ID E3H6T2_ILYPC Unreviewed; 690 AA.
AC E3H6T2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
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};
GN Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN OrderedLocusNames=Ilyop_0664 {ECO:0000313|EMBL:ADO82451.1};
OS Ilyobacter polytropus (strain ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Ilyobacter.
OX NCBI_TaxID=572544 {ECO:0000313|EMBL:ADO82451.1, ECO:0000313|Proteomes:UP000006875};
RN [1] {ECO:0000313|EMBL:ADO82451.1, ECO:0000313|Proteomes:UP000006875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1
RC {ECO:0000313|Proteomes:UP000006875};
RX PubMed=21304735; DOI=10.4056/sigs.1273360;
RA Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Yasawong M.,
RA Rohde M., Pukall R., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ilyobacter polytropus type strain (CuHbu1).";
RL Stand. Genomic Sci. 3:304-314(2010).
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|ARBA:ARBA00004496,
CC 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; CP002281; ADO82451.1; -; Genomic_DNA.
DR RefSeq; WP_013387121.1; NC_014632.1.
DR AlphaFoldDB; E3H6T2; -.
DR STRING; 572544.Ilyop_0664; -.
DR KEGG; ipo:Ilyop_0664; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_0; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000006875; 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_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
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; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
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:UP000006875}.
FT DOMAIN 587..680
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 690 AA; 78656 MW; 10802DEEB5D29714 CRC64;
MKILLEIGME EIPARFLKPA LNDIEKYIKK EFESQRIKFE TLKTFGTPRR LVLLVDGVSE
KQEDLDIVNT GPAKEVAYDV NGELTRAGVG FAKSQGIDPT DLEILETPKG EYIAVRKFVE
GKDTKELLSG LLKNLITGLT FPKSMKWSDL SMKFARPVQW FLAMADDELV EFEIEGIKSS
LNSKGHRFFG EEFEVTSIEE YFTKLRENNV IVDIEERKQM IIDMIKEKCT KTGEQVLIEP
DLLDEVTNLI EYPYPIVGTF NSEFLEVPQE VLIISMQVHQ RYFPILDSQG KLLPKFVVIR
NGITSSEHVR KGNEKVLSAR LSDARFFYQE DQKKSLEEFV DKLSTVVFQK DLGTIAQKIS
RSKKLAEYMS EKLALRDSKE DIMRTIHLAK ADLVSNMIGE KEFTKLQGFM GADYALKAGE
KEVVSKGIEE HYYPRYQGDK LPQGIEGVIA GICDRMDTLV GCFGIGMIPS GSKDPFALRR
AALAIVNIIL NSKLVISLEE LTSKMLDILE EDNVLKRPKK DVLKDLMEFF KQRAINVFAD
HGHRKDVIGA VLSIDCDVLL EASEKIETLE KVSKEEGFND LVLLLKRVGN ISKDHHEKAI
STDLLVEDAE KELHKFYVDL DSKTELNLQT KSYEEFFRNI LAGKNVINRF FDSVMVMDKD
QSLKNNRLSL LKSLNEIFNR VAKLNLIEEK
//