P37880 (SYRC_CRIGR) 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
Synonyms:	RRS1

Organism

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	661 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.
Domain	The N-terminus (AA 1-73) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative initiation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
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...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform Complexed (identifier: P37880-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Monomeric (identifier: P37880-2)

Also known as: Free;

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

Note: The alternative initiation site Met-74 is uncertain.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 661	661	Arginine--tRNA ligase, cytoplasmic		PRO_0000035795
Regions
	Region	1 – 73	73	Could be involved in the assembly of the multisynthetase complex
	Motif	202 – 213	12	"HIGH" region
Natural variations
	Alternative sequence	1 – 73	73	Missing in isoform Monomeric.		VSP_018904

Sequences

	Sequence		Length	Mass (Da)
	Isoform Complexed [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 12EB1C85655EB8F4	FASTA	661	75,602
	10 20 30 40 50 60 MDGLVAQCSA RLLQQEKEIK SLTAEIDRLK NCGHLEDSPS LDQLREENLK LKYRLNILQR 70 80 90 100 110 120 SLQAEKRRRP TKNMININSR LQDVFGCAIK AAYPDLDNPP LVVTPSQQPK FGDYQCNSAM 130 140 150 160 170 180 GISQMLKAKE QKVNPRGIAE NITKHLPNNE YIDRVEIAGP GFINVHLRKD FVSEQLTNLL 190 200 210 220 230 240 VNGIQLPALG ENKKVIVDFS SPNIAKEMHV GHLRSTIIGE SMSRLFEFAG YDVLRLNHVG 250 260 270 280 290 300 DWGTQFGMLI AHLQDQFPDY LTVSPPIGDL QAFYKESKKR FDTEEEFKKR AYQCVVSLQS 310 320 330 340 350 360 KDPDFIKAWN LICDVSRAEF NKIYDALDIT LIERGESFYQ DRMKDIVKEF EDKGYVQVDD 370 380 390 400 410 420 GRKIVFVPGC SIPLTIVKSD GGFTYDTSDL AAIKQRLFEE KANKIIYVVD NGQAVHFQTI 430 440 450 460 470 480 FAAAQMIGWY DPKVTQVTHV GFGVVLGEDK KKFKTRSGET VRLVDLLGEG LKRSMDKLKE 490 500 510 520 530 540 KERDKVLTEE ELTAAQTSIA YGCIKYADLS HNRLNDYIFS FDKMLDDRGN TAAYLLYAFT 550 560 570 580 590 600 RIRSIARLAN VDEEMLQKAA RETKIVLDHE KEWKLGRCIL RFPEILQKML DDLFLHTLCD 610 620 630 640 650 660 YIYELATTFT EFYDSCYCVE KDRQTGKVLK VNMWRMLLCE AVAAVMAKGF DILGIKPVQR M
	Isoform Monomeric (Free) [UniParc]. Checksum: 623A7303E0156F90	FASTA	588	67,088
	10 20 30 40 50 60 MININSRLQD VFGCAIKAAY PDLDNPPLVV TPSQQPKFGD YQCNSAMGIS QMLKAKEQKV 70 80 90 100 110 120 NPRGIAENIT KHLPNNEYID RVEIAGPGFI NVHLRKDFVS EQLTNLLVNG IQLPALGENK 130 140 150 160 170 180 KVIVDFSSPN IAKEMHVGHL RSTIIGESMS RLFEFAGYDV LRLNHVGDWG TQFGMLIAHL 190 200 210 220 230 240 QDQFPDYLTV SPPIGDLQAF YKESKKRFDT EEEFKKRAYQ CVVSLQSKDP DFIKAWNLIC 250 260 270 280 290 300 DVSRAEFNKI YDALDITLIE RGESFYQDRM KDIVKEFEDK GYVQVDDGRK IVFVPGCSIP 310 320 330 340 350 360 LTIVKSDGGF TYDTSDLAAI KQRLFEEKAN KIIYVVDNGQ AVHFQTIFAA AQMIGWYDPK 370 380 390 400 410 420 VTQVTHVGFG VVLGEDKKKF KTRSGETVRL VDLLGEGLKR SMDKLKEKER DKVLTEEELT 430 440 450 460 470 480 AAQTSIAYGC IKYADLSHNR LNDYIFSFDK MLDDRGNTAA YLLYAFTRIR SIARLANVDE 490 500 510 520 530 540 EMLQKAARET KIVLDHEKEW KLGRCILRFP EILQKMLDDL FLHTLCDYIY ELATTFTEFY 550 560 570 580 DSCYCVEKDR QTGKVLKVNM WRMLLCEAVA AVMAKGFDIL GIKPVQRM

References

[1]	"Cloning and analysis of a cDNA encoding mammalian arginyl-tRNA synthetase, a component of the multisynthetase complex with a hydrophobic N-terminal extension." Lazard M., Mirande M. Gene 132:237-245(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X63415 mRNA. Translation: CAA45012.1.
3D structure databases
ProteinModelPortal	P37880.
ModBase	Search...
Proteomic databases
PRIDE	P37880.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG029238.
Enzyme and pathway databases
SABIO-RK	P37880.
Family and domain databases
Gene3D	3.30.1360.70. 1 hit. 3.40.50.620. 1 hit.
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

SYRC_CRIGR

Accession

Primary (citable) accession number: P37880

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program