Reviewed, UniProtKB/Swiss-Prot Q5P9K5 (SYY_ANAMM)

Names and origin

Protein names

Recommended name:
    Tyrosyl-tRNA synthetase
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase
      Short name=TyrRS

Gene names

Name:	tyrS
Ordered Locus Names:	AM1205

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP MF_02006
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP RNA binding Inferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 414	414	Tyrosyl-tRNA synthetase HAMAP MF_02006		PRO_0000234665
Regions
	Domain	345 – 412	68	S4 RNA-binding
	Motif	43 – 52	10	"HIGH" region HAMAP MF_02006
	Motif	232 – 236	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	38	1	Tyrosine By similarity
	Binding site	172	1	Tyrosine By similarity
	Binding site	176	1	Tyrosine By similarity
	Binding site	235	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5P9K5-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 646549740C663131	FASTA	414	45,566
	10 20 30 40 50 60 MEFKSGFLNT LQVRGYLHQC TDDVALDELM ALQPITAYIG FDCTARSLHI GSLMQIMVMR 70 80 90 100 110 120 YLQKFGHKIV VLLGGGTTKI GDPSGKDKAR AMLSEAEIAA NKAGILATIN KFLNQGDGVV 130 140 150 160 170 180 IADNAEWLGE VRYLEFLREI GSKFSVNAML GLDSVRSRLD RDQNLSFLEF SYVLLQSYDF 190 200 210 220 230 240 VELHRRHKCV LQIGGADQWG NIVNGIDLGR KLGLPQLYGL TTHLLLTSTG EKMGKTADGA 250 260 270 280 290 300 VWLDAEMFDP GNYWQYFRNV ADVEVGRLLR LFTELPMNEI AELENLQGEA INEAKKVLAT 310 320 330 340 350 360 EATAICHGKS AALAAENAAL QVFEHNDDAG LPHFPLHKSL IAQGISVAKL LQLAGLEESI 370 380 390 400 410 SAGRRLIKGR GCKINGMVVE DADHALTHAD FARNSGYITV FCGKKRRIKV VVED

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000030 Genomic DNA. Translation: AAV87025.1.
RefSeq	YP_154280.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5P9K5.
Genome annotation databases
GeneID	3171475.
GenomeReviews	Gene locus AM1205 in contig CP000030_GR.
KEGG	ama:AM1205.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5P9K5.
OMA	TDPTGDS.
Enzyme and pathway databases
BioCyc	AMAR234826:AM1205-MON.
Family and domain databases
HAMAP	MF_02006. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002305. aa-tRNA-synth_Ib. IPR014729. Rossmann-like_a/b/a_fold. IPR002942. S4_RNA_bd. IPR002307. Tyr-tRNA-synth_Ib_bac/mito. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
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. False negative. PS50889. S4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYY_ANAMM

Accession

Primary (citable) accession number: Q5P9K5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	January 4, 2005
Last modified:	November 3, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)