Reviewed, UniProtKB/Swiss-Prot Q9UTB2 (SYSM_SCHPO)

Names and origin

Protein names

Recommended name:
    Seryl-tRNA synthetase, mitochondrial
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
      Short name=SerRS

Gene names

Name:	dia4
ORF Names:	SPAC25B8.06c

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	454 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity. UniProtKB Q9N0F3
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). UniProtKB Q9N0F3 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). UniProtKB Q9N0F3
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. UniProtKB Q9N0F3
Subunit structure	Homodimer. The tRNA molecule probably binds across the dimer By similarity. UniProtKB Q9N0F3
Subcellular location	Mitochondrion matrix Ref.2 UniProtKB Q9N0F3.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity. UniProtKB P0A8L1
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	seryl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW serine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 454	454	Seryl-tRNA synthetase, mitochondrial		PRO_0000315879
Regions
	Nucleotide binding	292 – 294	3	ATP By similarity UniProtKB Q9N0F3
	Nucleotide binding	379 – 382	4	ATP By similarity UniProtKB Q9N0F3
	Region	262 – 264	3	Serine binding By similarity UniProtKB Q9N0F3
Sites
	Binding site	315	1	Serine By similarity UniProtKB Q9N0F3
	Binding site	413	1	Serine By similarity UniProtKB Q9N0F3

Sequences

	Sequence		Length	Mass (Da)
	Q9UTB2-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 80F2B923E6399565	FASTA	454	51,268
	10 20 30 40 50 60 MSQLLYLRTF STHTSYLRSS WQAILNYKYI YQNAEAVQRN CINRNLQAIA ETVPKIRSLI 70 80 90 100 110 120 DEKESLKNEF FPLLSLKKEI TLQIERCSDP NERGKLVNEA KGLKKKTEEY NKIISKVTND 130 140 150 160 170 180 LYQYCLAVPN TTLPTVPVGP EDKAVVVQKI GSPLVKKTGS LKDHLQIANE GINLEDAAQA 190 200 210 220 230 240 SGHSFCYTTG DIALLEMAIT NYAMDFAISK GWCPVIPPTI VRTDIALACG FQPRDEEGQQ 250 260 270 280 290 300 IYELDSYTSP LVSSPKQCLI GTAEISLAAL GFKKTFNNFT ERKVVGVSRA YRREAGARGK 310 320 330 340 350 360 ENRGLYRLHE FTKVELFAWT HPSRSSEMFN EIVNFQKEFV ETLKIPARIL NMPTAELGSS 370 380 390 400 410 420 ASQKYDIEAW MPARQSYGEI TSASNCLEYQ ARRLLTRYRN DKDSGFVHTL NGTAAAIPRL 430 440 450 IIAILENHQQ EDGTVKVPET LVPYIHKEYL FKAK

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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB61772.1.
PIR	T50193.
RefSeq	NP_594466.1.
3D structure databases
HSSP	HSSP built from PDB template 1WLE based on UniProtKB Q9N0F3.
SMR	Q9UTB2. Positions 24-449, 117-450.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UTB2.
Genome annotation databases
GeneID	2541567.
GenomeReviews	Gene locus dia4 in contig CU329670_GR.
KEGG	spo:SPAC25B8.06c.
NMPDR	fig|4896.1.peg.4436.
Organism-specific databases
GeneDB_Spombe	SPAC25B8.06c.
Phylogenomic databases
eggNOG	fuNOG06563.
HOGENOM	HBG629391.
OMA	PKFDFKP.
OrthoDB	EOG9R51JX.
PhylomeDB	Q9UTB2.
Enzyme and pathway databases
BRENDA	6.1.1.11. 653.
Gene expression databases
ArrayExpress	Q9UTB2.
Family and domain databases
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II_cons-dom. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. IPR010978. tRNA_bd_arm. [Graphical view]
PANTHER	PTHR11778. tRNA-synt_ser. 1 hit.
Pfam	PF02403. Seryl_tRNA_N. 1 hit. PF00587. tRNA-synt_2b. 1 hit. [Graphical view]
PIRSF	PIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTS	PR00981. TRNASYNTHSER.
TIGRFAMs	TIGR00414. serS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYSM_SCHPO

Accession

Primary (citable) accession number: Q9UTB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)