ID A0A1Z4NMB1_9CYAN Unreviewed; 714 AA.
AC A0A1Z4NMB1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ECO:0000313|EMBL:BAZ06833.1};
GN ORFNames=NIES3974_34950 {ECO:0000313|EMBL:BAZ06833.1};
OS Calothrix sp. NIES-3974.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005462 {ECO:0000313|EMBL:BAZ06833.1, ECO:0000313|Proteomes:UP000218621};
RN [1] {ECO:0000313|EMBL:BAZ06833.1, ECO:0000313|Proteomes:UP000218621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3974 {ECO:0000313|EMBL:BAZ06833.1,
RC ECO:0000313|Proteomes:UP000218621};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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}.
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DR EMBL; AP018254; BAZ06833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4NMB1; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000218621; 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:UP000218621}.
FT DOMAIN 617..699
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 714 AA; 80129 MW; 29BF929C63BFAA38 CRC64;
MPAFLLEVGT EELPASFVSS AIQQWRDRIP QSLDEYGLER DDIKIYGTPR RLAVLITGLP
NQQSDRTEEV KGPPAQAAFK DGNPTPAALG FAKKQGVDVA ALEIRPTDKG DFVFINKLIP
GRPISEILSE LVPQWIFNLE GKRLMRWGDG DLRFSRPIRW LVTLLDDAVL PMKIENGRDV
VTSDRLSRGH RVLHPADISI PNAQAYVESL RSGYIMVDGA ERAQVITEQT TAAAARIGGR
AEIYPDLLGE VVNLVEWPNA VVGKFEPEYL ELPTEVITTV MVTHQRYFPV FKQDQELLPN
FITISNGDPS KADIIADGNA RVIRARLADG QYFYDKDLEK PLENLLPKLE TVTFQEDLGS
LRAKVDRICH IASLISQQLQ LGEPETNYTQ RAALLCKADL VSQMVYEFPE LQGVMGEKYA
RKGNEPEPVA TAIFEHYLPR HAGDILPQTR VGQIVAIADK LDTLVSIFGL GMIPSGSSDP
FALRRAANAI INITWAGNLP LNLLQLIHDS ATAFAQTYHK NAEELITLLQ DFFCQRLRTL
LQEENHIDYD LVNAVIGDND TEYTQRALSD VLDVRQRATY LQQIRENGTL GQIYEPINRS
TRLATQGDLD TQTLDPQNLI QPPLFQKTSE EKLYTALVNL LPQTQTCRES RNYQQLVTAF
LEIQPTVSNF FDGEESVLVM DENPDIRRNR LNLLGLLRNH ARVLADFGCI VKNQ
//
