ID T2IN98_CROWT Unreviewed; 291 AA.
AC T2IN98;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254};
GN ORFNames=CWATWH0005_2709 {ECO:0000313|EMBL:CCQ54369.1};
OS Crocosphaera watsonii WH 0005.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=423472 {ECO:0000313|EMBL:CCQ54369.1, ECO:0000313|Proteomes:UP000017981};
RN [1] {ECO:0000313|EMBL:CCQ54369.1, ECO:0000313|Proteomes:UP000017981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 0005 {ECO:0000313|EMBL:CCQ54369.1,
RC ECO:0000313|Proteomes:UP000017981};
RA Bench S.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCQ54369.1, ECO:0000313|Proteomes:UP000017981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 0005 {ECO:0000313|EMBL:CCQ54369.1,
RC ECO:0000313|Proteomes:UP000017981};
RA Bench S.R., Heller P., Frank I., Arciniega M., Shilova I.N., Zehr J.P.;
RT "Whole genome comparison of six Crocosphaera watsonii strains with
RT differing phenotypes.";
RL Submitted (SEP-2013) 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_00254};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCQ54369.1}.
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DR EMBL; CAQL01000152; CCQ54369.1; -; Genomic_DNA.
DR RefSeq; WP_007312200.1; NZ_CAQL01000152.1.
DR AlphaFoldDB; T2IN98; -.
DR Proteomes; UP000017981; Unassembled WGS sequence.
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 CDD; cd00733; GlyRS_alpha_core; 1.
DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR NCBIfam; TIGR00388; glyQ; 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 PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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_00254};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00254};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00254}.
SQ SEQUENCE 291 AA; 33848 MW; 809B334C31AC7800 CRC64;
MSINFQEIIA KLNEFWGNRS CLIVQPYDTE KGAGTMNPHT FLRAIGPEPW SVAYVEPCRR
PTDGRYGENP NRFQHYYQYQ VLIKPSPNDI QEIYLDSLRA LGIKPEDHDI RFVEDNWESP
TLGAWGVGWE VWLDGMEITQ FTYFQQCGGI DCRPVSIEIT YGLERLAMYL QEVEAITKIQ
WNDNINYGDI FLQSEVEQCT YNFEASDADL LFKLFSLYEQ EAKQLIDRGL VFPGLDYVLK
CSHSFNLLDA RGVIAVAERT RYIGRIRNLA REVANLYLQQ RERLNFPLQK S
//
