O14018 (SYSC_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine--tRNA ligase, cytoplasmic
EC=6.1.1.11

Alternative name(s):
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase

Gene names

ORF Names:

SPAC29A4.15

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the attachment of serine to tRNA(Ser). Is also 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.
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.
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	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	seryl-tRNA aminoacylation Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW serine-tRNA ligase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 450	450	Serine--tRNA ligase, cytoplasmic		PRO_0000122198
Regions
	Nucleotide binding	271 – 273	3	ATP By similarity
	Nucleotide binding	358 – 361	4	ATP By similarity
	Region	238 – 240	3	Serine binding By similarity
Sites
	Binding site	287	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	294	1	Serine By similarity
	Binding site	396	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O14018 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 052DE1D4DF7EA646	FASTA	450	51,643
	10 20 30 40 50 60 MLDINLFQVE KGGNPEIIRE SQRKRGADVG VVDKVIEMYK EWVSLRFELD NTNKSINRVQ 70 80 90 100 110 120 KEIGLKMKAK EDASELLEEK NSLTERKKNL IEQETAKNKE MLNVVSSIGN IVHDSVPVSM 130 140 150 160 170 180 DEDNNEIIRK WAPEGVTVEK KNCLSHHEVL TRLDGYDPER GVKVSGHRGY FLRQYGVFFN 190 200 210 220 230 240 LALIQYGLDF LEKRGYIALQ APTMLNKDVM AKTAQLEQFD EELYKVIDGD EERYLIATSE 250 260 270 280 290 300 QPISAYHSGE WFEKPSEQLP LKYAGYSTCY RREAGSHGRD AWGIFRVHAF EKIEQFVLTD 310 320 330 340 350 360 PEKSWEAFTE MINHAEDFYK SLELPYRIVA IVSGALNNAA AKKYDLEAWF PFQGEYKELV 370 380 390 400 410 420 SCSNCTDYQS RNLEIRCGVK KMGDREKKYV HCLNSTLCAT ERALCCILEN YQTPDGVNVP 430 440 450 KVLQPYMGGK TFLPFTKELP KNSTSKKGKN

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: 972 / ATCC 24843.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB10149.1.
PIR	T38474.
RefSeq	NP_594867.1. NM_001020296.1.
3D structure databases
ProteinModelPortal	O14018.
ModBase	Search...
Protein-protein interaction databases
STRING	O14018.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC29A4.15.1; SPAC29A4.15.1:pep; SPAC29A4.15.
GeneID	2542163.
KEGG	spo:SPAC29A4.15.
NMPDR	fig|4896.1.peg.4837.
Organism-specific databases
GeneDB_Spombe	SPAC29A4.15.
Phylogenomic databases
eggNOG	fuNOG05177.
GeneTree	EFGT00050000004865.
HOGENOM	HBG629391.
OMA	MMDEMIG.
OrthoDB	EOG425922.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002936-MONOMER.
Gene expression databases
ArrayExpress	O14018.
Family and domain databases
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR002317. Ser-tRNA-synth_IIa. IPR015866. Ser-tRNA-synth_IIa_N. IPR010978. tRNA-bd_arm. [Graphical view]
Gene3D	G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
KO	K01875.
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.
SUPFAM	SSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMs	TIGR00414. SerS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYSC_SCHPO

Accession

Primary (citable) accession number: O14018

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program