Reviewed, UniProtKB/Swiss-Prot Q9HGT6 (SYSC_CANAL)

Names and origin

Protein names

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

Gene names

Name:	SES1
ORF Names:	CaO19.7901

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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). Ref.1
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.
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
Gene Ontology (GO)
Biological process	seryl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm 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 – 462	462	Seryl-tRNA synthetase, cytoplasmic		PRO_0000122197
Regions
	Nucleotide binding	279 – 281	3	ATP By similarity
	Nucleotide binding	366 – 369	4	ATP By similarity
	Region	246 – 248	3	Serine binding By similarity
Sites
	Binding site	295	1	ATP; via carbonyl oxygen and amide nitrogen By similarity
	Binding site	302	1	Serine By similarity
	Binding site	404	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HGT6-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 9111C72CF7B37CDF	FASTA	462	52,991
	10 20 30 40 50 60 MLDINAFLVE KGGDPEIIKA SQKKRGDSVE LVDEIIAEYK EWVKLRFDLD EHNKKLNSVQ 70 80 90 100 110 120 KEIGKRFKAK EDAKDLIAEK EKLSNEKKEI IEKEAEADKN LRSKINQVGN IVHESVVDSQ 130 140 150 160 170 180 DEENNELVRT WTPENYKKPE QIAAATGAPA KLSHHEVLLR LDGYDPERGV RIVGHRGYFL 190 200 210 220 230 240 RNYGVFLNQA LINYGLSFLS SKGYVPLQAP VMMNKEVMAK TAQLSQFDEE LYKVIDGEDE 250 260 270 280 290 300 KYLIATSEQP ISAYHAGEWF ESPAEQLPVR YAGYSSCFRR EAGSHGKDAW GIFRVHAFEK 310 320 330 340 350 360 IEQFVLTEPE KSWEEFDRMI GCSEEFYQSL GLPYRVVGIV SGELNNAAAK KYDLEAWFPF 370 380 390 400 410 420 QQEYKELVSC SNCTDYQSRN LEIRCGIKQQ NQQEKKYVHC LNSTLSATER TICCILENYQ 430 440 450 460 KEDGLVIPEV LRKYIPGEPE FIPYIKELPK NTTSVKKAKG KN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Seryl-tRNA synthetase is not responsible for the evolution of CUG codon reassignment in Candida albicans." O'Sullivan J.M., Mihr M.J., Santos M.A.S., Tuite M.F. Yeast 18:313-322(2001) [PubMed: 11223940] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ATCC 32032 / CBS 5736 / DSM 3454 / IFO 1856.
[2]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF290915 Genomic DNA. Translation: AAG02209.1. AACQ01000026 Genomic DNA. Translation: EAL01244.1.
RefSeq	XP_720099.1.
3D structure databases
HSSP	HSSP built from PDB template 1SER based on UniProtKB P34945.
ModBase	Search...
Genome annotation databases
GeneID	3638226.
KEGG	cal:CaO19.7901.
Organism-specific databases
CGD	CAL0062570. SES1.
Phylogenomic databases
OMA	MCATTRV.
Enzyme and pathway databases
BRENDA	6.1.1.11. 1124.
Family and domain databases
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. [Graphical view]
Gene3D	G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
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

SYSC_CANAL

Accession

Primary (citable) accession number: Q9HGT6
Secondary accession number(s): Q5AEY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	March 1, 2001
Last modified:	November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)