Q81XC6 (SYY2_BACAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine--tRNA ligase 2
EC=6.1.1.1

Alternative name(s):
Tyrosyl-tRNA synthetase 2
Short name=TyrRS 2

Gene names

Name:	tyrS2
Synonyms:	tyrS-2
Ordered Locus Names:	BA_5314, GBAA_5314, BAS4936

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) By similarity. HAMAP MF_02006
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP MF_02006
Subunit structure	Homodimer By similarity. HAMAP MF_02006
Subcellular location	Cytoplasm By similarity HAMAP MF_02006.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. Contains 1 S4 RNA-binding domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	tyrosyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 419	419	Tyrosine--tRNA ligase 2 HAMAP MF_02006		PRO_0000234668
Regions
	Domain	352 – 418	67	S4 RNA-binding
	Motif	39 – 48	10	"HIGH" region HAMAP MF_02006
	Motif	230 – 234	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	34	1	Tyrosine By similarity
	Binding site	168	1	Tyrosine By similarity
	Binding site	172	1	Tyrosine By similarity
	Binding site	233	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81XC6 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: F276833EAC7D6F61	FASTA	419	47,350
	10 20 30 40 50 60 MNIIDELEWR GAVNQQTDEE GLRKLVEEKK ISLYCGVDPT GDSMHIGHLI PFMMMKRFQL 70 80 90 100 110 120 AGHHPVILIG GATGTIGDPS GRQSERQLQT LEVVQHNVDA LTAQMKKLFD FGGNSEVKMV 130 140 150 160 170 180 NNYDWTHEIN IIEFLRDYGK NFSINSMLAK DIVASRLDTG ISFTEFTYQI LQAMDFHHLY 190 200 210 220 230 240 TKEDVQLQIG GSDQWGNITS GLDLIRKLEG HEAKVFGLTI PLLLKSDGTK FGKSAGGAVW 250 260 270 280 290 300 LDPEKTTPFE FYQFWVNTDD RDVVKYLKYF TFLTKERIDE LAVKVETEPH KREAQKVLAE 310 320 330 340 350 360 EMTKFVHGEE ALLQAVKITA ALFSGDIKSL TADEIEQGFK EMPTFQSSKE TKNIVEWLVD 370 380 390 400 410 LGIEPSRRQA REDINNGAIS MNGEKVTDVG TDVTVENSFD GRFIIIRKGK KNYSLVKLG

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016879 Genomic DNA. Translation: AAP28976.1. AE017334 Genomic DNA. Translation: AAT34447.1. AE017225 Genomic DNA. Translation: AAT57227.1.
RefSeq	NP_847490.1. NC_003997.3. YP_021972.1. NC_007530.2. YP_031177.1. NC_005945.1.
3D structure databases
ProteinModelPortal	Q81XC6.
SMR	Q81XC6. Positions 2-319.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000012187; EBBACP00000011943; EBBACG00000012179. EBBACT00000017051; EBBACP00000016672; EBBACG00000017042. EBBACT00000024490; EBBACP00000023975; EBBACG00000024481.
GeneID	1084812. 2818712. 2850048.
GenomeReviews	Gene locus BA_5314 in contig AE016879_GR. Gene locus BAS4936 in contig AE017225_GR. Gene locus GBAA_5314 in contig AE017334_GR.
KEGG	ban:BA_5314. bar:GBAA_5314. bat:BAS4936.
TIGR	BA_5314. GBAA_5314.
Phylogenomic databases
GeneTree	EBGT00050000000599.
HOGENOM	HBG288125.
OMA	LVHGQEG.
ProtClustDB	PRK13354.
Enzyme and pathway databases
BioCyc	BANT260799:BAS4936-MONOMER. BANT261594:GBAA5314-MONOMER.
Family and domain databases
HAMAP	MF_02006. Tyr_tRNA_synth_type1. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ic. IPR014729. Rossmann-like_a/b/a_fold. IPR002942. S4_RNA-bd. IPR002307. Tyr-tRNA-synth. IPR024088. Tyr-tRNA-synth_bac-type. IPR024107. Tyr-tRNA-synth_bac_1. [Graphical view]
Gene3D	G3DSA:3.10.290.10. G3DSA:3.10.290.10. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01866.
PANTHER	PTHR11766. Tyr_tRNA-synt_1b. 1 hit.
Pfam	PF01479. S4. 1 hit. PF00579. tRNA-synt_1b. 1 hit. [Graphical view]
PRINTS	PR01040. TRNASYNTHTYR.
SMART	SM00363. S4. 1 hit. [Graphical view]
TIGRFAMs	TIGR00234. TyrS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. PS50889. S4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYY2_BACAN

Accession

Primary (citable) accession number: Q81XC6
Secondary accession number(s): Q6HR61, Q6KKH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program