER04568.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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|RuleBase:RU363037}.
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DR EMBL; GG681431; EER04568.1; -; Genomic_DNA.
DR RefSeq; XP_002772752.1; XM_002772706.1.
DR AlphaFoldDB; C5LFD6; -.
DR EnsemblProtists; EER04568; EER04568; Pmar_PMAR014969.
DR GeneID; 9037538; -.
DR InParanoid; C5LFD6; -.
DR OMA; TIHWVAK; -.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
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; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth.
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 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:UP000007800}.
FT DOMAIN 30..340
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 343..432
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 455..555
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 136..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 75325 MW; 1E594B5902D6A51C CRC64;
MSTTESTGKN FIQTAIDQDL APGGRCHGKK IVTRFPPEPN GYLHIGHAKS ICLNFGLAKQ
YGGTCHLRFD DTNPSAESDE YVRSIQEDVK WLGFDWDDNL FFASSYFDQL YEWAEYLINQ
GEAYVDLQTP DQIRINRGNI NTPGTNSPNR EQTPEENLRL FRDMRDGKFK EGEALLRAKI
DMASPNMNMR DPPMYRILHK EHHRTGKKWC IYPLYDFAHG QEDAIEHITH SICTLEFENH
RELYDWFLAH LPVPSRPHQY EFARLQVTNT IMSKRKLLKL VNSHSVRGWD DPRMPTISGM
RRRGVTPKAL RTFCQKVGVS TSLSTIDSVL LDECIREDLE ANSNRRMCVV NPVKVYIETM
PDEERIEVEA PNHPGMPEAG SRKLYLRNRL VIESSDFRID PPEGFKRLSL GGKVKLRYGY
VIKAERVTPE GVVICSHDPD SLHGEGSLPK DVKGVIHWAV DAEESNEDVV RGTVNWYENL
LLPESAPTDE GATSEEEASM VPGTAEVEEA DKDAWLSQLN PNSLREYKAY FEPSMAEAKP
METFQFERVG YFVVDKDSTA DQLTCNLTVT LKESGLKKTE GKHAGRSRKE AQAAQLAEKE
AKKKIRPEDM FKEQTDKYSQ FDESGIPTHD AAGEKLAKSA YKKLHKEWEK QRRLYESNH
//
