A1K581 (SYS_AZOSB) 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:	azo1369

Organism

Azoarcus sp. (strain BH72) [Complete proteome] [HAMAP]

Taxonomic identifier

62928 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Azoarcus

Protein attributes

Sequence length	430 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 – 430	430	Serine--tRNA ligase HAMAP MF_00176		PRO_1000019614
Regions
	Nucleotide binding	266 – 268	3	ATP By similarity
	Nucleotide binding	353 – 356	4	ATP By similarity
	Region	235 – 237	3	Serine binding By similarity
Sites
	Binding site	289	1	Serine By similarity
	Binding site	388	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1K581 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: B956A486F2D0EBD2	FASTA	430	47,189
	10 20 30 40 50 60 MLDIQLLRGQ LSQVAERLAL RGVTLDSGAF TALEDERKQL QTRTQELQAK RNALSKQIGI 70 80 90 100 110 120 LKGKGEDASA VMAEVGQLGD ELKACEQALP VVLEKLNAFL AGLPNLPQEG VPVGEDETGN 130 140 150 160 170 180 VEVRRWGTPR SFDFEVKDHV DLGAALGLDF DTGAKLSGSR FTFMRGQIAR LHRALAQFML 190 200 210 220 230 240 DTQTLEHGYT ECYAPYIVNR EVLVGTGQLP KFKEDMFWVL RGGDEEGGEQ YLISTSEIPL 250 260 270 280 290 300 TNTVREQILA ADALPIKLTA HSPCFRSEAG SAGRDTRGMI RQHQFDKVEM VQIVHPDASN 310 320 330 340 350 360 AALEEMVGHA EAILQKLELP YRVITLCTGD MGFSAAKTYD LEVWLPAQNT YREISSCSNC 370 380 390 400 410 420 EAFQARRMQA RFKTAQGKNE LVHTLNGSGL AVGRTLVAVL ENYQQADGSI VVPKALVPYM 430 GGLEVLRPAS

References

[1]

"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72." Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. , Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A. Nat. Biotechnol. 24:1385-1391(2006) [PubMed: 17057704] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BH72.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM406670 Genomic DNA. Translation: CAL93986.1.
RefSeq	YP_932873.1. NC_008702.1.
3D structure databases
ProteinModelPortal	A1K581.
SMR	A1K581. Positions 1-429.
ModBase	Search...
Protein-protein interaction databases
STRING	A1K581.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4606835.
GenomeReviews	Gene locus azo1369 in contig AM406670_GR.
KEGG	azo:azo1369.
PATRIC	21011096. VBIAzoSp26047_1394.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HBG629391.
OMA	ERSIINY.
PhylomeDB	A1K581.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	ASP62928:AZO1369-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_AZOSB

Accession

Primary (citable) accession number: A1K581

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program