Reviewed, UniProtKB/Swiss-Prot Q2GIN1 (SYY_ANAPZ)

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:	APH_1244

Organism

Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]

Taxonomic identifier

212042 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

Protein attributes

Sequence length	412 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: 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 – 412	412	Tyrosyl-tRNA synthetase HAMAP MF_02006		PRO_1000088575
Regions
	Domain	343 – 409	67	S4 RNA-binding
	Motif	43 – 52	10	"HIGH" region HAMAP MF_02006
	Motif	230 – 234	5	"KMSKS" region HAMAP MF_02006
Sites
	Binding site	38	1	Tyrosine By similarity
	Binding site	170	1	Tyrosine By similarity
	Binding site	174	1	Tyrosine By similarity
	Binding site	233	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2GIN1-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 82C86389EE3D73FA	FASTA	412	45,726
	10 20 30 40 50 60 MEFNSEFLAT LCARGYLHQL TDATALDGIM SSGAVTAYIG FDCTANSLHI GSLMQIMLLR 70 80 90 100 110 120 YLQRFGHKPI VLLGGATTKV GDPSGKEKTR AMLSEDNISA NKEGILRVIK KFLSEDVVVV 130 140 150 160 170 180 DNAEWLGNYG YLDFLREIGS KFSVNVMLGL ESVKSRLSRD QQLSFLEFSY VLLQSYDFVE 190 200 210 220 230 240 LHKRYGCILQ IGGSDQWGNI VSGIDLARKM GCPQLYGVTT PLLLNSSGAK MGKTADGAIW 250 260 270 280 290 300 LDETLYSPYN YWQYFRNVPD QDVGRLLRLF TELPLSEIER LEALKGEELN EAKKILATAV 310 320 330 340 350 360 TSICHGAEVA LQVENQALKV FEHNDHDELR SITFSRKTLG QGIPISKLLH MWGLEESISA 370 380 390 400 410 GRRLIRGGGC KINGGVVLDE EKLLNCGDFD DNGGYVAVFC GKKRRLKVVL ED

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000235 Genomic DNA. Translation: ABD43829.1.
RefSeq	YP_505770.1.
3D structure databases
SMR	Q2GIN1. Positions 7-313, 8-408.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2GIN1.
Genome annotation databases
GeneID	3930514.
GenomeReviews	Gene locus APH_1244 in contig CP000235_GR.
KEGG	aph:APH_1244.
NMPDR	fig|212042.5.peg.1192.
TIGR	APH_1244.
Phylogenomic databases
eggNOG	COG0162.
HOGENOM	HBG288125.
OMA	TDPTGDS.
PhylomeDB	Q2GIN1.
Enzyme and pathway databases
BioCyc	APHA212042:APH_1244-MONOMER.
Family and domain databases
HAMAP	MF_02006. Tyr_tRNA_synth_type1. [Tree]
InterPro	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_ANAPZ

Accession

Primary (citable) accession number: Q2GIN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	March 21, 2006
Last modified:	February 9, 2010
This is version 35 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)