ID E6UIZ4_RUMA7 Unreviewed; 406 AA.
AC E6UIZ4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 01-MAY-2013, entry version 20.
DE RecName: Full=Tyrosine--tRNA ligase;
DE EC=6.1.1.1;
DE AltName: Full=Tyrosyl-tRNA synthetase;
GN Name=tyrS; OrderedLocusNames=Rumal_1762;
OS Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO
OS 2250 / 7).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC Ruminococcus.
OX NCBI_TaxID=697329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7;
RX PubMed=21914885; DOI=10.1128/JB.05621-11;
RA Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A.,
RA Cheng J.F., Detter C., Detter J.C., Goodwin L.A., Han C.S.,
RA Hauser L.J., Ivanova N.N., Kyrpides N.C., Land M.L., Lapidus A.,
RA Lucas S., Ovchinnikova G., Pitluck S., Tapia R., Woyke T., Boyum J.,
RA Mead D., Weimer P.J.;
RT "Complete Genome of the Cellulolytic Ruminal Bacterium Ruminococcus
RT albus 7.";
RL J. Bacteriol. 193:5574-5575(2011).
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a
CC two-step reaction: tyrosine is first activated by ATP to form Tyr-
CC AMP and then transferred to the acceptor end of tRNA(Tyr) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP +
CC diphosphate + L-tyrosyl-tRNA(Tyr).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family. TyrS type 1 subfamily.
CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
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DR EMBL; CP002403; ADU22260.1; -; Genomic_DNA.
DR RefSeq; YP_004104894.1; NC_014833.1.
DR EnsemblBacteria; ADU22260; ADU22260; Rumal_1762.
DR GeneID; 10078032; -.
DR KEGG; ral:Rumal_1762; -.
DR PATRIC; 45359997; VBIRumAlb150544_2519.
DR HOGENOM; HOG000242790; -.
DR KO; K01866; -.
DR BioCyc; RALB697329:GIWQ-1809-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:HAMAP.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1; -.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR InterPro; IPR024107; Tyr-tRNA-ligase_bac_1.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF01479; S4; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW Ligase; Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT DOMAIN 344 404 S4 RNA-binding (By similarity).
FT MOTIF 39 48 "HIGH" region (By similarity).
FT MOTIF 227 231 "KMSKS" region (By similarity).
FT BINDING 34 34 Tyrosine (By similarity).
FT BINDING 167 167 Tyrosine (By similarity).
FT BINDING 171 171 Tyrosine (By similarity).
FT BINDING 230 230 ATP (By similarity).
SQ SEQUENCE 406 AA; 45531 MW; 3062CA43ABB7656D CRC64;
MTCFEELKRR GLIAQMTDEK ELEELINNGK ATFYIGFDPT ADSLHVGHFM ALCLMKRLQM
AGNKPIALVG GGTGMIGDPS GKTDMRKMLT PETIQHNCEC FKKQMSKFID FSDGKALMVN
NGDWLLNLNY VDVLREVGAC FSVNKMLTFE CYKQRMERGL TFLEFNYMIM QSYDFYRLFQ
DYGCNMQFGG DDQWANMLGG TELIRKKLGK DAYAMTITLL LNSEGKKMGK TEKGAVWLDA
EKTSPYDFYQ YWRNVDDADV IKCLKLLTFV PIEQIEEMEQ HMEGAEYNKA KELLAFELTK
LIHGEEEAQK ADAAAKAIFG GGADSADMPA VTLTADDVDE NKQIGILNLL VKSGLAPSNG
EARRLVQQNG IAVNGEKFTD PKGMVDLSEQ VIIKKGKKVF LKVVLG
//
