Q8P455 (SYR_XANCP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine--tRNA ligase
EC=6.1.1.19

Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS

Gene names

Name:	argS
Ordered Locus Names:	XCC3861

Organism

Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]

Taxonomic identifier

190485 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas campestris › Xanthomonas campestris pv. campestris

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	arginyl-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 arginine-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 – 562	562	Arginine--tRNA ligase HAMAP-Rule MF_00123		PRO_0000151638
Regions
	Motif	129 – 139	11	"HIGH" region HAMAP-Rule MF_00123

Sequences

	Sequence		Length	Mass (Da)
	Q8P455 [UniParc]. Last modified October 10, 2002. Version 1. Checksum: 9750B78D230FB1BD	FASTA	562	61,954
	10 20 30 40 50 60 MKAQLRALIG QGIEALRANG TLPADTLPPD FVVERPKTRE HGDFATNAAM LLAKAARSNP 70 80 90 100 110 120 RALAQALLAA LPASDDVARV EIAGPGFINF HLTPAAYQRE VIHVIKQGHD YGRGLAGNGR 130 140 150 160 170 180 SVGVEYVSAN PTGPLHVGHG RAAAIGDSLA RVLDANGWNV KREFYYNDAG VQIENLALSV 190 200 210 220 230 240 QARAQGLTPD SAGWPENGYR GDYIADVAKA YLAGDTVDLE GHLVTGTKDP ADLESIRRFA 250 260 270 280 290 300 VAYLRNEQNH DLAAFRVDFD IYFLESSLYK DGKVDEAVQK LIASGHTYEE GGALWLKSTD 310 320 330 340 350 360 FGDDKDRVMR KSDGTYTYFV PDVAYHLTKW QRGYERAITE LGADHHGSLT RVRAGLQAME 370 380 390 400 410 420 LGIPQGWPEY VLHQMVTVMR GGEEVKLSKR AGSYVTLRDL IEETSADAVR WFLIARKPDS 430 440 450 460 470 480 QLTFDIDLAR AQSNDNPVFY VQYAHARVCS VLRQAQEKGL KYDQTHGMAE LARLDDEHSL 490 500 510 520 530 540 ALMLELSRYA EVVELAGQTL EPYQIAQYLR ELAHAFHTWY HNSKVLVDDA AERDAKLTLA 550 560 VATQQVLANG LELLGVSAPE KM

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM43092.1.
RefSeq	NP_639201.1. NC_003902.1.
3D structure databases
ProteinModelPortal	Q8P455.
ModBase	Search...
Protein-protein interaction databases
STRING	190485.XCC3861.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM43092; AAM43092; XCC3861.
GeneID	1000443.
KEGG	xcc:XCC3861.
PATRIC	24078900. VBIXanCam115730_4130.
Phylogenomic databases
eggNOG	COG0018.
HOGENOM	HOG000247214.
KO	K01887.
OMA	HTSANPN.
ProtClustDB	PRK01611.
Family and domain databases
Gene3D	3.30.1360.70. 1 hit. 3.40.50.620. 1 hit.
HAMAP	MF_00123. Arg_tRNA_synth.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-ligase_Ia. IPR015945. Arg-tRNA-synth_Ia_core. IPR005148. Arg-tRNA-synth_N. IPR008909. DALR_anticod-bd. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view]
PANTHER	PTHR11956. PTHR11956. 1 hit.
Pfam	PF03485. Arg_tRNA_synt_N. 1 hit. PF05746. DALR_1. 1 hit. PF00750. tRNA-synt_1d. 1 hit. [Graphical view]
PRINTS	PR01038. TRNASYNTHARG.
SMART	SM01016. Arg_tRNA_synt_N. 1 hit. SM00836. DALR_1. 1 hit. [Graphical view]
SUPFAM	SSF55190. Arg-tRNA-synth_Ic_N. 1 hit. SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMs	TIGR00456. argS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYR_XANCP

Accession

Primary (citable) accession number: Q8P455

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	October 10, 2002
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program