A8FGA6 (SYY_BACP2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine--tRNA ligase
EC=6.1.1.1

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

Gene names

Name:	tyrS
Ordered Locus Names:	BPUM_2615

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]

Taxonomic identifier

315750 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	422 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
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 – 422	422	Tyrosine--tRNA ligase HAMAP MF_02006		PRO_1000088577
Regions
	Domain	355 – 421	67	S4 RNA-binding
	Motif	40 – 49	10	"HIGH" region HAMAP MF_02006
	Motif	232 – 236	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	35	1	Tyrosine By similarity
	Binding site	170	1	Tyrosine By similarity
	Binding site	174	1	Tyrosine By similarity
	Binding site	235	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8FGA6 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: BFED2C23DB8A40C5	FASTA	422	47,685
	10 20 30 40 50 60 MSQLMEELSF RGLIQQQTDE EGLTKLLAEE KIKLYSGFDP TADSLHIGHL LPILTLRRFQ 70 80 90 100 110 120 EAGHHPIALV GGATGLIGDP SFKKAERSLN PAEIVEHWSD KIKGQLSQFL DFEAGENPAV 130 140 150 160 170 180 IVNNYDWISQ MNVITFLRDI GKNFGVNFML AKDIVSSRIE TGISYTEFSY VILQSLDFLN 190 200 210 220 230 240 LYRNENCKLQ IGGSDQWGNI TSGLELIRKS EAEGAKAFGL TMPLVTKADG TKFGKTEGGA 250 260 270 280 290 300 IWLDKEKTSP YEFYQFWINT DDRDVVKYLK YFTFLSKEEI ASYEEKVQTA PEKREAQRRL 310 320 330 340 350 360 AEEVTTLVHG RESLEQAVNI SNALFKGEIK SLSAEEVKVG FKDVPSMEKS STEELTLVDL 370 380 390 400 410 420 LVESKLSPSK RQAREDITNG AVSINGERQT DKDYVLSAED RIENQFTVLR RGKKKYFLVT YK

References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. , Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., Weinstock G.M. PLoS ONE 2:E928-E928(2007) [PubMed: 17895969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SAFR-032.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000813 Genomic DNA. Translation: ABV63273.1.
RefSeq	YP_001487833.1. NC_009848.1.
3D structure databases
ProteinModelPortal	A8FGA6.
SMR	A8FGA6. Positions 4-321.
ModBase	Search...
Protein-protein interaction databases
STRING	A8FGA6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000066327; EBBACP00000064660; EBBACG00000066318.
GeneID	5621885.
GenomeReviews	Gene locus BPUM_2615 in contig CP000813_GR.
KEGG	bpu:BPUM_2615.
PATRIC	18969168. VBIBacPum16546_2678.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0162.
GeneTree	EBGT00050000000599.
HOGENOM	HBG288125.
OMA	TFYIGFD.
ProtClustDB	PRK05912.
Enzyme and pathway databases
BioCyc	BPUM315750:BPUM_2615-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

SYY_BACP2

Accession

Primary (citable) accession number: A8FGA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program