SYY2_BACAN
ID SYY2_BACAN Reviewed; 419 AA.
AC Q81XC6; Q6HR61; Q6KKH8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Tyrosine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_02006};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE AltName: Full=Tyrosyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_02006};
DE Short=TyrRS 2 {ECO:0000255|HAMAP-Rule:MF_02006};
GN Name=tyrS2 {ECO:0000255|HAMAP-Rule:MF_02006}; Synonyms=tyrS-2;
GN OrderedLocusNames=BA_5314, GBAA_5314, BAS4936;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr). {ECO:0000255|HAMAP-
CC Rule:MF_02006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02006};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}.
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DR EMBL; AE016879; AAP28976.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34447.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57227.1; -; Genomic_DNA.
DR RefSeq; NP_847490.1; NC_003997.3.
DR RefSeq; WP_001021109.1; NZ_WXXJ01000007.1.
DR RefSeq; YP_031177.1; NC_005945.1.
DR AlphaFoldDB; Q81XC6; -.
DR SMR; Q81XC6; -.
DR STRING; 260799.BAS4936; -.
DR DNASU; 1084812; -.
DR EnsemblBacteria; AAP28976; AAP28976; BA_5314.
DR EnsemblBacteria; AAT34447; AAT34447; GBAA_5314.
DR GeneID; 45024921; -.
DR KEGG; ban:BA_5314; -.
DR KEGG; bar:GBAA_5314; -.
DR KEGG; bat:BAS4936; -.
DR PATRIC; fig|198094.11.peg.5274; -.
DR eggNOG; COG0162; Bacteria.
DR HOGENOM; CLU_024003_0_3_9; -.
DR OMA; YHSSVQA; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 1.
DR CDD; cd00805; TyrRS_core; 1.
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; IPR036986; S4_RNA-bd_sf.
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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..419
FT /note="Tyrosine--tRNA ligase 2"
FT /id="PRO_0000234668"
FT DOMAIN 352..418
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT MOTIF 39..48
FT /note="'HIGH' region"
FT MOTIF 230..234
FT /note="'KMSKS' region"
FT BINDING 34
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 168
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 172
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ SEQUENCE 419 AA; 47350 MW; F276833EAC7D6F61 CRC64;
MNIIDELEWR GAVNQQTDEE GLRKLVEEKK ISLYCGVDPT GDSMHIGHLI PFMMMKRFQL
AGHHPVILIG GATGTIGDPS GRQSERQLQT LEVVQHNVDA LTAQMKKLFD FGGNSEVKMV
NNYDWTHEIN IIEFLRDYGK NFSINSMLAK DIVASRLDTG ISFTEFTYQI LQAMDFHHLY
TKEDVQLQIG GSDQWGNITS GLDLIRKLEG HEAKVFGLTI PLLLKSDGTK FGKSAGGAVW
LDPEKTTPFE FYQFWVNTDD RDVVKYLKYF TFLTKERIDE LAVKVETEPH KREAQKVLAE
EMTKFVHGEE ALLQAVKITA ALFSGDIKSL TADEIEQGFK EMPTFQSSKE TKNIVEWLVD
LGIEPSRRQA REDINNGAIS MNGEKVTDVG TDVTVENSFD GRFIIIRKGK KNYSLVKLG
