Reviewed, UniProtKB/Swiss-Prot Q2GK20 (SYR_ANAPZ)

Names and origin

Protein names

Recommended name:
    Arginyl-tRNA synthetase
    EC=6.1.1.19
Alternative name(s):
    Arginine--tRNA ligase
      Short name=ArgRS

Gene names

Name:	argS
Ordered Locus Names:	APH_0700

Organism

Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]

Taxonomic identifier

212042 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP MF_00123
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm. HAMAP MF_00123
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
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 – 580	580	Arginyl-tRNA synthetase HAMAP MF_00123		PRO_0000241977
Regions
	Motif	137 – 147	11	"HIGH" region HAMAP MF_00123

Sequences

	Sequence		Length	Mass (Da)
	Q2GK20-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: A5A0216ABAD6C597	FASTA	580	65,545
	10 20 30 40 50 60 MLLDDKILDI FGFFRNAIEE RIRAVWSGDN IPESLFKRII VGPPAQPKHG DLYTNAALIL 70 80 90 100 110 120 GKFDKKNPME LASTLCNAFE NIEGIESINV VAPGFINFHC VNSVWHGVVR NINKLGREYG 130 140 150 160 170 180 RTDLGHNKKV NIEFVSANPT GPLHIGHARG AVFGDVLSNL LKWVGYDVIK EYYVNDAGSQ 190 200 210 220 230 240 VKTLVSSVFL RYKEALGEEI TIGAGLYPGE YLKPIARDLV EKYGSDLLNA SDKDEIIRSF 250 260 270 280 290 300 TLSSMLNLIK EDLALLGVEH DVFVSESDLQ NRNVIEECVK YLRERGIIYE GVLEKPKRED 310 320 330 340 350 360 ELSEWQPRVQ MLFKSTEFGD DSDRALQKED GTWSYFAGDI GYHFHKISRG FDSMIMTLGF 370 380 390 400 410 420 DHKGYVSRLK AAVAALSNGK ASIDIKLYNL VNFLENGTPV KMSKRKGEFL TVRDVIDEVG 430 440 450 460 470 480 RDVARFMMLT RRNDVVLDFD FAKAREESKD SQIFYIQYAH ARIRSIVRRC PELLAIEKID 490 500 510 520 530 540 FSCVITEQEL SLLRLLSRWP SVIKTSAENY EPHTIAFYLI EVAEAFHALW GCGNSDPSMR 550 560 570 580 FIVEGDLHTT SARIYIAIAV SHVIASGLDI FSITPSEEMR

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000235 Genomic DNA. Translation: ABD43701.1.
RefSeq	YP_505281.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3930454.
GenomeReviews	Gene locus APH_0700 in contig CP000235_GR.
KEGG	aph:APH_0700.
NMPDR	fig|212042.5.peg.681.
TIGR	APH_0700.
Phylogenomic databases
HOGENOM	Q2GK20.
OMA	Q2GK20. MDFDFAK.
Enzyme and pathway databases
BioCyc	APHA212042:APH_0700-MON.
Family and domain databases
HAMAP	MF_00123. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-synth_Ic. IPR015945. Arg-tRNA-synth_Ic_core. IPR005148. Arg-tRNA-synth_Ic_N. IPR008909. DALR_anticod_bd. IPR014729. Rossmann-like_a/b/a_fold. [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. 1 hit. [Graphical view]
PRINTS	PR01038. TRNASYNTHARG.
TIGRFAMs	TIGR00456. argS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYR_ANAPZ

Accession

Primary (citable) accession number: Q2GK20

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	March 21, 2006
Last modified:	June 16, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)