A0LWR6 (SYS_ACIC1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine--tRNA ligase
EC=6.1.1.11

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

Gene names

Name:	serS
Ordered Locus Names:	Acel_2104

Organism

Acidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]

Taxonomic identifier

351607 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Acidothermaceae › Acidothermus

Protein attributes

Sequence length	420 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
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 – 420	420	Serine--tRNA ligase HAMAP MF_00176		PRO_1000019600
Regions
	Nucleotide binding	258 – 260	3	ATP By similarity
	Nucleotide binding	345 – 348	4	ATP By similarity
	Region	227 – 229	3	Serine binding By similarity
Sites
	Binding site	274	1	ATP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	281	1	Serine By similarity
	Binding site	379	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0LWR6 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: EBF1650A834A00CE	FASTA	420	46,280
	10 20 30 40 50 60 MIDLRLLRDD PERLRASQRA RGEDPGLVDA ALAADENRRA AVARFEALRA EQKALGRRIA 70 80 90 100 110 120 SAPPDEKPAL LDRAKELAEL VKAAEAARDD ADAACREALL AISNLVDDEA PRGGEEDFVV 130 140 150 160 170 180 LEEIGTPPTF SFPPRDHLEL GERLGAIDVE RAAKVSGSRF YYLTGVGALL EFALVDLALR 190 200 210 220 230 240 QAVTAGFVPV IPPVLVRPPA MEGTGFLGQA AENVFHLEKD DFYLVGTSEV SLAAYHMGEI 250 260 270 280 290 300 LDAAQLPRRY VGFSTCFRRE AGSHGKDTRG IIRVHQFDKV EMFSFTTVGE AAAEHRRLLE 310 320 330 340 350 360 WEKQFLTALE IPFRVIDVAT GDLGASAARK FDCEAWIPTQ GRYREVTSTS NCTEFQARRL 370 380 390 400 410 420 DIRMRDEQGI RPLATLNGTL VAIPRTIVAV LENHQQADGS VVVPRALRDY LGTDVLRPKR

References

[1]

"Complete sequence of Acidothermus cellulolyticus 11B." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43068 / 11B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000481 Genomic DNA. Translation: ABK53876.1.
RefSeq	YP_873862.1. NC_008578.1.
3D structure databases
ProteinModelPortal	A0LWR6.
ModBase	Search...
Protein-protein interaction databases
STRING	A0LWR6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4484957.
GenomeReviews	Gene locus Acel_2104 in contig CP000481_GR.
KEGG	ace:Acel_2104.
PATRIC	20674858. VBIAciCel132453_2240.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HBG629391.
OMA	RLNVRYR.
PhylomeDB	A0LWR6.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	ACEL351607:ACEL_2104-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

SYS_ACIC1

Accession

Primary (citable) accession number: A0LWR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	December 12, 2006
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program