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P27002

- SYFB_THETH

UniProt

P27002 - SYFB_THETH

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Protein

Phenylalanine--tRNA ligase beta subunit

Gene

pheT

Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 2 magnesium ions per tetramer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi452 – 4521Magnesium
Metal bindingi458 – 4581Magnesium; via carbonyl oxygen
Metal bindingi461 – 4611Magnesium
Metal bindingi462 – 4621Magnesium

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. magnesium ion binding Source: UniProtKB-HAMAP
  3. phenylalanine-tRNA ligase activity Source: UniProtKB-HAMAP
  4. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. phenylalanyl-tRNA aminoacylation Source: UniProtKB-HAMAP
  2. tRNA processing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine--tRNA ligase beta subunit (EC:6.1.1.20)
Alternative name(s):
Phenylalanyl-tRNA synthetase beta subunit
Short name:
PheRS
Gene namesi
Name:pheT
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 785785Phenylalanine--tRNA ligase beta subunitPRO_0000126978Add
BLAST

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.

Protein-protein interaction databases

DIPiDIP-6105N.
MINTiMINT-88295.
STRINGi262724.TTC1595.

Structurei

Secondary structure

1
785
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Helixi5 – 84Combined sources
Turni9 – 113Combined sources
Helixi18 – 2811Combined sources
Beta strandi34 – 374Combined sources
Beta strandi45 – 5511Combined sources
Turni57 – 604Combined sources
Beta strandi62 – 7615Combined sources
Beta strandi86 – 905Combined sources
Turni97 – 993Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi105 – 1084Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi115 – 1173Combined sources
Helixi120 – 1234Combined sources
Beta strandi125 – 1273Combined sources
Helixi146 – 1483Combined sources
Beta strandi154 – 1574Combined sources
Helixi165 – 1684Combined sources
Helixi170 – 17910Combined sources
Beta strandi199 – 2057Combined sources
Turni207 – 2093Combined sources
Beta strandi211 – 22010Combined sources
Helixi228 – 2369Combined sources
Helixi244 – 25512Combined sources
Beta strandi261 – 2644Combined sources
Helixi265 – 2673Combined sources
Beta strandi271 – 2766Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi298 – 3047Combined sources
Beta strandi307 – 3137Combined sources
Turni314 – 3163Combined sources
Beta strandi317 – 3193Combined sources
Turni320 – 3223Combined sources
Beta strandi330 – 3378Combined sources
Helixi340 – 34910Combined sources
Helixi355 – 3628Combined sources
Helixi369 – 38315Combined sources
Beta strandi387 – 3904Combined sources
Beta strandi393 – 3953Combined sources
Beta strandi404 – 4063Combined sources
Helixi408 – 4158Combined sources
Helixi421 – 43010Combined sources
Beta strandi434 – 44512Combined sources
Helixi456 – 46712Combined sources
Helixi469 – 4713Combined sources
Helixi483 – 4853Combined sources
Turni486 – 4894Combined sources
Helixi490 – 50516Combined sources
Beta strandi514 – 5163Combined sources
Helixi520 – 5234Combined sources
Beta strandi532 – 5354Combined sources
Beta strandi541 – 5444Combined sources
Helixi549 – 56214Combined sources
Beta strandi568 – 59225Combined sources
Beta strandi597 – 6004Combined sources
Helixi606 – 62015Combined sources
Beta strandi625 – 6273Combined sources
Beta strandi634 – 64411Combined sources
Beta strandi647 – 6559Combined sources
Helixi657 – 6626Combined sources
Beta strandi669 – 6768Combined sources
Beta strandi693 – 6975Combined sources
Beta strandi701 – 7055Combined sources
Helixi707 – 71812Combined sources
Beta strandi722 – 7298Combined sources
Beta strandi733 – 7364Combined sources
Helixi737 – 7393Combined sources
Beta strandi744 – 7496Combined sources
Beta strandi752 – 7543Combined sources
Helixi758 – 77316Combined sources
Turni774 – 7763Combined sources
Beta strandi782 – 7843Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B70X-ray2.70B1-785[»]
1B7YX-ray2.50B1-785[»]
2AKWX-ray2.80B1-785[»]
2ALYX-ray2.60B1-785[»]
2AMCX-ray2.70B1-785[»]
2IY5X-ray3.10B1-785[»]
3TEHX-ray2.85B1-785[»]
ProteinModelPortaliP27002.
SMRiP27002. Positions 1-785.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27002.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 147109tRNA-bindingAdd
BLAST
Domaini399 – 47476B5Add
BLAST
Domaini688 – 78093FDX-ACBAdd
BLAST

Sequence similaritiesi

Contains 1 B5 domain.Curated
Contains 1 FDX-ACB domain.Curated
Contains 1 tRNA-binding domain.Curated

