ID SYC_HUMAN STANDARD; PRT; 595 AA. AC P49589; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE CYSTEINYL-TRNA SYNTHETASE (EC 6.1.1.16) (CYSTEINE--TRNA LIGASE) DE (CYSRS) (FRAGMENT). GN CARS. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RX MEDLINE; 95078457. RA CRUZEN M.E., ARFIN S.M.; 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 SYNTHETASES. 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; G927229; -. DR MIM; 123859; 11TH EDITION. KW AMINOACYL-TRNA SYNTHASE; PROTEIN BIOSYNTHESIS; LIGASE; ATP-BINDING. FT NON_TER 1 1 FT SIMILAR 14 24 "HIGH" REGION. FT SIMILAR 363 367 "KMSKS" REGION. FT BINDING 366 366 ATP (BY SIMILARITY). SQ SEQUENCE 595 AA; 67495 MW; B9750DA6 CRC32; PQDGKKVTWY CCGPTVYDAS HMGHARSYIS FDILRRVLKD YFKFDVFYCM NITDIDDKII KRARQNHLFE QYREKRPEAA QLLEDVQAAL KPFSVKLNET TDPDKKQMLE RIQHAVQLAT EPLEKAVQSR LTGEEVNSCV EVLLEEAKDL LSDWLDSTLG CDVTDNSIFS KLPKFWEGDF HRDMEALNVL PPDVLTRVSE YVPEIVNFVQ KIVDNGYGYV SNGSVYFDTA KFASSEKHSY GKLVPEAVGD QKALQEGEGD LSISADRLSE KRSPNDFALW KASKPGEPSW PCPWGKGRPG WHIECSAMAG TLLGASMDIH GGGFDLRFPH HDNELAQSEA YFENDCWVRY FLHTGHLTIA GCKMSKSLKN FITIKDALKK HSARQLRLAF LMHSWKDTLD YSSNTMESAL QYEKFLNEFF LNVKDILRAP VDITGQFEKW GEEEAELNKN FYDKKTAIHK ALCDNVDTRT VMEEMRALVS QCNLYMAARK AVRKRPNQAL LENIALYLTH MLKIFGAVEE DSSLGFPVGG PGTSLSLEAT VMPYLQVLSE FREGVRKIAR EQKVPEILQL SDALRTTSCP SLGCGLKTTK DCPQW //