ID K9S562_9CYAN Unreviewed; 722 AA.
AC K9S562;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 ORFNames=GEI7407_0613 {ECO:0000313|EMBL:AFY65111.1};
OS Geitlerinema sp. PCC 7407.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Geitlerinematales;
OC Geitlerinemataceae; Geitlerinema.
OX NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY65111.1, ECO:0000313|Proteomes:UP000010383};
RN [1] {ECO:0000313|EMBL:AFY65111.1, ECO:0000313|Proteomes:UP000010383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY65111.1,
RC ECO:0000313|Proteomes:UP000010383};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished genome of Geitlerinema sp. PCC 7407.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003591; AFY65111.1; -; Genomic_DNA.
DR RefSeq; WP_015170679.1; NC_019703.1.
DR AlphaFoldDB; K9S562; -.
DR STRING; 1173025.GEI7407_0613; -.
DR KEGG; gei:GEI7407_0613; -.
DR PATRIC; fig|1173025.3.peg.687; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_3; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000010383; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
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:UP000010383}.
FT DOMAIN 630..708
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 722 AA; 79559 MW; EABF8D21D281BE99 CRC64;
MATFLLEVGT EELPADFVDS ALAQWRSRLP QALSEHYLHT EALELYGTPR RLAVLIKGLP
DRQPDREELV KGPSAQAAFK DGQPTKAAEG FVRSRGASVS DLEIRSTEKG DFVFLQQQIP
GRPTAEILQE LALGWISALE GRRFMRWGTG DLRFPRPIRW LVALLDGAVL PLTLPNDGAT
VTSDRVSQGH RVLHPDPVTL DHADHYLDRL RKAFVEPDVD IRRQAIEAEI KLVAEKAGGV
AEISPDLLEE VTQLVEWPTA VLGTFEDEFL ELPPEVITTV MVTHQRYFPI FQADPSAPGA
SLLPRFITIS NGDPKKSDII AAGNARVIRA RLADGQFFYK ADCGQSLEKF LPQLETVTFQ
EALGSMGDKV KRVGQIAGQI AEQLGVSAGD RALIERAALL CKADLVTQMV FEFPELQGIM
GEKYARVSGE PEAVAQAISE HYLPKGAGDR LPPSLVGQVV GLADRLDTLV SIFALGLIPS
GSSDPFALRR AATAIVNIIW GADLSINLAA LLDQVVQRFS AEKGAVMKLS AEDLLGQLRS
FFLQRIQTLL QEDRHIDYDL VSAVLGEDDP EYTERALQDL LDVRDRAQFL QTIRQDGTLE
PIYEIVNRAS RLAVKGDLDT VTLDPANVVD TGRFQQPSEQ AFYEALGKLL PETQAAQSAR
DYRRLVTALA DTAPTISNFF DGPQSVLVMD ENPDIRRNRL NLLGLLRNHA RVLADFGPIV
KR
//
