ID Q0RP65_FRAAA Unreviewed; 1069 AA.
AC Q0RP65;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00254, ECO:0000256|HAMAP-Rule:MF_00255};
DE Includes:
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
DE Includes:
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
GN Name=glyQS {ECO:0000313|EMBL:CAJ60668.1};
GN Synonyms=glyQ {ECO:0000256|HAMAP-Rule:MF_00254}, glyS
GN {ECO:0000256|HAMAP-Rule:MF_00255};
GN OrderedLocusNames=FRAAL2019 {ECO:0000313|EMBL:CAJ60668.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ60668.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ60668.1, ECO:0000313|Proteomes:UP000000657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC EC=6.1.1.14; Evidence={ECO:0000256|ARBA:ARBA00000201,
CC ECO:0000256|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
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DR EMBL; CT573213; CAJ60668.1; -; Genomic_DNA.
DR RefSeq; WP_011603191.1; NC_008278.1.
DR AlphaFoldDB; Q0RP65; -.
DR STRING; 326424.FRAAL2019; -.
DR KEGG; fal:FRAAL2019; -.
DR eggNOG; COG0751; Bacteria.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_007220_0_0_11; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000000657; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR NCBIfam; TIGR00388; glyQ; 1.
DR NCBIfam; TIGR00211; glyS; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02091; tRNA-synt_2e; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 2.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00255};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00255};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Reference proteome {ECO:0000313|Proteomes:UP000000657}.
FT REGION 888..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 112857 MW; 1F1573AEF60DDA82 CRC64;
MLTMQDALLA LTRYWTDRGC MIMQPFNTEV GAGTLNPATV LRVLGPEPWR VAYVEPSVRP
DDSRYGQNPN RLQTHTQFQV ILKPDPGNAQ ELYLGSLAAI GVDTAAHDVR FVEDNWASPA
LGAWGLGWEV WLDGLEITQF TYFQQAGGQT LDTISVEITY GMERILMALQ GVRHFSELAY
APGISYGEVF GQAEYEMSRY YLDDADIDTV RRLYADYAAE ARRLVDARLP VPAHSYVLKC
SHAFNILDSR GAVSTTERAT SFAQMRGLSR EVAALWRDRR EELGHPLGVA SPPPAAVPVA
MTTAVRAPAT LLFEIGTEEL PAAEVTRTAA AVRAGLLDRL AATRLTHGDV RVQGTPRRIV
AIVDDVAPRE PDVERVVRGP RVAAAYDAAG APTKAAVGFA RGQGADPADL QVVTHRDVEH
VALVRTEAGR DATDVLAEVL GELVAGLRAE RNMRWNDPEL SFSRPVRWLV ALLGETVVPV
AVSSLAAGRT TVGHRRAGSP PIEVASADGY PELLATRSIL LDPAVRRDLV LEQAAKLTAD
TGGHIDPDAD ADTLAEVTNL VEFPRPLLGA FEARFLELPA EILTTVMRKH QRYLPVRDAA
GRLLPAFVAV ADGQVDDALV RAGNEDVIRA RFTDAAFFYD ADVKVAPETF RAELAKLTFE
QRLGSVADRA DRIGALARAL GDEIGLGADD RATLDRAATL AKFDLATQMV VELSSLAGTM
AREYARRAGE PEAVATALYE MELPRRAGDD LPATVAGSLL ALADRLDLLV GLFALDAAPT
GSSDPFGLRR AALGAAAILG SRPELAGLAV ADVLARAARL TPVPVSEQAL AAAEAFLRGR
YTQQLLDSGV DHRLVGAVGP LTGTPARAAA TLATLRGLIA VPAAATSAGE ASSATPSTPS
TPSTPSTPST PSTTGDQVAF AALAAALQRV RRIVPADAPA ILDGERLTEP AAARLLAVVT
ALAERLGARA GSPAPVVADS PVVGDAPVVG DVAAGSGASA NPAFVPLGEL VAAAGELPAA
IDGFFDALMV MDPDPALRAA RLGLLARIRD LTAGTLDWEA LGSLPASGH
//
