ID SYG_HUMAN STANDARD; PRT; 739 AA. AC P41250; Q969Y1; DT 01-FEB-1995 (Rel. 31, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Glycyl-tRNA synthetase (EC 6.1.1.14) (Glycine--tRNA ligase) (GlyRS). GN GARS. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95050870; PubMed=7962006; RA Shiba K., Schimmel P., Motegi H., Noda T.; RT "Human glycyl-tRNA synthetase. Wide divergence of primary structure RT from bacterial counterpart and species-specific aminoacylation."; RL J. Biol. Chem. 269:30049-30055(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95273165; PubMed=7753621; RA Williams J.H., Osvath S.R., Khong T.-F., Pearse M.J., Power D.A.; RT "Cloning, sequencing and bacterial expression of human glycine tRNA RT synthetase."; RL Nucleic Acids Res. 23:1307-1310(1995). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Eye, and Muscle; RA Strausberg R.; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 3-739 FROM N.A. RX MEDLINE=95050687; PubMed=7961834; RA Ge Q., Trieu E.P., Targoff I.N.; RT "Primary structure and functional expression of human glycyl-tRNA RT synthetase, an autoantigen in myositis."; RL J. Biol. Chem. 269:28790-28797(1994). RN [5] RP SEQUENCE OF 348-739 FROM N.A. RA Andrews S., Langston Y., Stoneking T., Maupin R.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: BELONGS TO CLASS-II AMINOACYL-TRNA SYNTHETASE FAMILY. CC -!- SIMILARITY: Contains 1 WHEP-TRS domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D30658; BAA06338.1; -. DR EMBL; U09510; AAA86443.1; ALT_INIT. DR EMBL; BC007722; AAH07722.1; -. DR EMBL; BC007755; AAH07755.1; -. DR EMBL; U09587; AAA57001.1; ALT_INIT. DR EMBL; AC004976; AAC71652.1; -. DR HSSP; P56206; 1ATI. DR Genew; HGNC:4162; GARS. DR MIM; 600287; -. DR GO; GO:0005737; C:cytoplasm; TAS. DR GO; GO:0005625; C:soluble fraction; TAS. DR GO; GO:0004820; F:glycine-tRNA ligase activity; TAS. DR InterPro; IPR004154; HGTP_anticodon. DR InterPro; IPR002314; tRNA-synt_2b. DR InterPro; IPR002315; tRNA-synt_gly. DR InterPro; IPR006195; tRNA_ligase_II. DR InterPro; IPR000738; WHEP-TRS. DR Pfam; PF00458; WHEP-TRS; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR PRINTS; PR01043; TRNASYNTHGLY. DR TIGRFAMs; TIGR00389; glyS_dimeric; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. DR PROSITE; PS00762; WHEP_TRS; 1. KW Aminoacyl-tRNA synthetase; Protein biosynthesis; Ligase; ATP-binding. FT DOMAIN 74 119 WHEP-TRS. FT CONFLICT 530 530 M -> I (IN REF. 2). SQ SEQUENCE 739 AA; 83139 MW; 55DDD57119F438E5 CRC64; MPSPRPVLLR GARAALLLLL PPRLLARPSL LLRRSLSAAS CAPISLPAAA SRSSMDGAGA EEVLAPLRLA VRQQGDLVRK LKEDKAPQVD VDKAVAELKA RKRVLEAKEL ALQPKDDIVD RAKMEDTLKR RFFYDQAFAI YGGVSGLYDF GPVGCALKNN IIQTWRQHFI QEEQILEIDC TMLTPEPVLK TSGHVDKFAD FMVKDVKNGE CFRADHLLKA HLQKLMSDKK CSVEKKSEME SVLAQLDNYG QQELADLFVN YNVKSPITGN DLSPPVSFNL MFKTFIGPGG NMPGYLRPET AQGIFLNFKR LLEFNQGKLP FAAAQIGNSF RNEISPRSGL IRVREFTMAE IEHFVDPSEK DHPKFQNVAD LHLYLYSAKA QVSGQSARKM RLGDAVEQGV INNTVLGYFI GRIYLYLTKV GISPDKLRFR QHMENEMAHY ACDCWDAESK TSYGWIEIVG CADRSCYDLS CHARATKVPL VAEKPLKEPK TVNVVQFEPS KGAIGKAYKK DAKLVMEYLA ICDECYITEM EMLLNEKGEF TIETEGKTFQ LTKDMINVKR FQKTLYVEEV VPNVIEPSFG LGRIMYTVFE HTFHVREGDE QRTFFSFPAV VAPFKCSVLP LSQNQEFMPF VKELSEALTR HGVSHKVDDS SGSIGRRYAR TDEIGVAFGV TIDFDTVNKT PHTATLRDRD SMRQIRAEIS ELPSIVQDLA NGNITWADVE ARYPLFEGQE TGKKETIEE //