Q6BU46 (SYNC_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Asparagine--tRNA ligase, cytoplasmic
EC=6.1.1.22

Alternative name(s):
Asparaginyl-tRNA synthetase
Short name=AsnRS

Gene names

Name:	DED81
Ordered Locus Names:	DEHA2C13684g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn).
Subcellular location	Cytoplasm By similarity.
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	asparaginyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine-tRNA ligase activity Inferred from electronic annotation. Source: EC 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 – 552	552	Asparagine--tRNA ligase, cytoplasmic		PRO_0000176498

Sequences

	Sequence		Length	Mass (Da)
	Q6BU46 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 926B1E81A92DCFD9	FASTA	552	62,236
	10 20 30 40 50 60 MSQVYVNEKT GADSTDVSGS EQQPFQTPAF ALFKNEDAKI LVYKQLEDSE EFGYGEISAS 70 80 90 100 110 120 ALKKAKKGAE GLKKKQEKQA KLQEEQRKHQ DDAAKKFAEM DLISIKEDES LPQAKKIKLR 130 140 150 160 170 180 TVQDNIGTRV VVQGWIHRLR LQKGLGFITL RDGTGFIQCI LTGDLAKCKT THELTLESTV 190 200 210 220 230 240 TIKGVINKLP EGKSAPGGVE LKVDYYEVVG LAPSGEEAFS NKVQENADPS LLLDQRHLAL 250 260 270 280 290 300 RGESLSAVMK VRSTLLQAIR RFFAEEGLLE VTPPCMVQTQ VEGGSTLFKM DYYGEEAYLT 310 320 330 340 350 360 QSSQLYLETC LPALGDVFCV QESFRAEKSH TRRHLSEYTH IESELGFIEF DDLLTHLERL 370 380 390 400 410 420 ITYVVKYVVE DPVAGPLIKQ LNPNFVPPQM PFKRMEYIHA LDWLNEHGIP NEDGEKFKFG 430 440 450 460 470 480 DDIAEAAERK MTDTIGVPIL LIRFPVEIKS FYMQKCADDP RVTESVDVLM PTVGEITGGS 490 500 510 520 530 540 MRTYDNDELV AAIKREGLDL DSYYWFTDQR KYGTCPHGGY GLGTERILAW LCDRFTVRDC 550 SLYPRFTGRC KP

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382135 Genomic DNA. Translation: CAG86350.1.
RefSeq	XP_458273.1. XM_458273.1.
3D structure databases
ProteinModelPortal	Q6BU46.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6BU46.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2900062.
GenomeReviews	Gene locus DEHA2C13684g in contig CR382135_GR.
KEGG	dha:DEHA2C13684g.
Phylogenomic databases
eggNOG	fuNOG07411.
HOGENOM	HBG745843.
OMA	CMVQTQV.
OrthoDB	EOG47WRX6.
Family and domain databases
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR004522. Asn-tRNA-synth_IIb. IPR002312. Asp/Asn-tRNA-synth_IIb. 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.
KO	K01893.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF6. PTHR22594:SF6. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR00457. AsnS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYNC_DEBHA

Accession

Primary (citable) accession number: Q6BU46

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program