Q55FI3 (SYNM_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable asparagine--tRNA ligase, mitochondrial
EC=6.1.1.22

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

Gene names

Name:	asnS2
ORF Names:	DDB_G0268100

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn).
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	asparaginyl-tRNA aminoacylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine-tRNA ligase activity Inferred from sequence or structural similarity. Source: UniProtKB 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
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 460		Probable asparagine--tRNA ligase, mitochondrial		PRO_0000327476

Sequences

	Sequence		Length	Mass (Da)
	Q55FI3 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: D58FDB7FC4200947	FASTA	460	53,166
	10 20 30 40 50 60 MNNIIKRFYK WPIRINEINK NNKDLIGKEI KVKGWVRNIR NQKSVSFIEL GDGSSIKGLQ 70 80 90 100 110 120 IVGDKDSFSK LKYGSSIEVN GKLINSLGND KEAIEVQLTE PYKLIGNCPD CYPLQPKNHS 130 140 150 160 170 180 FEFLRDIAHI RSRGNSIGAL LRVRNKSTQL IHQYFNDNGF INVHTPIITA SDCEGGGEQF 190 200 210 220 230 240 QIKSSLDTKE SMFFGQPSFL TVSGQLEAEI YACSHSRVYT FGPTFRAEKS NTPRHLSEFW 250 260 270 280 290 300 MIEPEMAFID LNDNLDIAED FCKYLIRNLL DSCKEDIEFF NKRIDTNLLS RLEKTLSTPF 310 320 330 340 350 360 IRLEYKDAIQ LLQNNNHPIK WGDDIQREQE KFITTHFGEI PVFVINWPKS IKPFYMRENE 370 380 390 400 410 420 QTDHSNIMPT VSNMDLLVPT VGELIGGSIR EERYDKLLNT INEMGMDKDQ YSWYLDLRKY 430 440 450 460 GTVPHGGFGL GFERFLQFVT GLQNIKDVIP IPRHQNYCKF

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000003 Genomic DNA. Translation: EAL73503.1.
RefSeq	XP_647550.1. XM_642458.1.
3D structure databases
HSSP	HSSP built from PDB template 1X56 based on UniProtKB O57980.
ProteinModelPortal	Q55FI3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55FI3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0231334; DDB0231334; DDB_G0268100.
GeneID	8616358.
GenomeReviews	Gene locus asnS2 in contig CM000150_GR.
KEGG	ddi:DDB_G0268100.
Organism-specific databases
dictyBase	DDB_G0268100. asnS2.
Phylogenomic databases
eggNOG	KOG0554.
GeneTree	EPrGT00050000000242.
HOGENOM	HBG745843.
OMA	AIHRFFH.
PhylomeDB	Q55FI3.
ProtClustDB	CLSZ2729369.
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

SYNM_DICDI

Accession

Primary (citable) accession number: Q55FI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)