Q93RP5 (Q93RP5_THETH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Arginine--tRNA ligase HAMAP MF_00123
EC=6.1.1.19 HAMAP MF_00123

Alternative name(s):
Arginyl-tRNA synthetase HAMAP MF_00123

Gene names

Name:

argS HAMAP MF_00123 EMBL CAC39622.1

Organism

Thermus thermophilus EMBL CAC39622.1

Taxonomic identifier

274 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP MF_00123
Subunit structure	Monomer By similarity. HAMAP MF_00123
Subcellular location	Cytoplasm By similarity HAMAP MF_00123.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. RuleBase RU003489 HAMAP MF_00123

Ontologies

Keywords
Biological process	Protein biosynthesis RuleBase RU003489 HAMAP MF_00123
Cellular component	Cytoplasm HAMAP MF_00123
Ligand	ATP-binding RuleBase RU003489 HAMAP MF_00123 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase RuleBase RU003489 HAMAP MF_00123 EMBL CAC39622.1 Ligase
Technical term	3D-structure PDB 1IQ0
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
Regions
	Motif	112 – 122	11	"HIGH" region By similarity HAMAP MF_00123

Sequences

	Sequence		Length	Mass (Da)
	Q93RP5 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: BA300E5F28F672E6	FASTA	592	66,227
	10 20 30 40 50 60 MLRRALEEAI AQALKEMGVP VRLKVARAPK DKPGDYGVPL FALAKELRKP PQAIAQELKD 70 80 90 100 110 120 RLPLPEFVEE AVPVGGYLNF RLRTEALLRE ALRPKAPFPR RPGVVLVEHT SVNPNKELHV 130 140 150 160 170 180 GHLRNIALGD AIARILAYAG REVLVLNYID DTGRQAAETL FALRHYGLTW DGKEKYDHFA 190 200 210 220 230 240 GRAYVRLHQD PEYERLQPAI EEVLHALERG ELREEVNRIL LAQMATMHAL NARYDLLVWE 250 260 270 280 290 300 SDIVRAGLLQ KALALLEQSP HVFRPREGKY AGALVMDASP VIPGLEDPFF VLLRSNGTAT 310 320 330 340 350 360 YYAKDIAFQF WKMGILEGLR FRPYENPYYP GLRTSAPEGE AYTPKAEETI NVVDVRQSHP 370 380 390 400 410 420 QALVRAALAL AGYPALAEKA HHLAYETVLL EGRQMSGRKG LAVSVDEVLE EATRRARAIV 430 440 450 460 470 480 EEKNPDHPDK EEAARMVALG AIRFSMVKTE PKKQIDFRYQ EALSFEGDTG PYVQYAHARA 490 500 510 520 530 540 HSILRKAGEW GAPDLSQATP YERALALDLL DFEEAVLEAA EERTPHVLAQ YLLDLAASWN 550 560 570 580 590 AYYNARENGQ PATPVLTAPE GLRELRLSLV QSLQRTLATG LDLLGIPAPE VM

References

[1]	"Gene cloning, expression, crystallization and preliminary X-ray analysis of Thermus thermophilus arginyl-tRNA synthetase." Shimada A., Nureki O., Dohmae N., Takio K., Yokoyama S. Acta Crystallogr. 50:760-763(2001) Cited for: NUCLEOTIDE SEQUENCE. Strain: HB8 EMBL CAC39622.1.
[2]	"Structural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase." Shimada A., Nureki O., Goto M., Takahashi S., Yokoyama S. Proc. Natl. Acad. Sci. U.S.A. 98:13537-13542(2001) [PubMed: 11698642] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ278815 Genomic DNA. Translation: CAC39622.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IQ0	X-ray	2.30	A	1-592	[»]

ProteinModelPortal

Q93RP5.

SMR

Q93RP5. Positions 1-592.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

6.1.1.19. 245.

Family and domain databases

HAMAP

MF_00123. Arg_tRNA_synth.
[Tree]

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.

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. 2 hits.
[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.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q93RP5_THETH

Accession

Primary (citable) accession number: Q93RP5

Entry history

Integrated into UniProtKB/TrEMBL:	December 1, 2001
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)