A9NE72 (SYS_ACHLI) 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:	ACL_0009

Organism

Acholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]

Taxonomic identifier

441768 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Protein attributes

Sequence length	423 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 – 423	423	Serine--tRNA ligase HAMAP MF_00176		PRO_1000077184
Regions
	Nucleotide binding	262 – 264	3	ATP By similarity
	Nucleotide binding	349 – 352	4	ATP By similarity
	Region	231 – 233	3	Serine binding By similarity
Sites
	Binding site	285	1	Serine By similarity
	Binding site	385	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9NE72 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: EA1814CFC34520F2	FASTA	423	48,263
	10 20 30 40 50 60 MLDLKYITEN IDEVILKLNT RGGDFSHLRQ LIDLQEERKS VIKEVEDLKA KRNEYSKEIG 70 80 90 100 110 120 ELKRQKQDAS HVLLKVESIK SDIPALELKL GEIDEKINKE LIVLPNIPAD DVPVGKDESA 130 140 150 160 170 180 NIEIKKWGTI RHFDFEVKDH TQLGEALNIL DFERATKITG PRFVVDKGLG ARLERALINF 190 200 210 220 230 240 MIDTHAYTHG YTEIIPPFIV NDKSMYATGQ FPKFKEDAFK LEGFDWYLNP TAEVPTINLF 250 260 270 280 290 300 RDEIIDNDAL PIQYVAYTTA FRSEAGSAGR DTKGILRQHQ FNKVELIKFA RPEDSEQAHQ 310 320 330 340 350 360 DMLANSERIL QLLNIPYRVV VLSTGDMGFG MSKTYDIEVW LPGQNMYREI GSISNARDFQ 370 380 390 400 410 420 ARRANIRFKR SKDAKTEYVH TLNGSGLAVG RTMIAVLENY QNQDGSITIP EVLKPYMGVE VIK

References

[1]

"Complete genome and proteome of Acholeplasma laidlawii." Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A., Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I. , Alexeev D.G., Ladygina V.G., Govorun V.M. J. Bacteriol. 193:4943-4953(2011) [PubMed: 21784942] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PG-8A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000896 Genomic DNA. Translation: ABX80652.1.
RefSeq	YP_001620028.1. NC_010163.1.
3D structure databases
ProteinModelPortal	A9NE72.
SMR	A9NE72. Positions 1-423.
ModBase	Search...
Protein-protein interaction databases
STRING	A9NE72.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5803497.
GenomeReviews	Gene locus ACL_0009 in contig CP000896_GR.
KEGG	acl:ACL_0009.
PATRIC	20636736. VBIAchLai134690_0010.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG629391.
OMA	HANEILK.
Enzyme and pathway databases
BioCyc	ALAI441768:ACL_0009-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_ACHLI

Accession

Primary (citable) accession number: A9NE72

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program