Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot B2UPP6 (SYS_AKKM8)

Last modified November 3, 2009. Version 9. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Seryl-tRNA synthetase
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
      Short name=SerRS
Gene names
Name: serS
Ordered Locus Names: Amuc_2115
OrganismAkkermansia muciniphila (strain ATCC BAA-835) [Complete proteome] [HAMAP]
Taxonomic identifier349741 [NCBI]
Taxonomic lineageBacteriaVerrucomicrobiaVerrucomicrobiaeVerrucomicrobialesVerrucomicrobiaceaeAkkermansia

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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.

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.

Domain

Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processselenocysteine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

seryl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

serine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Seryl-tRNA synthetase HAMAP MF_00176
PRO_1000098028

Regions

Nucleotide binding262 – 2643ATP By similarity
Nucleotide binding349 – 3524ATP By similarity
Region231 – 2333Serine binding By similarity

Sites

Binding site2781ATP; via carbonyl oxygen and amide nitrogen By similarity
Binding site2851Serine By similarity
Binding site3841Serine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2UPP6-1 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 9F53BB6E59D5E567

FASTA42647,900
        10         20         30         40         50         60 
MLDIRVIREN PEEVKARLKP RSGDAWKLVD DVLACDEARR NAETEKQALQ SERNATSKQI 

        70         80         90        100        110        120 
GMLKKKGEDT SSIEARVREI GDRIRELDRV AEENAAQLTS LLMNIPNLPH LECPVGADET 

       130        140        150        160        170        180 
ANPEIKLWGE KPAIENPKDH VELAANLGMI SFEDGARITG SGFVVYRGAG ARLERALINF 

       190        200        210        220        230        240 
LLNTQTVENG YQEVGVPFVV KRECMEGTGQ LPKFEEDMYG TEDQQMFLIP TAEVPVTNLY 

       250        260        270        280        290        300 
RDTILQESDL PIKMAAYTPC FRREAGSAGR INRGMIRVHQ FDKVELVQIL KPEDSFRELE 

       310        320        330        340        350        360 
VLRSHAESIL QKLGLHYRVI ELCTGDLGFS SAKTYDIEVW APGQGQYLEV SSCSCFTDYQ 

       370        380        390        400        410        420 
ARRMRLRYKD ADGKNQFCHT LNGSGTALPR LYVALLETYQ QPDGSIRIPE ALVPYFGADC 


IRPEQA 

« Hide

References

[1]"Complete sequence of Akkermansia muciniphila ATCC BAA-835."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N. expand/collapse author list , Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., de Vos W.M., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001071 Genomic DNA. Translation: ACD05924.1.
RefSeqYP_001878705.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6275481.
GenomeReviewsGene locus Amuc_2115 in contig CP001071_GR.
KEGGamu:Amuc_2115.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMALKPYMGG.

Family and domain databases

HAMAPMF_00176.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR002317. Ser-tRNA-synth_IIa.
IPR018156. Ser-tRNA-synth_IIa_C.
IPR015866. Ser-tRNA-synth_IIa_N.
[Graphical view]
Gene3DG3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
PANTHERPTHR11778. tRNA-synt_ser. 1 hit.
PfamPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSPR00981. TRNASYNTHSER.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYS_AKKM8
AccessionPrimary (citable) accession number: B2UPP6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: November 3, 2009
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents