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Protein

FKBP-type peptidyl-prolyl cis-trans isomerase

Gene
N/A
Organism
Methanothermococcus thermolithotrophicus (Methanococcus thermolithotrophicus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by FK506.

Temperature dependencei

Thermostable.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BRENDAi5.2.1.8. 3266.

Names & Taxonomyi

Protein namesi
Recommended name:
FKBP-type peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
MtFK
Rotamase
OrganismiMethanothermococcus thermolithotrophicus (Methanococcus thermolithotrophicus)
Taxonomic identifieri2186 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanothermococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000753781 – 154FKBP-type peptidyl-prolyl cis-trans isomeraseAdd BLAST154

Structurei

Secondary structure

1154
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 13Combined sources4
Beta strandi26 – 28Combined sources3
Helixi30 – 36Combined sources7
Beta strandi48 – 51Combined sources4
Turni52 – 55Combined sources4
Helixi59 – 66Combined sources8
Beta strandi75 – 78Combined sources4
Turni80 – 82Combined sources3
Helixi98 – 101Combined sources4
Beta strandi111 – 117Combined sources7
Beta strandi119 – 126Combined sources8
Beta strandi129 – 133Combined sources5
Beta strandi143 – 146Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IX5NMR-A4-154[»]
ProteinModelPortaliO52980.
SMRiO52980.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO52980.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 112PPIase FKBP-typePROSITE-ProRule annotationAdd BLAST102

Sequence similaritiesi

Belongs to the FKBP-type PPIase family.Curated
Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O52980-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIFLVDKGVK IKVDYIGKLE SGDVFDTSIE EVAKEAGIYA PDREYEPLEF
60 70 80 90 100
VVGEGQLIQG FEEAVLDMEV GDEKTVKIPA EKAYGNRNEM LIQKIPRDAF
110 120 130 140 150
KEADFEPEEG MVILAEGIPA TITEVTDNEV TLDFNHELAG KDLVFTIKII

EVVE
Length:154
Mass (Da):17,184
Last modified:June 1, 1998 - v1
Checksum:i2CD3DDF8B26A006F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89881 Genomic DNA. Translation: BAA24446.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89881 Genomic DNA. Translation: BAA24446.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IX5NMR-A4-154[»]
ProteinModelPortaliO52980.
SMRiO52980.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi5.2.1.8. 3266.

Miscellaneous databases

EvolutionaryTraceiO52980.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFKBP_METTL
AccessioniPrimary (citable) accession number: O52980
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: November 2, 2016
This is version 68 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

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.