Q3ILJ9 (SYY2_PSEHT) 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
Ordered Locus Names:	PSHAa0545

Organism

Pseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]

Taxonomic identifier

326442 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas

Protein attributes

Sequence length	399 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_02007
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr). HAMAP MF_02007
Subunit structure	Homodimer By similarity. HAMAP MF_02007
Subcellular location	Cytoplasm By similarity HAMAP MF_02007.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 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 – 399	399	Tyrosine--tRNA ligase 2 HAMAP MF_02007		PRO_0000236749
Regions
	Domain	336 – 398	63	S4 RNA-binding
	Motif	41 – 50	10	"HIGH" region HAMAP MF_02007
	Motif	225 – 229	5	"KMSKS" region HAMAP MF_02007
Sites
	Binding site	228	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3ILJ9 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: A2EDA9154F632B6D	FASTA	399	44,283
	10 20 30 40 50 60 MDLQTALAEI KRGTEEILIE DELVEKLKSG KKLKIKAGFD PTAPDLHLGH TVLINKMKTF 70 80 90 100 110 120 QDLGHEVVFL IGDFTGMIGD PTGKNVTRKP LTREDVLANA ETYKEQVFKI LDPAKTTVAF 130 140 150 160 170 180 NSTWMENLGA AGMIKLAARQ TVARMLERDD FKKRYASGQS IAIHEFLYPL VQGWDSVALE 190 200 210 220 230 240 ADVELGGTDQ RFNLLMGREL QKDEGQKPQT VIMTPLLEGT DGVQKMSKSL GNYIGITDAP 250 260 270 280 290 300 NDMFGKIMSI SDVLMWRYYD LLSGLSIAGI NAQKERVEQG TNPRDIKIEL AKELIARFHS 310 320 330 340 350 360 EADAQAAHDD FIQRFQKKAL PDEIPELTVT IEQDSILIAN LLKEANLVAS TSEAMRMIKQ 370 380 390 GAVKLNGEDK ITDTKLEIAK GSTAIYQVGK RKFANITVA

References

[1]

"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125." Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A. Genome Res. 15:1325-1335(2005) [PubMed: 16169927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TAC 125.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR954246 Genomic DNA. Translation: CAI85633.1.
RefSeq	YP_339076.1. NC_007481.1.
3D structure databases
ProteinModelPortal	Q3ILJ9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3ILJ9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3710331.
GenomeReviews	Gene locus PSHAa0545 in contig CR954246_GR.
KEGG	pha:PSHAa0545.
NMPDR	fig|326442.4.peg.519.
PATRIC	32294617. VBIPseHal105694_0514.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0162.
HOGENOM	HBG288125.
OMA	YVVQVGK.
PhylomeDB	Q3ILJ9.
Enzyme and pathway databases
BioCyc	PHAL326442:PSHAA0545-MONOMER.
Family and domain databases
HAMAP	MF_02007. Tyr_tRNA_synth_type2. [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. IPR024108. Tyr-tRNA-synth_bac_2. [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	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_PSEHT

Accession

Primary (citable) accession number: Q3ILJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	November 8, 2005
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program