Skip Header

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

Q7SYV0 (SYFAB_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenylalanine--tRNA ligase alpha chain B
EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase alpha chain B
Short name=PheRS
Gene names
Name:farsa-b
Synonyms:farsla-b
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).

Subunit structure

Tetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha chain type 2 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
Gene Ontology (GO)
   Biological processphenylalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phenylalanine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 499498Phenylalanine--tRNA ligase alpha chain B
PRO_0000280453

Sequences

Sequence LengthMass (Da)Tools
Q7SYV0 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: A632A4680B2C27C2

FASTA49956,750
        10         20         30         40         50         60 
MADNLLSEQL LQRLQDGDNK GVDTLELAAV LSVDHQQVVG AVKSLQCLGE IIEAEQRSSK 

        70         80         90        100        110        120 
KWELSSEGEE IAQVGSHEAR VFQSLPKEGL LQAELMKLPF AKVGFSKAMS NKWIRLDKAA 

       130        140        150        160        170        180 
AGGPCVYRVV ETIEDTVKEK LQLILKGRAD DVNEKDKNEL KKRKLVNEVT VKSYWVTKGS 

       190        200        210        220        230        240 
GFSTSITKQE TDLTPEMIAS GSWREKQFKG YNFNALGVMP ECGHLHPLLK VRTQFRQIFL 

       250        260        270        280        290        300 
EMGFTEMPTN NFIESSFWNF DALFQPQQHP ARDQHDTFFL QDPALATEFP MEYLERVKKV 

       310        320        330        340        350        360 
HSEGGYGSQG YKYDWSIHEA QKNILRTHTT AVSARMLYKL AHQKEFTPVK YFSIDRVFRN 

       370        380        390        400        410        420 
ETLDATHLAE FHQIEGVVAD RGLTLGNLMG VLKEFFHKLG ITKLRFKPAY NPYTEPSMEV 

       430        440        450        460        470        480 
FSYHEGLKKW VEVGNSGLFR PELLLPMGLP GDVNVLGWGL SLERPTMIRY GIKNIRELVG 

       490 
HKVNLQMVYD SPICRLDAC

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC054256 mRNA. Translation: AAH54256.1.
RefSeqNP_001080851.1. NM_001087382.1.
UniGeneXl.62819.

3D structure databases

HSSPHSSP built from PDB template 2ALY based on UniProtKB P27001.
ProteinModelPortalQ7SYV0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID380545.
KEGGxla:380545.

Organism-specific databases

CTD380545.
XenbaseXB-GENE-6253419. farsa.

Phylogenomic databases

HOVERGENHBG068046.

Family and domain databases

InterProIPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR002319. Phenylalanyl-tRNA_Synthase.
[Graphical view]
KOK01889.
PfamPF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
TIGRFAMsTIGR00468. PheS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYFAB_XENLA
AccessionPrimary (citable) accession number: Q7SYV0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents