Reviewed, UniProtKB/Swiss-Prot O74407 (SYDC_SCHPO)

Names and origin

Protein names

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

Gene names

Name:	dps1
ORF Names:	SPCC1223.07c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm. Ref.2
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
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aspartyl-tRNA aminoacylation Inferred by curator. Source: GeneDB_SPombe
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred by curator. Source: GeneDB_SPombe aspartate-tRNA ligase activity Inferred from electronic annotation. Source: EC nucleic acid binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity 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 – 580	580	Aspartyl-tRNA synthetase, cytoplasmic		PRO_0000315951
Amino acid modifications
	Modified residue	282	1	Phosphoserine Ref.3
	Modified residue	307	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O74407-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 432FCC074D558A4C	FASTA	580	66,671
	10 20 30 40 50 60 MSEMEKQVEN LSLEAKNEKP KEVILGEDGK PLSKKALKKL EKEREKEQKR KEREAREAEE 70 80 90 100 110 120 KKKREANEID YSAGKYGDLP LNRSTARPGR TYTQISDISA KNDGQTVLLR ARVYTSRLQG 130 140 150 160 170 180 NKMCFFSLRQ KYDTIQALAV VNKDTISKQM VKWCGSISLE SIVLVEGIVK KSPEIIKSAT 190 200 210 220 230 240 VQDAEIHISS IYVISPIKKN LPFLVEDAGR SEEQIRESEE NAAEGDSKFV RVNLDTRLDN 250 260 270 280 290 300 RVLDLRTPTN QAIFDIQAGI CQAFREFLLS NSFNEIHTPK MSGASSEGGS NVFKIQYFKT 310 320 330 340 350 360 DGFLSQSPQL YKQMLIAADR ERVFEIGPVF RAEDSNTYRH MTEFTGLDLE MAFNEHYHEV 370 380 390 400 410 420 MEFIEKLFLY IFKTIREKYA KQVAVVRQQY PSEDFILPDA DRIRFHFKDA VKLLKEAGYR 430 440 450 460 470 480 KQLVPGQKVP EDEEFHYCED PEFDDFSTPE ERALGQIVRE KYHTDFYVID KYPSSVRPFY 490 500 510 520 530 540 TMPDPEDPRY SNSYDFFMKG QEIMSGAQRI HDPELLVERM KALGVSPDVG LQQYIDAFAI 550 560 570 580 GCPPHAGGGI GLERVVMFYL NLPNIRLASS FPRDPKRLLP

References

[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-307, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAA20876.1.
PIR	T40867.
RefSeq	NP_588352.1.
3D structure databases
HSSP	HSSP built from PDB template 1EOV based on UniProtKB P04802.
ModBase	Search...
Protein-protein interaction databases
STRING	O74407.
Genome annotation databases
GeneID	2539278.
GenomeReviews	Gene locus dps1 in contig CU329672_GR.
KEGG	spo:SPCC1223.07c.
NMPDR	fig|4896.1.peg.690.
Organism-specific databases
GeneDB_Spombe	SPCC1223.07c.
Phylogenomic databases
OMA	RNPKQSN.
Enzyme and pathway databases
BRENDA	6.1.1.12. 653.
Gene expression databases
ArrayExpress	O74407.
Family and domain databases
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-reg. IPR002312. Asp-tRNA-synth_IIb. IPR004523. Asp-tRNA-synth_IIb_arc/euk. IPR002198. DH_sc/Rdtase_SDR. IPR012340. NA-bd_OB-fold. 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. PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYDC_SCHPO

Accession

Primary (citable) accession number: O74407

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 1, 1998
Last modified:	November 3, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)