ID Q8TUH0_METAC Unreviewed; 612 AA.
AC Q8TUH0;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00012829};
DE EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
GN Name=glyS {ECO:0000313|EMBL:AAM03551.1};
GN OrderedLocusNames=MA_0097 {ECO:0000313|EMBL:AAM03551.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM03551.1, ECO:0000313|Proteomes:UP000002487};
RN [1] {ECO:0000313|EMBL:AAM03551.1, ECO:0000313|Proteomes:UP000002487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC {ECO:0000313|Proteomes:UP000002487};
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; AE010299; AAM03551.1; -; Genomic_DNA.
DR RefSeq; WP_011020156.1; NC_003552.1.
DR AlphaFoldDB; Q8TUH0; -.
DR STRING; 188937.MA_0097; -.
DR EnsemblBacteria; AAM03551; AAM03551; MA_0097.
DR GeneID; 1471989; -.
DR KEGG; mac:MA_0097; -.
DR HOGENOM; CLU_015515_1_0_2; -.
DR InParanoid; Q8TUH0; -.
DR OrthoDB; 6113at2157; -.
DR PhylomeDB; Q8TUH0; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00774; GlyRS-like_core; 1.
DR CDD; cd00858; GlyRS_anticodon; 1.
DR Gene3D; 3.30.40.230; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR002315; tRNA-synt_gly.
DR NCBIfam; TIGR00389; glyS_dimeric; 1.
DR PANTHER; PTHR10745:SF0; GLYCINE--TRNA LIGASE; 1.
DR PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000002487}.
FT DOMAIN 2..367
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 457..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 69166 MW; A12AF972927C8B55 CRC64;
MDKYEKVFEL AKRRGFLWNS FELYGGSRGF YDYGPLGSTL KRRIEQVWRE FYVIQEGHME
IECPTIGIEE VFIASGHVGG FSDPLCECMN CKEAFRADHL VENVTEAAGT LSAEELTKVI
REKEIRCPEC GGEFEDAYEF NLMFKTTIGP GTGRQGYLRP ETAQGMFVDF QRLSRFYRDK
LPFGAVQIGK SYRNEIAPRQ GVIRLREFTQ AECELFVDPR NKKHPNFERF ADKELVLYSQ
AAQQTGEPVR LTVREAVETG VIAHEILGYN IALTNEFLTK VGIDPEKLRF RQHLTDEMAH
YAIDCWDAEI ETDRFGWVEI VGIADRTDYD LKAHARVSKT DLYVYVEYDE PKIVTRFVVK
PNMGKLGPLF KGKAKAVADA LKQLSEEELS KDQIKVTLDG EELTVSPDVV DFAEENIKVS
GENVIPHVIE PSYGIDRIFY GIMEHAFDEE NVAQKAAESG LKGAGEAEGT EDAGKESGGA
KSESEAEGEE ARLVMHFSSA VAPVQVAVLP LLTRKELADP AKEIIAKLRE KTLLVNYDDS
GTIGRRYRRN DEIGTPYSVT VDYDTLQDGT VTIRDRDSMR QVRAPINGIE NVLYELIYRG
RDFESAGKPF NF
//
