Reviewed, UniProtKB/Swiss-Prot Q0A582 (SYD_ALHEH)

Names and origin

Protein names

Recommended name:
    Aspartyl-tRNA synthetase
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS

Gene names

Name:	aspS
Ordered Locus Names:	Mlg_2665

Organism

Alkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]

Taxonomic identifier

187272 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044
Subunit structure	Homodimer By similarity. HAMAP MF_00044
Subcellular location	Cytoplasm By similarity HAMAP MF_00044.
Sequence similarities	Belongs to the class-II 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	aspartyl-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 aspartate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 592	592	Aspartyl-tRNA synthetase HAMAP MF_00044		PRO_1000006631

Sequences

	Sequence		Length	Mass (Da)
	Q0A582-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: A0D5FB4D7D5337E6	FASTA	592	66,792
	10 20 30 40 50 60 MRTHYCGHVS ETDLDQEVTL CGWAHRRRDH GGVIFIDLRD REGLVQVVFD PDRPETFALA 70 80 90 100 110 120 ERVRSEFVLK VRGRVRRRPA GTENPDLPTG QVEVLGLELD LLNPAKTPPF QLDEHEQAGE 130 140 150 160 170 180 DVRLRYRYVD LRRPEMLQRL RARARITSNL RRFLDEHGFL DIETPMLTRA TPEGARDYLV 190 200 210 220 230 240 PSRTHPGSFF ALPQSPQLFK QLLMMAGMDR YYQIVRCFRD EDLRADRQPE FTQLDIETSF 250 260 270 280 290 300 MDEEGIMHLT ERMMRRLFAD VLQVDLPDPF PRMGYAEAMA RFGSDKPDLR IPLELVEVAD 310 320 330 340 350 360 LMGGVEFKVF AGPAADPRGR VAALHVPGGA GLTRKQIDDY TQFVGRYGAK GLAYIKVNDP 370 380 390 400 410 420 AQGREGLQSP ILKFLTDEAV DGILRRTEAR AGDLIFFGAD KAKVVNDALG ALRVKLGHDL 430 440 450 460 470 480 AMVEDEWRPL WVVDFPMFEY DEKDGRLYAL HHPFTAPNVD DPAELADKDP EQLVSRAYDM 490 500 510 520 530 540 VLNGTELGGG SVRIHRQDMQ QAVFRLLGID EDEARAKFGF LLDALEYGAP PHGGIAFGLD 550 560 570 580 590 RLVMLMTGAS SIREVMAFPK TQTAACLLTD APAEVDIAQL QELALRITKP QA

References

[1]

"Complete sequence of Alkalilimnicola ehrilichei MLHE-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000453 Genomic DNA. Translation: ABI58005.1.
RefSeq	YP_743495.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0A582.
Genome annotation databases
GeneID	4268798.
GenomeReviews	Gene locus Mlg_2665 in contig CP000453_GR.
KEGG	aeh:Mlg_2665.
NMPDR	fig|187272.6.peg.2542.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0173.
HOGENOM	HBG396032.
OMA	PLFEYDE.
PhylomeDB	Q0A582.
Family and domain databases
HAMAP	MF_00044_B. Asp_tRNA_synth_B. [Tree]
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-dom. IPR002312. Asp-tRNA-synth_IIb. IPR020564. Asp-tRNA-synth_IIb_bac-type. IPR004524. Asp-tRNA-synth_IIb_bac/mt. IPR018153. Asp-tRNA-synth_IIb_C_bac/mt. IPR004115. GAD_dom. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA_bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF5. AspS_bac. 1 hit.
Pfam	PF02938. GAD. 1 hit. PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
TIGRFAMs	TIGR00459. aspS_bact. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYD_ALHEH

Accession

Primary (citable) accession number: Q0A582

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 17, 2006
Last modified:	February 9, 2010
This is version 33 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)