A8ERP6 (SYS_ARCB4) 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:	Abu_0345

Organism

Arcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]

Taxonomic identifier

367737 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Arcobacter

Protein attributes

Sequence length	412 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 – 412	412	Serine--tRNA ligase HAMAP MF_00176		PRO_1000058349
Regions
	Nucleotide binding	259 – 261	3	ATP By similarity
	Nucleotide binding	346 – 349	4	ATP By similarity
	Region	228 – 230	3	Serine binding By similarity
Sites
	Binding site	282	1	Serine By similarity
	Binding site	380	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8ERP6 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: 52F80ABA044D44AF	FASTA	412	46,990
	10 20 30 40 50 60 MIDIKLLQKD FDYVVKALQK KGVDNALLNN LKDLALKTKQ KRQEMEDVTA EQNLLSKEFG 70 80 90 100 110 120 RYKKENLDIS ELQEKINALK TKKQELEDEV RTLEDDLNSI ILSVPNMPDE NVPFGVDENE 130 140 150 160 170 180 NVILEVIGEK PTFNFTPKEH WDLSCDWLDF ERGVKLAKSR FTAIKGDGAR LERALINYML 190 200 210 220 230 240 DFNRQRGFNE WYVPFMANSN TLQGTGQLPK FADDLFKIEG EDLYLIPTAE VSLTNLYNDE 250 260 270 280 290 300 IIDKSELPLL LTSYTPCFRK EAGSAGRDTR GLIRQHQFDK VEMVAITSQE QSDEIFEKMV 310 320 330 340 350 360 NCASDLLSSL GLCHQKVQLC SGDLGFSAAV TIDLEVWLPG QNKFREISSI SNTRDFQARR 370 380 390 400 410 AKIRYKEDKK NILAHTLNGS SLAVGRTLLA IMENYQQADG SVKIPEVLKK YL

References

[1]

"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri." Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E. PLoS ONE 2:E1358-E1358(2007) [PubMed: 18159241] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RM4018.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000361 Genomic DNA. Translation: ABV66620.1.
RefSeq	YP_001489289.1. NC_009850.1.
3D structure databases
ProteinModelPortal	A8ERP6.
SMR	A8ERP6. Positions 1-412.
ModBase	Search...
Protein-protein interaction databases
STRING	A8ERP6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5624527.
GenomeReviews	Gene locus Abu_0345 in contig CP000361_GR.
KEGG	abu:Abu_0345.
PATRIC	20962050. VBIArcBut20197_0338.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HBG629391.
OMA	PKFADDM.
ProtClustDB	CLSK2794731.
Enzyme and pathway databases
BioCyc	ABUT367737:ABU_0345-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_ARCB4

Accession

Primary (citable) accession number: A8ERP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program