ID SYC_HUMAN STANDARD; PRT; 638 AA. AC P49589; DT 01-FEB-1996 (Rel. 33, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE CYSTEINYL-TRNA SYNTHETASE (EC 6.1.1.16) (CYSTEINE--TRNA LIGASE) DE (CYSRS). GN CARS. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RX MEDLINE; 95078457. RA Cruzen M.E., Arfin S.M.; RT "Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA RT synthetase."; RL DNA Seq. 4:243-248(1994). CC -!- CATALYTIC ACTIVITY: ATP + L-CYSTEINE + TRNA(CYS) = AMP + CC PYROPHOSPHATE + L-CYSTEINYL-TRNA(CYS). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASE FAMILY. 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; L06845; AAA73901.1; -. DR MIM; 123859; -. DR INTERPRO; IPR001412; -. DR INTERPRO; IPR002308; -. DR PFAM; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG. KW Aminoacyl-tRNA synthetase; Protein biosynthesis; Ligase; ATP-binding. FT SIMILAR 57 67 "HIGH" REGION. FT SIMILAR 406 410 "KMSKS" REGION. FT BINDING 409 409 ATP (BY SIMILARITY). SQ SEQUENCE 638 AA; 72318 MW; 101BED7633732196 CRC64; MADSSGQQGK GRRVQPQWSP PAGTQPCRLH LYNSLTRNKE VFIPQDGKKV TWYCCGPTVY DASHMGHARS YISFDILRRV LKDYFKFDVF YCMNITDIDD KIIKRARQNH LFEQYREKRP EAAQLLEDVQ AALKPFSVKL NETTDPDKKQ MLERIQHAVQ LATEPLEKAV QSRLTGEEVN SCVEVLLEEA KDLLSDWLDS TLGCDVTDNS IFSKLPKFWE GDFHRDMEAL NVLPPDVLTR VSEYVPEIVN FVQKIVDNGY GYVSNGSVYF DTAKFASSEK HSYGKLVPEA VGDQKALQEG EGDLSISADR LSEKRSPNDF ALWKASKPGE PSWPCPWGKG RPGWHIECSA MAGTLLGASM DIHGGGFDLR FPHHDNELAQ SEAYFENDCW VRYFLHTGHL TIAGCKMSKS LKNFITIKDA LKKHSARQLR LAFLMHSWKD TLDYSSNTME SALQYEKFLN EFFLNVKDIL RAPVDITGQF EKWGEEEAEL NKNFYDKKTA IHKALCDNVD TRTVMEEMRA LVSQCNLYMA ARKAVRKRPN QALLENIALY LTHMLKIFGA VEEDSSLGFP VGGPGTSLSL EATVMPYLQV LSEFREGVRK IAREQKVPEI LQLSDALRTT SCPSLGCGLK TTKDCPQW //