Reviewed, UniProtKB/Swiss-Prot Q9Y9U7 (SYD_AERPE)

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:	APE_2192.1

Organism

Aeropyrum pernix [Complete proteome] [HAMAP]

Taxonomic identifier

56636 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	442 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
Cofactor	Binds 3 magnesium ions per subunit By similarity. HAMAP MF_00044
Subcellular location	Cytoplasm 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 Magnesium Metal-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 magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 442	442	Aspartyl-tRNA synthetase HAMAP MF_00044		PRO_0000110989
Sites
	Metal binding	365	1	Magnesium 2 By similarity
	Metal binding	365	1	Magnesium 3 By similarity
	Metal binding	368	1	Magnesium 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Y9U7-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 0AFAC6050871CB84	FASTA	442	50,853
	10 20 30 40 50 60 MLKDRFIADI IASKESLVGG RVRVCGWAYR IRDLGRLKFI LVRDRSGVIQ ATVKRGESPE 70 80 90 100 110 120 DALRAAEDLK LESVVCVEGE LRQAPTREGV EVKVERLEVL STPVEPLPLE VEGSEKASLP 130 140 150 160 170 180 TRLKYRWLDI RNPMVSAIFE LEAMVAKVFR DYYWSQGFVE IFTPKIVAAG TESGAEVFPV 190 200 210 220 230 240 VYFDKTAFLA QSPQFYKQFA VIAGLERVFE IGPVFRAEPH HTSRHLNEYH SLDIEVGFIE 250 260 270 280 290 300 SYNDVMNYVE GFMRAIVRML EEDGRRVLEL YGVELPRIPA SGIPKIPLRK AYEILEEKYG 310 320 330 340 350 360 KKVEYGEDLD SEGERLMGAY AGEELDSDFV FIVEYPWKVR PFYTMRKDDE PSWTYSFDLL 370 380 390 400 410 420 YRGLEIVTGG QREHRYHRLL ENLRDKGLDA ESFQFYLDFF KHGAPPHGGA GMGLERIVMQ 430 440 TLKLENIREA RMLPRDTERI TP

References

[1]

"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000002 Genomic DNA. Translation: BAA81203.2.
PIR	C72527.
RefSeq	NP_148450.2.
3D structure databases
SMR	Q9Y9U7. Positions 1-442.
ModBase	Search...
Genome annotation databases
GeneID	1445256.
GenomeReviews	Gene locus APE_2192.1 in contig BA000002_GR.
KEGG	ape:APE_2192.1.
NMPDR	fig|272557.1.peg.1558.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG745843.
OMA	ASAFPRD.
Enzyme and pathway databases
BioCyc	APER272557:APE2192-MONOMER.
BRENDA	6.1.1.12. 256344.
Family and domain databases
HAMAP	MF_00044_A. Asp_tRNA_synth_A. [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. IPR020780. Asp-tRNA-synth_IIb_arc. IPR004523. Asp-tRNA-synth_IIb_arc/euk. 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.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
TIGRFAMs	TIGR00458. aspS_arch. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYD_AERPE

Accession

Primary (citable) accession number: Q9Y9U7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	February 9, 2010
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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