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Database: UniProt
Entry: A0A399F847_9DEIN
LinkDB: A0A399F847_9DEIN
Original site: A0A399F847_9DEIN 
ID   A0A399F847_9DEIN        Unreviewed;       779 AA.
AC   A0A399F847;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glutamine--tRNA ligase {ECO:0000313|EMBL:RIH92837.1};
DE            EC=6.1.1.18 {ECO:0000313|EMBL:RIH92837.1};
GN   Name=glnS {ECO:0000313|EMBL:RIH92837.1};
GN   ORFNames=Mgrana_01245 {ECO:0000313|EMBL:RIH92837.1};
OS   Meiothermus granaticius NBRC 107808.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX   NCBI_TaxID=1227551 {ECO:0000313|EMBL:RIH92837.1, ECO:0000313|Proteomes:UP000266178};
RN   [1] {ECO:0000313|EMBL:RIH92837.1, ECO:0000313|Proteomes:UP000266178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF-68 {ECO:0000313|EMBL:RIH92837.1,
RC   ECO:0000313|Proteomes:UP000266178};
RA   Da Costa M.S., Albuquerque L., Raposo P., Froufe H.J.C., Barroso C.S.,
RA   Egas C.;
RT   "Meiothermus granaticius genome AF-68 sequencing project.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {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:RIH92837.1}.
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DR   EMBL; QWLB01000013; RIH92837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399F847; -.
DR   OrthoDB; 9801560at2; -.
DR   Proteomes; UP000266178; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR   GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 1.10.10.410; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR018027; Asn/Gln_amidotransferase.
DR   InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR   InterPro; IPR023168; GatB_Yqey_C_2.
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; PF02637; GatB_Yqey; 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   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 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:UP000266178}.
FT   DOMAIN          637..778
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
FT   REGION          578..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..595
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   779 AA;  87384 MW;  658BE1EE9528923E CRC64;
     MSTPTVQRRV NPNFITEIID EDLKAGRYSQ IVTRFPPEPN GYAHLGHAIA SYLNWGIAQD
     YGGLFRLRMD DTNPQTERQE YAEALVRDLA WLGLRWDGKV EYASDYFEDL YQMALRLIQK
     GLAYVDSIPH EEMVRLRGSV EVPGTPSPYR QRSIEENLEL FQRMRAGEFP TGAHVLRAKI
     DLASPNMKLR DPVLYRIVHA EHYRTGTTWP IYPSYDFAQA PTDALIGVTH SLCSLEFVDN
     RAIYDWLMEH LWGEPRPRQY EFGRRSLEYT VVSKRKLLKL IAGGHVTGWD DPRMPTLAGQ
     RRRGVTPEAL RTFAKSVGIS RTNRTVDIAL LEHAIREDLN LRAPRVMAVI RPLKVVLTNL
     EAESTLSLRY WPDDVVRGSP DGLVARPNGE RVRPEEAVRP VPLTPELYIE ADDFEVEPPP
     GFKRLTPGGT VRLRGAGLIR CDEYLRDATG QVCELRCTWL GEAGKASGVI HWVSATQSLR
     AEFRLYDRLF RVPLPESEAK ELEEEEEGET REDRDFLSFL NPQSLEVRQG WVEASVASDP
     PETRYQFERL GYFWPDPLDS KPGALVFNRI VGLRDSWKGA EGPRPKGEPR APKEEKGQGP
     GQVVLSAQEQ ARFERFKGQG VGEADARVLA RDPALEAYLN QAARWAPVAH LASWVVNELG
     SSIREGSNKV SPAALAELVA LVQGGEINTR IAKDVLAEAQ SSGENPAEIV RARGLRQVND
     SAALEAVLDR ILAAHPDQVA AYRGGKTGLL GFFVGQVMRE TGGQANPQTV RELVLRRLG
//
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