ID Q821W2_CHLCV Unreviewed; 1006 AA.
AC Q821W2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 135.
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=glyQS {ECO:0000313|EMBL:AAP05564.1};
GN Synonyms=glyQ {ECO:0000256|HAMAP-Rule:MF_00254}, glyS
GN {ECO:0000256|HAMAP-Rule:MF_00255};
GN OrderedLocusNames=CCA_00823 {ECO:0000313|EMBL:AAP05564.1};
OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS (Chlamydophila caviae).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=227941 {ECO:0000313|EMBL:AAP05564.1, ECO:0000313|Proteomes:UP000002193};
RN [1] {ECO:0000313|EMBL:AAP05564.1, ECO:0000313|Proteomes:UP000002193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-813 / DSM 19441 / GPIC
RC {ECO:0000313|Proteomes:UP000002193};
RX PubMed=12682364; DOI=10.1093/nar/gkg321;
RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA Fraser C.M.;
RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT examining the role of niche-specific genes in the evolution of the
RT Chlamydiaceae.";
RL Nucleic Acids Res. 31:2134-2147(2003).
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|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; AE015925; AAP05564.1; -; Genomic_DNA.
DR RefSeq; WP_011006778.1; NC_003361.3.
DR AlphaFoldDB; Q821W2; -.
DR STRING; 227941.CCA_00823; -.
DR KEGG; cca:CCA_00823; -.
DR eggNOG; COG0751; Bacteria.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_007220_1_0_0; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000002193; 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 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; 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; 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 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}.
SQ SEQUENCE 1006 AA; 113436 MW; 8F60BF0C04FF4B41 CRC64;
MSQPLTLQAM IAKILQFWSE QGCVIHQGYD LEVGAGTFNP ATFLRALGPE PYKTAYVEPS
RRPQDGRYGM HPNRLQNYHQ LQVILKPVPS NFLSLYKESL QIIGLDLREH DIRFVHDDWE
NPTIGAWGLG WEVWLNGMEI TQLTYFQAIG SKPLDTISGE ITYGIERIAM YLQKKSSIFD
VLWNDELTYG DITQASEKSW SEYNFDVANT QMWLKHFEDF AQEALATLDK GLPAPAYDFV
IKASHAFNIL DARGVISVTE RTRYITRIRQ LARAVADGYV EWRASLNYPL LHKQGVHKDE
TSPSLPCPKI TTTENYLLEI GSEELPATFV PIGIQQLESL AKKLLADYNI GYESLEVLGS
PRRLALLVYK LEPTAIQKAV EKKGPMLSSL FSDSGDITAQ GEQFFASHNI SIRHYDELSQ
HSLFEIREIG SVNYLFILHP EVCRDTVTIL ANELPKLIQS MKFPKKMVYD DSGVEYARPI
RWIVSLYGTS ILPFSFGKVV AGNTSMGHRQ LDPREVPIPS CEHYIDTLRN ACVVVSHKER
REIIEQGLKL HSSDNVSPVA NPRLLEETVF LTEHPFVTCA QFDKKFCALP KELLIAEMVN
HQKYFPTQNT AKEITNQFIL VCDNCPNDII IEGNEKALTP RLTDGDFLFA QDLKTSLAIF
VDKLKAVTYF EALGSLYDKV ERLKAHKEVV YPLLPISSQE DITTAIEFCK ADLVSAVVNE
FAELQGIMGE YYIKHAGLSH AAAVAVGEHL RHITDGQTIS TTGTLLSLID RFDNLLSCFI
LDLRPTSSHD PYALRRQSLE ILTLLHASEA SLDLESLLHH LADNFPATVQ GATWDKPAVI
RDILTFIWGR LKTFMASLGF SKDEIATVLS DTSEKNPVEM LKSATALQAM KNSHRAILEK
ITTTHNRLKK ILASLKLSTN TLTPIELDLQ ESQLKAALDH FDASVQTKDS KKDYFLSLGD
LTDSINTFLN EVHVTSGSEE LQNLRIYLLL TALEKFSSYH WEALKV
//
