ID SYC_HUMAN STANDARD; PRT; 748 AA. AC P49589; Q9HD25; Q9HD24; DT 01-FEB-1996 (Rel. 33, Created) DT 01-MAR-2002 (Rel. 41, Last sequence update) DT 01-MAR-2002 (Rel. 41, 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. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Brain; RX MEDLINE=95078457; PubMed=7987009; 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). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RX MEDLINE=21245111; PubMed=11347887; RA Davidson E., Caffarella J., Vitseva O., Hou Y.M., King M.P.; RT "Isolation of two cDNAs encoding functional human cytoplasmic RT cysteinyl-tRNA synthetase."; RL Biol. Chem. 382:399-406(2001). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 1). RC TISSUE=Lung; RA Strausberg R.; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP + CC diphosphate + L-cysteinyl-tRNA(Cys). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- ALTERNATIVE PRODUCTS: 2 isoforms; 1 (shown here) and 2; are CC produced by alternative splicing. Isoform 2 is found in 20% of the CC mRNAs. CC -!- SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASE FAMILY. CC -!- CAUTION: Ref.1 sequence differs from that shown due to a CC frameshift in position 619. 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; ALT_FRAME. DR EMBL; AF288206; AAG00578.1; -. DR EMBL; AF288207; AAG00579.1; -. DR EMBL; BC002880; AAH02880.1; -. DR MIM; 123859; -. DR InterPro; IPR002308; tRNA-synt_1e. DR InterPro; IPR001412; tRNA-synt_I. 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; KW Alternative splicing. FT SITE 57 67 "HIGH" REGION. FT SITE 406 410 "KMSKS" REGION. FT BINDING 409 409 ATP (BY SIMILARITY). FT VARSPLIC 705 748 GLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNG FT SFQ -> VSMVCPHMTWRAKSSAKGKPRS (IN ISOFORM FT 2). SQ SEQUENCE 748 AA; 85473 MW; D0B7A29EC03AA87F 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 LQLSDALRDN ILPELGVRFE DHEGLPTVVK LVDRNTLLKE REEKRRVEEE KRKKKEEAAR RKQEQEAAKL AKMKIPPSEM FLSETDKYSK FDENGLPTHD MEGKELSKGQ AKKLKKLFEA QEKLYKEYLQ MAQNGSFQ //