F0MQP5 (F0MQP5_NEIMM) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

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

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

Gene names

Name:	argS HAMAP-Rule MF_00123 EMBL ADY97255.1
Ordered Locus Names:	NMBM01240149_0661 EMBL ADY97255.1

Organism

Neisseria meningitidis serogroup B (strain M01-240149) [Complete proteome] [HAMAP]

Taxonomic identifier

935591 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria › Neisseria meningitidis

Protein attributes

Sequence length	572 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. HAMAP-Rule MF_00123
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00123.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. RuleBase RU003489 HAMAP-Rule MF_00123

Ontologies

Keywords
Biological process	Protein biosynthesis RuleBase RU003489 HAMAP-Rule MF_00123
Cellular component	Cytoplasm HAMAP-Rule MF_00123
Ligand	ATP-binding RuleBase RU003489 HAMAP-Rule MF_00123 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase RuleBase RU003489 HAMAP-Rule MF_00123 EMBL ADY97255.1 Ligase
Technical term	Complete 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
Regions
	Motif	122 – 132	11	"HIGH" region By similarity HAMAP-Rule MF_00123

Sequences

	Sequence		Length	Mass (Da)
	F0MQP5 [UniParc]. Last modified May 3, 2011. Version 1. Checksum: 47951856B0F6FB5D	FASTA	572	62,644
	10 20 30 40 50 60 MNLHQTVERE AAAAFAAAGI AGSPVVLQPT KNAEHGDFQI NGVMGAAKKA KQNPRELAQK 70 80 90 100 110 120 VADALAGNAV IESAEVAGPG FINLRLRPEF LAQNIHAALN DARFGIAQTD KPQTVVIDYS 130 140 150 160 170 180 SPNLAKEMHV GHLRSSIIGD SISRVSEFMG NTVIRQNHVG DWGTQFGMLV AYLVEQQKDN 190 200 210 220 230 240 AAFELADLEQ FYRAAKVRFD EDPAFADTAR EYVVKLQGGD ETVLALWKQF VDISLSHAQA 250 260 270 280 290 300 VYDTLGLKLR PEDVAGESKY NDDLQPVVDD LVQKGLAVED DGAKVVFLDE FKNKEGEPAA 310 320 330 340 350 360 FIVQKQGGGF LYASTDLACL RYRVGTLHAD RLLYVVDHRQ ALHFEQLFTT SRKAGYLPEN 370 380 390 400 410 420 VGAAFVGFGT MMGKDGKPFK TRSGDTVKLV DLLTEAVERA TALVKEKNPE LGTDEAGKIG 430 440 450 460 470 480 KTVGIGAVKY ADLSKNRTSD YVFDWDAMLS FEGNTAPYLQ YAYTRVQSVF RKAGEWDANA 490 500 510 520 530 540 PTVLTEPLEK QLAAELLKFE DVLQSVADTA YPHYLAAYLY QIATLFSRFY EACPILKAEG 550 560 570 ASRNSRLQLA KLTGDTLKQG LDLLGIDVLD VM

References

[1]

"Neisseria meningitidis is structured in clades associated with restriction modification systems that modulate homologous recombination." Budroni S., Siena E., Dunning Hotopp J., Seib K.L., Serruto D., Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S., Covacci A., Pizza M., Rappuoli R., Moxon E., Tettelin H., Medini D. Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: M01-240149 EMBL ADY97255.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002421 Genomic DNA. Translation: ADY97255.1.
RefSeq	YP_005895466.1. NC_017514.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADY97255; ADY97255; NMBM01240149_0661.
GeneID	12412341.
KEGG	nmm:NMBM01240149_0661.
PATRIC	47156202. VBINeiMen175098_0912.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K01887.
OMA	QGAKCVF.
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

F0MQP5_NEIMM

Accession

Primary (citable) accession number: F0MQP5

Entry history

Integrated into UniProtKB/TrEMBL:	May 3, 2011
Last sequence update:	May 3, 2011
Last modified:	April 3, 2013
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)