A5FX43 (SYS_ACICJ) 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:	Acry_0957

Organism

Acidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]

Taxonomic identifier

349163 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acidiphilium

Protein attributes

Sequence length	433 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 – 433	433	Serine--tRNA ligase HAMAP MF_00176		PRO_1000019601
Regions
	Nucleotide binding	267 – 269	3	ATP By similarity
	Nucleotide binding	354 – 357	4	ATP By similarity
	Region	236 – 238	3	Serine binding By similarity
Sites
	Binding site	290	1	Serine By similarity
	Binding site	394	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5FX43 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 1C3687EA39D9EF3C	FASTA	433	47,129
	10 20 30 40 50 60 MHDLKAIRDD AAAFGAAMRR RGLAGPEGAD EGAAAPIRAL DEERRRAQTE LQGHETRRNE 70 80 90 100 110 120 LARAIGQAKR AGEDTTALEA EGTALRQSIE TANAWLAESA RKLDELLAVL PNVLDADVPD 130 140 150 160 170 180 GPDETANVEQ KRVGAPPSFD FEARQHFELG EALGLMDFAG AAKLAGARFT VLRGDLARLE 190 200 210 220 230 240 RALGQFMLDL HVNEHGYTEV SPPLLVNDAT MYGTGQLPKF AEDLFRTTDG RWLIPTAEVP 250 260 270 280 290 300 LTNLAAGEIL DAASLPLRMT ALTPSFRSEA GSAGRDTRGM LRQHQFWKVE LVSLTTPEAS 310 320 330 340 350 360 ADEHERMTSC AESVLERLGL PYRRMLLCAG DTGFSSAKTY DLEVWLPGQG AYREISSCSN 370 380 390 400 410 420 CRAFQARRMN ARYRPPQTGP KPAKPDFVHT LNGSGVATGR ALIAVMENYQ NADGSITVPD 430 ALRPYMRGCD RIG

References

[1]

"Complete sequence of chromosome of Acidiphilium cryptum JF-5." US DOE Joint Genome Institute 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., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JF-5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000697 Genomic DNA. Translation: ABQ30175.1.
RefSeq	YP_001234094.1. NC_009484.1.
3D structure databases
ProteinModelPortal	A5FX43.
ModBase	Search...
Protein-protein interaction databases
STRING	A5FX43.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5161950.
GenomeReviews	Gene locus Acry_0957 in contig CP000697_GR.
KEGG	acr:Acry_0957.
PATRIC	20646908. VBIAciCry6074_1448.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HBG629391.
OMA	HANEILK.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	ACRY349163:ACRY_0957-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_ACICJ

Accession

Primary (citable) accession number: A5FX43

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 12, 2007
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program