Reviewed, UniProtKB/Swiss-Prot Q97N21 (SYS2_CLOAB)

Names and origin

Protein names

Recommended name:
    Seryl-tRNA synthetase 2
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase 2
    Serine--tRNA ligase 2
      Short name=SerRS 2

Gene names

Name:	serS2
Ordered Locus Names:	CA_C0017

Organism

Clostridium acetobutylicum [Complete proteome] [HAMAP]

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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. HAMAP MF_00176
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_00176
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_00176
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity. HAMAP MF_00176
Subcellular location	Cytoplasm By similarity HAMAP MF_00176.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity. HAMAP MF_00176
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
Gene Ontology (GO)
Biological process	selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP seryl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP serine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 425	425	Seryl-tRNA synthetase 2 HAMAP MF_00176		PRO_0000122035
Regions
	Nucleotide binding	265 – 267	3	ATP By similarity
	Nucleotide binding	352 – 355	4	ATP By similarity
	Region	234 – 236	3	Serine binding By similarity
Sites
	Binding site	288	1	Serine By similarity
	Binding site	388	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97N21-1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 6B526DF08277FEA2	FASTA	425	48,653
	10 20 30 40 50 60 MLDLDLIRND TEKVKKALLK KIDNVDFTEL LKLDDERRKL IHEVEVLKNK KNEASKQISN 70 80 90 100 110 120 IKSQGGKVDE SFFKDIKEIS NKISELETSL EPIKGKMDTF LEALPNIPDE DVLPGGKENN 130 140 150 160 170 180 KVVHVYGEKP QFEFEPKDHV ELSNIHDLID YKRGTKLSGN GFWIYKGYGA ILEWALLNYF 190 200 210 220 230 240 IEEHIKDGYE FILPPHILNY ECGRTAGQFP KFKDEVFKVG SNGEGEGMQF ILPTAETALV 250 260 270 280 290 300 NLHRDEILKE DELPKKYFAY TPCYRVEAGS YRASERGMIR GHQFNKIEMF QYTKPEDSDA 310 320 330 340 350 360 ALEELIGKAE KLVKGLGLHY RLSKLAAADC SASMAKTYDI EVWIPSMNEY KEVSSASNAR 370 380 390 400 410 420 DYQARRGKIR FRREETKKIE YVNTLNASGL ATSRVLPAIL EQMQDKDGSI VVPEVLRKWV GKDKL

References

[1]

"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum." Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R. J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001437 Genomic DNA. Translation: AAK78004.1.
PIR	A96902.
RefSeq	NP_346664.1.
3D structure databases
SMR	Q97N21. Positions 1-425.
ModBase	Search...
Genome annotation databases
GeneID	1116200.
GenomeReviews	Gene locus CA_C0017 in contig AE001437_GR.
KEGG	cac:CAC0017.
NMPDR	fig|272562.1.peg.193.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG629391.
OMA	MEREMLA.
Enzyme and pathway databases
BioCyc	CACE272562:CAC0017-MONOMER.
BRENDA	6.1.1.11. 2866.
Family and domain databases
HAMAP	MF_00176. Ser_tRNA_synth_type1. [Tree]
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]
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

SYS2_CLOAB

Accession

Primary (citable) accession number: Q97N21

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	October 1, 2001
Last modified:	February 9, 2010
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)