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Protein

tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase

Gene

taw2

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent transferase that acts as a component of the wyosine derivatives biosynthesis pathway. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to 4-demethylwyosine (imG-14), forming 7-aminocarboxypropyl-demethylwyosine (wybutosine-86) at position 37 of tRNA(Phe).UniRule annotation1 Publication

Catalytic activityi

S-adenosyl-L-methionine + 4-demethylwyosine(37) in tRNA(Phe) = S-methyl-5'-thioadenosine + 7-((3S)-3-amino-3-carboxypropyl)-4-demethylwyosine(37) in tRNA(Phe).UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei109S-adenosyl-L-methionine1
Binding sitei116S-adenosyl-L-methionine1
Binding sitei155S-adenosyl-L-methionine1

GO - Molecular functioni

GO - Biological processi

  • tRNA modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18048.
BRENDAi2.5.1.114. 5244.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferaseUniRule annotation (EC:2.5.1.114UniRule annotation)
Alternative name(s):
PhTYW2
tRNA wyosine derivatives biosynthesis protein Taw2UniRule annotation
Gene namesi
Name:taw2UniRule annotation
Ordered Locus Names:PH0793
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi76R → A: Loss of activity. 1 Publication1
Mutagenesisi107M → A: Decrease in activity. 1 Publication1
Mutagenesisi112N → A: Loss of activity. 1 Publication1
Mutagenesisi116R → A: Loss of activity. 1 Publication1
Mutagenesisi138H → A: Decrease in activity. 1 Publication1
Mutagenesisi142P → A: Decrease in activity. 1 Publication1
Mutagenesisi155E → A: Loss of activity. 1 Publication1
Mutagenesisi183D → A: Decrease in activity. 1 Publication1
Mutagenesisi199G → N: Decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004078491 – 278tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferaseAdd BLAST278

Interactioni

Protein-protein interaction databases

STRINGi70601.PH0793.

Structurei

Secondary structure

1278
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 14Combined sources8
Turni15 – 17Combined sources3
Helixi20 – 25Combined sources6
Beta strandi31 – 33Combined sources3
Beta strandi36 – 39Combined sources4
Helixi46 – 48Combined sources3
Helixi49 – 60Combined sources12
Beta strandi63 – 67Combined sources5
Beta strandi81 – 84Combined sources4
Beta strandi89 – 94Combined sources6
Beta strandi97 – 102Combined sources6
Turni103 – 105Combined sources3
Helixi110 – 112Combined sources3
Helixi113 – 122Combined sources10
Beta strandi128 – 131Combined sources4
Turni135 – 139Combined sources5
Helixi140 – 145Combined sources6
Beta strandi150 – 154Combined sources5
Helixi158 – 170Combined sources13
Turni174 – 176Combined sources3
Beta strandi177 – 180Combined sources4
Turni184 – 186Combined sources3
Beta strandi193 – 198Combined sources6
Helixi204 – 207Combined sources4
Helixi208 – 214Combined sources7
Beta strandi215 – 228Combined sources14
Helixi229 – 231Combined sources3
Turni232 – 236Combined sources5
Helixi237 – 246Combined sources10
Beta strandi250 – 262Combined sources13
Turni263 – 265Combined sources3
Beta strandi266 – 276Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A25X-ray2.30A1-278[»]
3A26X-ray2.50A1-278[»]
3K6RX-ray2.10A1-278[»]
ProteinModelPortaliO58523.
SMRiO58523.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58523.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni183 – 184S-adenosyl-L-methionine binding2

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG10124. Archaea.
COG2520. LUCA.
HOGENOMiHOG000222903.
KOiK07055.
OMAiGHIHGET.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01922. TYW2_archaea. 1 hit.
InterProiIPR030382. MeTrfase_TRM5/TYW2.
IPR029063. SAM-dependent_MTases.
IPR030867. TYW2_archaea.
[Graphical view]
PfamiPF02475. Met_10. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51684. SAM_MT_TRM5_TYW2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O58523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTQGIKPRI REILSKELPE ELVKLLPKRW VRIGDVLLLP LRPELEPYKH
60 70 80 90 100
RIAEVYAEVL GVKTVLRKGH IHGETRKPDY ELLYGSDTVT VHVENGIKYK
110 120 130 140 150
LDVAKIMFSP ANVKERVRMA KVAKPDELVV DMFAGIGHLS LPIAVYGKAK
160 170 180 190 200
VIAIEKDPYT FKFLVENIHL NKVEDRMSAY NMDNRDFPGE NIADRILMGY
210 220 230 240 250
VVRTHEFIPK ALSIAKDGAI IHYHNTVPEK LMPREPFETF KRITKEYGYD
260 270
VEKLNELKIK RYAPGVWHVV LDLRVFKS
Length:278
Mass (Da):32,151
Last modified:August 1, 1998 - v1
Checksum:i392887387506C3F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29886.1.
PIRiD71128.
RefSeqiWP_010884887.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA29886; BAA29886; BAA29886.
GeneIDi1443122.
KEGGipho:PH0793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29886.1.
PIRiD71128.
RefSeqiWP_010884887.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A25X-ray2.30A1-278[»]
3A26X-ray2.50A1-278[»]
3K6RX-ray2.10A1-278[»]
ProteinModelPortaliO58523.
SMRiO58523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH0793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA29886; BAA29886; BAA29886.
GeneIDi1443122.
KEGGipho:PH0793.

Phylogenomic databases

eggNOGiarCOG10124. Archaea.
COG2520. LUCA.
HOGENOMiHOG000222903.
KOiK07055.
OMAiGHIHGET.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18048.
BRENDAi2.5.1.114. 5244.

Miscellaneous databases

EvolutionaryTraceiO58523.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01922. TYW2_archaea. 1 hit.
InterProiIPR030382. MeTrfase_TRM5/TYW2.
IPR029063. SAM-dependent_MTases.
IPR030867. TYW2_archaea.
[Graphical view]
PfamiPF02475. Met_10. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51684. SAM_MT_TRM5_TYW2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTYW2_PYRHO
AccessioniPrimary (citable) accession number: O58523
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.