Q9HDX9 (SYEM_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase, mitochondrial
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS

Gene names

Name:	mse1
ORF Names:	SPAPB1A10.11c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity.
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).
Subcellular location	Mitochondrion Ref.2.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamyl-tRNA aminoacylation Inferred from sequence or structural similarity. Source: PomBase mitochondrial translation Non-traceable author statement. Source: PomBase
Cellular_component	mitochondrion Inferred from direct assay Ref.2. Source: PomBase
Molecular_function	ATP binding Inferred from sequence model. Source: PomBase glutamate-tRNA ligase activity Inferred from sequence or structural similarity. Source: PomBase tRNA 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 – 38	38	Mitochondrion Potential
	Chain	39 – 526	488	Glutamate--tRNA ligase, mitochondrial		PRO_0000314764
Regions
	Nucleotide binding	278 – 282	5	ATP By similarity
	Region	37 – 39	3	Glutamate binding By similarity
	Region	222 – 226	5	Glutamate binding By similarity
	Motif	42 – 50	9	"HIGH" region
	Motif	278 – 282	5	"KMSKS" region
Sites
	Binding site	47	1	ATP By similarity
	Binding site	73	1	Glutamate By similarity
	Binding site	240	1	Glutamate By similarity
	Binding site	243	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HDX9 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: F8F34F510B43A2F4	FASTA	526	60,645
	10 20 30 40 50 60 MLSYTSCAKL ICSRYIVSKI SFYSLKRCNS TAVVRTRFAP SPTGFLHLGS LRTALFNYLW 70 80 90 100 110 120 AKKSNGKFIL RLEDTDQKRK VTGSDLEIYK VLKQFNLQWD EGPIVGGPYG PYEQSSRLQI 130 140 150 160 170 180 YQKYAQHLIE TGRAYVSYSV PIATTKIDSS TKYHEISIDD LTDAQRKLYK SKKFPYVVRF 190 200 210 220 230 240 RMKEPSPFTD LVYGKIAIKS DSREIEESNN FVILKSDGFP TYHFANVVDD HLMHITHVIR 250 260 270 280 290 300 GEEWVPSTIK HIQLYEAFGW KPPKFAHLPL LVNPDGSKLS KRQNDAHVSS LLQEGFLPEA 310 320 330 340 350 360 ILNFIALMGW SSRQKSDFLP MKELIDLFSI DKLTKSSSIV AFEKLYFLNK NYLRRAISDV 370 380 390 400 410 420 NRLDELIELV QPRLIQKFSH SSRSHDKSYT KKLLLLLKNK VHTIKEFEKI VFYFYEASDL 430 440 450 460 470 480 QQIRSLVSSL ITVEELPKIL TTILNKFETI EWNTHEIQIS LKEIAMEHQM PLKKIQSLLR 490 500 510 520 YGLCGNLPGG GISDTISLLG KETVKSRLER LLLSLKHELP KRSCIV

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAC21484.1.
RefSeq	NP_593525.1. NM_001018959.2.
3D structure databases
ProteinModelPortal	Q9HDX9.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4702716.
STRING	4896.SPAPB1A10.11c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAPB1A10.11c.1; SPAPB1A10.11c.1:pep; SPAPB1A10.11c.
GeneID	2543394.
KEGG	spo:SPAPB1A10.11c.
Organism-specific databases
PomBase	SPAPB1A10.11c.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	ISFESDG.
OrthoDB	EOG4GMZ5K.
Family and domain databases
Gene3D	1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 3.40.50.620. 2 hits.
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR004527. Glu-tRNA-ligase_Ib_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ib. IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
PANTHER	PTHR10119. PTHR10119. 1 hit. PTHR10119:SF1. PTHR10119:SF1. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMs	TIGR00464. gltX_bact. 1 hit.
ProtoNet	Search...
Other
NextBio	20804409.

Entry information

Entry name

SYEM_SCHPO

Accession

Primary (citable) accession number: Q9HDX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 1, 2001
Last modified:	May 29, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program