ID D7BHV4_MEISD Unreviewed; 507 AA.
AC D7BHV4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 01-MAY-2013, entry version 21.
DE RecName: Full=Glycine--tRNA ligase;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase;
GN Name=glyQS; OrderedLocusNames=Mesil_2174;
OS Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus
OS silvanus).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Meiothermus.
OX NCBI_TaxID=526227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700542 / DSM 9946 / VI-R2;
RX DOI=10.4056/sigs.1042812;
RA Sikorski J., Tindall B., Lowry S., Lucas S., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Cheng J., Han C., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Goodwin L.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C.,
RA Rohde M., Goker M., Woyke T., Bristow J., Eisen J., Markowitz V.,
RA Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT "Complete genome sequence of Meiothermus silvanus type strain (VI-
RT R2).";
RL Stand. Genomic Sci. 3:37-46(2010).
CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC + glycyl-tRNA(Gly).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family.
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DR EMBL; CP002042; ADH64044.1; -; Genomic_DNA.
DR RefSeq; YP_003685552.1; NC_014212.1.
DR EnsemblBacteria; ADH64044; ADH64044; Mesil_2174.
DR GeneID; 9251688; -.
DR KEGG; msv:Mesil_2174; -.
DR PATRIC; 38193157; VBIMeiSil18825_2216.
DR HOGENOM; HOG000242016; -.
DR KO; K01880; -.
DR OMA; NEITTGN; -.
DR BioCyc; MSIL526227:GJ9Q-2213-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:HAMAP.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1; -.
DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR022961; Gly_tRNA_ligase_bac.
DR InterPro; IPR002315; tRNA-synt_gly.
DR PANTHER; PTHR10745; PTHR10745; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF52954; Anticodon_bd; 1.
DR TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW Ligase; Nucleotide-binding; Protein biosynthesis.
FT NP_BIND 222 224 ATP (By similarity).
FT NP_BIND 232 237 ATP (By similarity).
FT NP_BIND 307 308 ATP (By similarity).
FT NP_BIND 366 369 ATP (By similarity).
FT REGION 237 241 Substrate binding (By similarity).
FT REGION 362 366 Substrate binding (By similarity).
FT BINDING 99 99 Substrate (By similarity).
FT BINDING 190 190 Substrate (By similarity).
SQ SEQUENCE 507 AA; 57458 MW; E15FD5E05CC3A941 CRC64;
MPAETMDELV SLCKRRGFIF QGSEIYGGLQ GTYDYGPLGV ELKNNLKAAW WRANVYERDD
MEGLDASILT HRLVLHYSGH EATFADPLID NRISKKRYRL DHLLKEQKPG VCAAVAVGMG
LEPNTDIATL VAALMADPER AAQAMNAARV VDPADGAPGD WTPPRPFNMM FKTTIGPVAD
EDSYGYLRPE TAQGIFVNFK NVLDSTSRRL PFGIAQIGKA FRNEITPRNF IFRVREFEQM
EIEYFVKPGT DEHWHQHWLE TRLEWWEAQG IPRAQIQVLD VPKEDLAHYS KRTYDLLYNF
PTLGFEEIEG IANRSDYDLG SHTKAQSELG IQARVMENTD STAKLAIQDP ETGKWIVPFV
IEPSAGVDRG VLAVLSEAYT REKLESGEER IVLKLKPHLA PIKVAVIPLA KNKEEITRYA
KDLKRKLQAL GMGRVLYEDT GNIGKAYRRH DEVGTPFCVT VDYDTIGKSQ DGSTTLMDTV
TVRDRDTMQQ ERVHVKELPQ YLQERLR
//
