ID SYG_HUMAN STANDARD; PRT; 685 AA. AC P41250; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 20-AUG-2001 (Rel. 40, 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. 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 [4] RP SEQUENCE OF 294-685 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 + L-GLYCINE + TRNA(GLY) = AMP + CC PYROPHOSPHATE + L-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; ALT_INIT. DR EMBL; U09510; AAA86443.1; -. DR EMBL; U09587; AAA57001.1; -. DR EMBL; AC004976; AAC71652.1; -. DR HSSP; P56206; 1ATI. DR MIM; 600287; -. DR InterPro; IPR002106; AA_tRNA_ligase_II. DR InterPro; IPR000738; WHEP-TRS. DR InterPro; IPR002314; tRNA-synt_2b. DR InterPro; IPR002315; tRNA-synt_gly. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF00458; WHEP-TRS; 1. DR PRINTS; PR01043; TRNASYNTHGLY. DR PROSITE; PS00179; AA_TRNA_LIGASE_II_1; 1. DR PROSITE; PS00339; AA_TRNA_LIGASE_II_2; FALSE_NEG. DR PROSITE; PS00762; WHEP_TRS; 1. KW Aminoacyl-tRNA synthetase; Protein biosynthesis; Ligase; ATP-binding. FT DOMAIN 20 65 WHEP-TRS. FT CONFLICT 476 476 M -> I (IN REF. 2). SQ SEQUENCE 685 AA; 77530 MW; D63AF159912F0750 CRC64; MDGAGAEEVL APLRLAVRQQ GDLVRKLKED KAPQVDVDKA VAELKARKRV LEAKELALQP KDDIVDRAKM EDTLKRRFFY DQAFAIYGGV SGLYDFGPVG CALKNNIIQT WRQHFIQEEQ ILEIDCTMLT PEPVLKTSGH VDKFADFMVK DVKNGECFRA DHLLKAHLQK LMSDKKCSVE KKSEMESVLA QLDNYGQQEL ADLFVNYNVK SPITGNDLSP PVSFNLMFKT FIGPGGNMPG YLRPETAQGI FLNFKRLLEF NQGKLPFAAA QIGNSFRNEI SPRSGLIRVR EFTMAEIEHF VDPSEKDHPK FQNVADLHLY LYSAKAQVSG QSARKMRLGD AVEQGVINNT VLGYFIGRIY LYLTKVGISP DKLRFRQHME NEMAHYACDC WDAESKTSYG WIEIVGCADR SCYDLSCHAR ATKVPLVAEK PLKEPKTVNV VQFEPSKGAI GKAYKKDAKL VMEYLAICDE CYITEMEMLL NEKGEFTIET EGKTFQLTKD MINVKRFQKT LYVEEVVPNV IEPSFGLGRI MYTVFEHTFH VREGDEQRTF FSFPAVVAPF KCSVLPLSQN QEFMPFVKEL SEALTRHGVS HKVDDSSGSI GRRYARTDEI GVAFGVTIDF DTVNKTPHTA TLRDRDSMRQ IRAEISELPS IVQDLANGNI TWADVEARYP LFEGQETGKK ETIEE //