B4RZU0 (SYS_ALTMD) 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:	MADE_1010695

Organism

Alteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]

Taxonomic identifier

314275 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Alteromonas

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_1000098030
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	390	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B4RZU0 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: 3ACA3AC3DA3E2C41	FASTA	430	47,682
	10 20 30 40 50 60 MLDPKCLRSD IEQTAKRLAA RGFNLDVAAF SSLEEKRKTL QSRTQDLQNE RNVRSKSIGK 70 80 90 100 110 120 AKAQGEDIAP LLAEVGKLGD ELDAAKAELS ELLEEINTLT QGIPNLPHES VPEGKDEDDN 130 140 150 160 170 180 VEISRWGEPR TFDFEVKDHV DVAEGLNNGL DFATASKLTG SRFVVMRGDI ARLNRALAQF 190 200 210 220 230 240 MLDTHTQEHG YQEMYVPYLV NADSLYGTGQ LPKFGEDLFH TKPATEEGQG LSLIPTAEVP 250 260 270 280 290 300 LTNIARDEIL DAKTLPVKMT AHTPCFRSEA GSYGRDTRGL IRQHQFDKVE LVQLVKPEDS 310 320 330 340 350 360 FDALEALTGH AEVILQKLEL PYRKVLLCTG DMGFGACKTY DLEVWLPAQN TYREISSCSN 370 380 390 400 410 420 MLDFQARRMQ ARFRNPETNK PELLHTLNGS GLAVGRTLVA ILENNQQADG SVTVPKALVP 430 YMAGQEVIKA

References

[1]

"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter." Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F. ISME J. 2:1194-1212(2008) [PubMed: 18670397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001103 Genomic DNA. Translation: AEA98277.1.
RefSeq	YP_004427275.1. NC_011138.2.
3D structure databases
ProteinModelPortal	B4RZU0.
SMR	B4RZU0. Positions 1-429.
ModBase	Search...
Protein-protein interaction databases
STRING	B4RZU0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	10557486.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG629391.
OMA	PKFADDM.
ProtClustDB	PRK05431.
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.
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_ALTMD

Accession

Primary (citable) accession number: B4RZU0
Secondary accession number(s): F2G3A5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	September 23, 2008
Last modified:	January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program