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.56.20. 1 hit.
3.30.70.380. 1 hit.
3.50.40.10. 1 hit.
HAMAPiMF_00283. Phe_tRNA_synth_beta1.
InterProiIPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR012340. NA-bd_OB-fold.
IPR004532. Phe-tRNA-ligase_IIc_bsu.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR005121. PheS_beta_Fdx_antiC-bd.
IPR002547. tRNA-bd_dom.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view]
PfamiPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
PF03147. FDX-ACB. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
SMARTiSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
SM00896. FDX-ACB. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 3 hits.
SSF50249. SSF50249. 1 hit.
SSF54991. SSF54991. 1 hit.
SSF56037. SSF56037. 1 hit.
TIGRFAMsiTIGR00472. pheT_bact. 1 hit.
PROSITEiPS51483. B5. 1 hit.
PS51447. FDX_ACB. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27002-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRVPFSWLKA YVPELESPEV LEERLAGLGF ETDRIERVFP IPRGVVFARV
60 70 80 90 100
LEAHPIPGTR LKRLVLDAGR TVEVVSGAEN ARKGIGVALA LPGTELPGLG
110 120 130 140 150
QKVGERVIQG VRSFGMALSP RELGVGEYGG GLLEFPEDAL PPGTPLSEAW
160 170 180 190 200
PEEVVLDLEV TPNRPDALGL LGLARDLHAL GYALVEPEAA LKAEALPLPF
210 220 230 240 250
ALKVEDPEGA PHFTLGYAFG LRVAPSPLWM QRALFAAGMR PINNVVDVTN
260 270 280 290 300
YVMLERAQPM HAFDLRFVGE GIAVRRAREG ERLKTLDGVE RTLHPEDLVI
310 320 330 340 350
AGWRGEESFP LGLAGVMGGA ESEVREDTEA IALEVACFDP VSIRKTARRH
360 370 380 390 400
GLRTEASHRF ERGVDPLGQV PAQRRALSLL QALAGARVAE ALLEAGSPKP
410 420 430 440 450
PEAIPFRPEY ANRLLGTSYP EAEQIAILKR LGCRVEGEGP TYRVTPPSHR
460 470 480 490 500
LDLRLEEDLV EEVARIQGYE TIPLALPAFF PAPDNRGVEA PYRKEQRLRE
510 520 530 540 550
VLSGLGFQEV YTYSFMDPED ARRFRLDPPR LLLLNPLAPE KAALRTHLFP
560 570 580 590 600
GLVRVLKENL DLDRPERALL FEVGRVFRER EETHLAGLLF GEGVGLPWAK
610 620 630 640 650
ERLSGYFLLK GYLEALFARL GLAFRVEAQA FPFLHPGVSG RVLVEGEEVG
660 670 680 690 700
FLGALHPEIA QELELPPVHL FELRLPLPDK PLAFQDPSRH PAAFRDLAVV
710 720 730 740 750
VPAPTPYGEV EALVREAAGP YLESLALFDL YQGPPLPEGH KSLAFHLRFR
760 770 780
HPKRTLRDEE VEEAVSRVAE ALRARGFGLR GLDTP
Length:785
Mass (Da):86,611
Last modified:December 1, 1992 - v2
Checksum:iBDC51952DE8E0F00
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B70 X-ray 2.70 B 1-785 [» ]
1B7Y X-ray 2.50 B 1-785 [» ]
2AKW X-ray 2.80 B 1-785 [» ]
2ALY X-ray 2.60 B 1-785 [» ]
2AMC X-ray 2.70 B 1-785 [» ]
2IY5 X-ray 3.10 B 1-785 [» ]
3TEH X-ray 2.85 B 1-785 [» ]
ProteinModelPortali P27002.
SMRi P27002. Positions 1-785.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6105N.
MINTi MINT-88295.
STRINGi 262724.TTC1595.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P27002.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
3.30.56.20. 1 hit.
3.30.70.380. 1 hit.
3.50.40.10. 1 hit.
HAMAPi MF_00283. Phe_tRNA_synth_beta1.
InterProi IPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR012340. NA-bd_OB-fold.
IPR004532. Phe-tRNA-ligase_IIc_bsu.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR005121. PheS_beta_Fdx_antiC-bd.
IPR002547. tRNA-bd_dom.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view ]
Pfami PF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
PF03147. FDX-ACB. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view ]
SMARTi SM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
SM00896. FDX-ACB. 1 hit.
[Graphical view ]
SUPFAMi SSF46955. SSF46955. 3 hits.
SSF50249. SSF50249. 1 hit.
SSF54991. SSF54991. 1 hit.
SSF56037. SSF56037. 1 hit.
TIGRFAMsi TIGR00472. pheT_bact. 1 hit.
PROSITEi PS51483. B5. 1 hit.
PS51447. FDX_ACB. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue."
    Reshetnikova L., Moor N., Lavrik O., Vassylyev D.G.
    J. Mol. Biol. 287:555-568(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiSYFB_THETH
AccessioniPrimary (citable) accession number: P27002
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 1, 1992
Last modified: November 26, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The sequence shown here has been extracted from PDB entry 1B70.Curated

Keywords - Technical termi

3D-structure

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3