Q97N17 (SYS1_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine--tRNA ligase 1
EC=6.1.1.11

Alternative name(s):
Seryl-tRNA synthetase 1
Short name=SerRS 1
Seryl-tRNA(Ser/Sec) synthetase 1

Gene names

Name:	serS1
Synonyms:	serS
Ordered Locus Names:	CA_C0021

Organism

Clostridium acetobutylicum

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	424 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.
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 Reference proteome
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 – 424	424	Serine--tRNA ligase 1 HAMAP MF_00176		PRO_0000122034
Regions
	Nucleotide binding	263 – 265	3	ATP By similarity
	Nucleotide binding	350 – 353	4	ATP By similarity
	Region	232 – 234	3	Serine binding By similarity
Sites
	Binding site	286	1	Serine By similarity
	Binding site	386	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97N17 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 8F0B7E452E92BEEC	FASTA	424	48,446
	10 20 30 40 50 60 MLDLKRIRTN PEEIKKALTN RGEDFDISVI DELVSLDEER RKNLVEVENL KSKRNKDSGE 70 80 90 100 110 120 IAKLKKSGQN ADELLAEMKK ISDDIKGIDA KVSEIDEKMQ YIMLRIPNIP HPSVPEGKSD 130 140 150 160 170 180 EENVEIRKWG EPRKFDFEFK AHWDIGTDLG LLDFERGGKV AGSRFTFYKG LGARLERAVI 190 200 210 220 230 240 NYFLDTHVEK HGYTEILPPY MVNRVSMTGT GQLPKFEEDA FKVDNGFFLI PTAEVPVTNM 250 260 270 280 290 300 FRDEILKAED LPYKFAAYSA CFRSEAGSAG RDTRGLVRQH QFNKVELVKF AKPEESYDEL 310 320 330 340 350 360 EKLTHDAEEI LQILNIPYRV VRICKGDLGF TAALKYDIEV WMPSYGRYVE ISSCSNFEDF 370 380 390 400 410 420 QARRANIKFR RDPKAKPEFV HTLNGSGLAV GRTVAAILEN YQNEDGSVNV PEALKKYIGK DVIR

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.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001437 Genomic DNA. Translation: AAK78008.1.
PIR	E96902.
RefSeq	NP_346668.1. NC_003030.1.
3D structure databases
ProteinModelPortal	Q97N17.
SMR	Q97N17. Positions 1-424.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1116204.
GenomeReviews	Gene locus CA_C0021 in contig AE001437_GR.
KEGG	cac:CA_C0021.
NMPDR	fig|272562.1.peg.197.
PATRIC	32034295. VBICloAce74127_0200.
Phylogenomic databases
HOGENOM	HBG629391.
OMA	PKFADDM.
PhylomeDB	Q97N17.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	CACE272562:CAC0021-MONOMER.
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. 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

SYS1_CLOAB

Accession

Primary (citable) accession number: Q97N17

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	October 1, 2001
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program