ID A0A0H5DS21_9BACT Unreviewed; 1016 AA.
AC A0A0H5DS21;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00254, ECO:0000256|HAMAP-Rule:MF_00255};
DE Includes:
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};
DE Includes:
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
GN Name=glyqs3 {ECO:0000313|EMBL:CRX39457.1};
GN Synonyms=glyQ {ECO:0000256|HAMAP-Rule:MF_00254}, glyS
GN {ECO:0000256|HAMAP-Rule:MF_00255};
GN ORFNames=ELAC_2136 {ECO:0000313|EMBL:CRX39457.1};
OS Estrella lausannensis.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Criblamydiaceae;
OC Estrella.
OX NCBI_TaxID=483423 {ECO:0000313|EMBL:CRX39457.1, ECO:0000313|Proteomes:UP000220251};
RN [1] {ECO:0000313|Proteomes:UP000220251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB-30 {ECO:0000313|Proteomes:UP000220251};
RA Bertelli C.;
RL Submitted (JUN-2015) 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; CWGJ01000028; CRX39457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5DS21; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000220251; Unassembled WGS sequence.
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 CDD; cd00733; GlyRS_alpha_core; 1.
DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR NCBIfam; TIGR00388; glyQ; 1.
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; PF02091; tRNA-synt_2e; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 2.
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:UP000220251}.
FT DOMAIN 927..1009
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 1016 AA; 115193 MW; 89621C8393D10F86 CRC64;
MVTFQDIIRR LTRFWEEQGC ILQQGYDLEV GAGTFNPATF FRCLGPEPYR ACYVEPSRRP
TDGRYGLNPN RVQHYFQFQV MLKPAPLNIQ ELYLQSLEAV GFNLKEHDVR FVHDDWESPT
LGASGLGWEV WMDGMEITQF TYFQNCGGLP LKPVTGELTY GLERLALYIQ KVESIFDIQW
TGDITYGDIY QQSEYEWSRY NFEESDARLW LQHFDAYEKE ASLLVAKGLV IPAYDFVMKA
SHAFNMLDAR GVISVTERTS YIARVRQLAC DVAKAYLLSR EKQKFPLMPR FKGIREEVPV
KLTPKERLPE ELMDASSDEK MDYLLEIGSE ELPASFIEPA LESLQGKLRA LFDKENIPYT
AIEMYGTPRR LAACVKGLSL AKPARTEERK GPAKESAFDA DGSLKPAGLG FFKAVAAKPL
ALQEIAAGRH PKVRLREIGG KEYLFATIQE DSRPTTDILM ETLPDIILGI DFPKKMRWSD
LDISYARPLR WIVSLFGNHI VPFTVGNITA GRESTGHSQL HPWAFALVKS EDYLPILKDH
KVIADIAERK KIIAKKIREI EECQGAVAAE KEKVLNQVVN LVEWPELLTG TFKAEYLKAP
TEVLISEMVE HQKYFPLIKK DGTLKSCFII TANTRPTDKV REGNERALSP RLADGLALFE
ADLKIPLHEL NERLKSITFQ KDLGSVFAKV ERLTRHAALI QQKLGISTPE QCARAALLSK
CDIASRMVFE FPELQGTMGR HFALAQGETA EIAHAIEEHW MPKGEAAPLP STPTGIVISL
AEKFDNLLGS ALVGLKATSS SDPYALRRQA LGLIKILIAN SLKLPLRELM QDLIDHFPLE
LRKRKEGAVD EVLEFLMNRI RTVFLEFGLS KDAIEASASI GFNDVYDSFL KAKAFQNFRE
KEGRFYKLFE VYKRVKGQLT SQKSINFSEA LLEERAEIAL HKLLQTTEEP FHSAVSSGRY
DEAYRMIAEI QPALATLFDE VKIMAEDPKI QGNRLALLQL VFDRFSKLLD FSKIRE
//
