GenomeNet

Database: UniProt
Entry: E3H6T2_ILYPC
LinkDB: E3H6T2_ILYPC
Original site: E3H6T2_ILYPC 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system