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P74296 (SYFB_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 beta subunit
EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase beta subunit
Short name=PheRS
Gene names
Name:pheT
Ordered Locus Names:sll1553
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis ›

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP-Rule MF_00283

Cofactor

Binds 2 magnesium ions per tetramer By similarity. HAMAP-Rule MF_00283

Subunit structure

Tetramer of two alpha and two beta subunits By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00283.

Sequence similarities

Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.

Contains 1 B5 domain.

Contains 1 FDX-ACB domain.

Contains 1 tRNA-binding domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
RNA-binding
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphenylalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phenylalanine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 810810Phenylalanine--tRNA ligase beta subunit HAMAP-Rule MF_00283
PRO_0000126974

Regions

Domain39 – 150112tRNA-binding
Domain407 – 49589B5
Domain716 – 80994FDX-ACB

Sites

Metal binding4731Magnesium By similarity
Metal binding4791Magnesium; via carbonyl oxygen By similarity
Metal binding4821Magnesium By similarity
Metal binding4831Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
P74296 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 4D14168774C12BE9

FASTA81087,888
        10         20         30         40         50         60 
MRISVNWLQS LVELNLSPEE LGELLTIAGL EVEEIEDRRS WAAGVVLGRV ISREKHPNAD 

        70         80         90        100        110        120 
KLSVCVVDIG TEEPSTIVCG AANVRADILV PVATLGSYLP KVDLKIKPAK LRGVKSSGMI 

       130        140        150        160        170        180 
CSLAELGLSK ESEGIHIFPD LDLPSGSPVG PLLGLDDVIL EISPTANRAD ALSMVGVARE 

       190        200        210        220        230        240 
VAALTGGKLS LPEIKAVSVS DQDLPISVTE PQACPTYVGT VIRGVKVGPS PDWLQQRLLA 

       250        260        270        280        290        300 
AGTRPINNVV DVTNYVLLEW GQPLHSFDQD KLQTLVGPEG FALGVRFAEE GEKLITLDDQ 

       310        320        330        340        350        360 
ERTLQPQNLL VTANDQPVAI AGVMGGAATE VDENTQNIVL ETALFDGVTI RKSSKAINLR 

       370        380        390        400        410        420 
SESSTRYERG VNRCELEVAL HRAIALMTEL AGGTVVRQGK ADQRQDRGEA IINLRLERLQ 

       430        440        450        460        470        480 
QLLGKVNTPT GIGNITAEDV ERILTDLGCG LTRQSDSDTP VWAVTVPSYR QRDIEREIDL 

       490        500        510        520        530        540 
IEEVARLYGY DHFCEQLPSN TIAGGLSPSY QAELALREAC RGVGLTEVVH YSLVKPHGSE 

       550        560        570        580        590        600 
VMLANPLFAE YSALRTNLLD GLITAFANNQ AQNNGALNAF EVGRVFWQNE GDIGEADHLA 

       610        620        630        640        650        660 
GICGGSQITE GTWPQGGKPQ PMSWYDAKGL LEAIFQRLGA TVTYSGDHQD PRLHPGRTAL 

       670        680        690        700        710        720 
LSCNGTVLGR FGQLHPQLRR EKGLIDEVYA FEITLTPLYQ AMETQILGTP DFRPYSPYPA 

       730        740        750        760        770        780 
VARDLALYAP LELTVAELTQ AMVKAGGDLL EQVELFDEYR GQSVPAGQRS LAFSLAYRVG 

       790        800        810 
DRTLTDADVE PLHNQIREAL TKQFAVSLRS

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References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000022 Genomic DNA. Translation: BAA18390.1.
PIRS75931.
RefSeqNP_441710.1. NC_000911.1.
YP_005651768.1. NC_017277.1.
YP_007451592.1. NC_020286.1.

3D structure databases

ProteinModelPortalP74296.
ModBaseSearch...

Protein-protein interaction databases

IntActP74296. 4 interactions.
STRING1148.sll1553.

Proteomic databases

PaxDbP74296.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA18390; BAA18390; BAA18390.
GeneID12254423.
14617255.
952901.
KEGGsyn:sll1553.
syy:SYNGTS_1815.
syz:MYO_118330.
PATRIC23840898. VBISynSp132158_2003.

Phylogenomic databases

eggNOGCOG0072.
HOGENOMHOG000292087.
KOK01890.
OMAMKFSEQW.
OrthoDBEOG6CCH1J.
ProtClustDBPRK00629.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.30.56.20. 1 hit.
3.30.70.380. 1 hit.
3.50.40.10. 1 hit.
HAMAPMF_00283. Phe_tRNA_synth_beta1.
InterProIPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR012340. NA-bd_OB-fold.
IPR004532. Phe-tRNA-ligase_IIc_bsu_bac.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR005121. PheS_beta_Fdx_antiC-bd.
IPR002547. tRNA-bd_dom.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view]
PfamPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
PF03147. FDX-ACB. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
SMARTSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
SM00896. FDX-ACB. 1 hit.
[Graphical view]
SUPFAMSSF46955. SSF46955. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54991. SSF54991. 1 hit.
SSF56037. SSF56037. 1 hit.
TIGRFAMsTIGR00472. pheT_bact. 1 hit.
PROSITEPS51483. B5. 1 hit.
PS51447. FDX_ACB. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYFB_SYNY3
AccessionPrimary (citable) accession number: P74296
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 13, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

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