ID SYC_HUMAN STANDARD; PRT; 748 AA. AC P49589; Q9HD24; Q9HD25; DT 01-FEB-1996 (Rel. 33, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Cysteinyl-tRNA synthetase (EC 6.1.1.16) (Cysteine--tRNA ligase) DE (CysRS). GN Name=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; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP + CC diphosphate + L-cysteinyl-tRNA(Cys). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P49589-1; Sequence=Displayed; CC Name=2; CC IsoId=P49589-2; Sequence=VSP_006312; CC Note=Found in 20% of the 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 HSSP; P21888; 1LI5. DR Genew; HGNC:1493; CARS. DR MIM; 123859; -. DR GO; GO:0005737; C:cytoplasm; TAS. DR GO; GO:0005625; C:soluble fraction; TAS. DR GO; GO:0000049; F:tRNA binding; TAS. DR InterPro; IPR002308; Cys_tRNA-synt_1a. DR InterPro; IPR001412; tRNA-synt_I. DR InterPro; IPR009080; tRNAsyn_1a_bind. DR Pfam; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. DR TIGRFAMs; TIGR00435; cysS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG. KW Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; KW Metal-binding; Protein biosynthesis; Zinc. FT SITE 57 67 "HIGH" region. FT SITE 406 410 "KMSKS" region. FT BINDING 409 409 ATP (By similarity). FT METAL 55 55 Zinc (By similarity). FT METAL 348 348 Zinc (By similarity). FT METAL 373 373 Zinc (By similarity). FT METAL 377 377 Zinc (By similarity). FT VARSPLIC 705 748 GLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNG FT SFQ -> VSMVCPHMTWRAKSSAKGKPRS (in isoform FT 2). FT /FTId=VSP_006312. 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 //