ID SYY_THICR Reviewed; 398 AA.
AC Q31E84;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 29-MAY-2013, entry version 51.
DE RecName: Full=Tyrosine--tRNA ligase;
DE EC=6.1.1.1;
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
GN Name=tyrS; OrderedLocusNames=Tcr_1949;
OS Thiomicrospira crunogena (strain XCL-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J.,
RA Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R.,
RA Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A.,
RA Freyermuth S.K., Harmer T.L., Hauser L.J., Huegler M., Kerfeld C.A.,
RA Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L.,
RA Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z.,
RA Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T.,
RA Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E.,
RA Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira
RT crunogena XCL-2.";
RL PLoS Biol. 4:1-17(2006).
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 2 subfamily.
CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
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DR EMBL; CP000109; ABB42539.1; -; Genomic_DNA.
DR RefSeq; YP_392213.1; NC_007520.2.
DR ProteinModelPortal; Q31E84; -.
DR STRING; 317025.Tcr_1949; -.
DR EnsemblBacteria; ABB42539; ABB42539; Tcr_1949.
DR GeneID; 3761149; -.
DR KEGG; tcx:Tcr_1949; -.
DR PATRIC; 23976020; VBIThiCru83387_2032.
DR eggNOG; COG0162; -.
DR HOGENOM; HOG000242791; -.
DR KO; K01866; -.
DR OMA; GGNDQKF; -.
DR BioCyc; TCRU317025:GHE8-2005-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_02007; Tyr_tRNA_synth_type2; 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; IPR024108; Tyr-tRNA-ligase_bac_2.
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 CHAIN 1 398 Tyrosine--tRNA ligase.
FT /FTId=PRO_0000236774.
FT DOMAIN 335 396 S4 RNA-binding.
FT MOTIF 43 52 "HIGH" region.
FT MOTIF 227 231 "KMSKS" region.
FT BINDING 230 230 ATP (By similarity).
SQ SEQUENCE 398 AA; 44602 MW; 4D807BBD7CD02909 CRC64;
MMKTVEEQMA VIQRGAEEIL VEKELIEKLK KGKPLKIKAG FDPTAPDLHL GHTVLINKLR
QFQDLGHEIL FLIGDFTAMI GDPTGKSATR PPLSEEDVLK NAETYKEQVF KILDPAKTKV
VFNSEWMSKL SAADMIKLAG TTTVARMLER NDFGERYQSN TPIAIHEFLY PLVQGYDSVA
LDSDIELGGT DQKFNLLMGR TLQQHYGKEA QCTLTMPILE GLDGVQKMSK SLNNYIGIKD
APNDMFGKVM SVSDELMWRY FELLSFESLE TIAGYKDAVA NGENPRNIKI KLALELIERF
HDKESAEAAL KDFETRFSKN AIPDEMPEFT FNEVMPLANL LKEAGLVSST SDGHRMVKQG
AVKLNGEKVT DSRAPVENCE QQVYQVGKRK FARITVAA
//
