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 01-OCT-1996 (REL. 34, 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; VERTEBRATA; MAMMALIA; EUTHERIA; OC PRIMATES; CATARRHINI; HOMINIDAE; HOMO. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 95050870. 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. 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. 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). 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 This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; G1311463; ALT_INIT. DR EMBL; U09510; G493066; -. DR EMBL; U09587; G600727; -. DR MIM; 600287; -. 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. DR PFAM; PF00458; WHEP-TRS; 1. DR PFAM; PF00587; tRNA-synt_2b; 1. DR HSSP; P56206; 1ATI. 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; 36A81DA6 CRC32; 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 //