Q5RA20 (SYRC_PONAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine--tRNA ligase, cytoplasmic
EC=6.1.1.19

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

Gene names

Name:

RARS

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	660 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 By similarity.
Catalytic activity	ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).
Subunit structure	Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts with EPRS (via N-terminus). Interacts with LARS2. Monomer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly 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
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	arginyl-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 arginine-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 – 660	660	Arginine--tRNA ligase, cytoplasmic		PRO_0000250728
Regions
	Region	1 – 72	72	Could be involved in the assembly of the multisynthetase complex
	Motif	201 – 212	12	"HIGH" region
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	38	1	Phosphoserine By similarity
	Modified residue	60	1	N6-acetyllysine By similarity
	Modified residue	205	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	164	1	I → V in CAI29693. Ref.1
	Sequence conflict	271	1	V → A in CAI29693. Ref.1
	Sequence conflict	402	1	Missing in CAI29693. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q5RA20 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: C114CA5ED797D8E8	FASTA	660	75,344
	10 20 30 40 50 60 MDVLVTECSA RLLQQEEEIK SLTAEIDRLK NCGCLGASAN LEQLQEENLK LKYRLNILQK 70 80 90 100 110 120 SLQAERNKPT KNMINVISRL QEVFGHAIKA AYPDLENPPL LVTPSQQAKF GDYQCNSAMG 130 140 150 160 170 180 ISQMLKTKEQ KVNPREIAEN ITKHLPDNEC IEKVEIAGPG FINIHLRKDF VSEQLTSLLV 190 200 210 220 230 240 NGVQLPALGE NKKVIVDFSS PNIAKEMHVG HLRSTIIGES ISRLFEFAGY DVLRLNHIGD 250 260 270 280 290 300 WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ VFYKESKKRF DTEEEFKKRA YQCVVLLQGK 310 320 330 340 350 360 NPDITKAWKL ICDVSRQELN KIYDALDVSL IERGESFYQD MMNDIVKEFE DRGFVQVDDG 370 380 390 400 410 420 RKIVFVPGCS IPLTILKSDG GYTYDTSDLA AIKQRLFEEK ADMIIYVVDN GQSVHFQTIF 430 440 450 460 470 480 AAAQMIGWYD PKVTRVFHAG FGVVLGEDKK KFKTRSGETV RLMDLLGEGL KRSMDKLKEK 490 500 510 520 530 540 ERDKVLTAEE LNAAQTSIAY GCVKYADLSH NRLNDYIFSF DKMLDDKGNT AAYLLYAFTR 550 560 570 580 590 600 IRSIARLANI DEEMLQKAAR ETKILLDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 610 620 630 640 650 660 IYELATTFTE FYDSCYCVEK DRQTGKILKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR859203 mRNA. Translation: CAH91390.1. CR926065 mRNA. Translation: CAI29693.1.
RefSeq	NP_001127107.1. NM_001133635.1.
UniGene	Pab.18398.
3D structure databases
ProteinModelPortal	Q5RA20.
ModBase	Search...
Proteomic databases
PRIDE	Q5RA20.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100174147.
KEGG	pon:100174147.
Organism-specific databases
CTD	5917.
Phylogenomic databases
HOVERGEN	HBG029238.
InParanoid	Q5RA20.
Family and domain databases
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-synth_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]
Gene3D	G3DSA:3.30.1360.70. Arg-tRNA-synth_Ic_N. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01887.
PANTHER	PTHR11956. Arg_tRNA-synt_1c. 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

SYRC_PONAB

Accession

Primary (citable) accession number: Q5RA20
Secondary accession number(s): Q5NVH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	December 21, 2004
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program