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O52980

- FKBP_METTL

UniProt

O52980 - FKBP_METTL

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Protein

FKBP-type peptidyl-prolyl cis-trans isomerase

Gene
N/A
Organism
Methanothermococcus thermolithotrophicus (Methanococcus thermolithotrophicus)
Status
Reviewed - 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

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 154154FKBP-type peptidyl-prolyl cis-trans isomerasePRO_0000075378Add
BLAST

Structurei

Secondary structure

1
154
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Beta strandi26 – 283Combined sources
Helixi30 – 367Combined sources
Beta strandi48 – 514Combined sources
Turni52 – 554Combined sources
Helixi59 – 668Combined sources
Beta strandi75 – 784Combined sources
Turni80 – 823Combined sources
Helixi98 – 1014Combined sources
Beta strandi111 – 1177Combined sources
Beta strandi119 – 1268Combined sources
Beta strandi129 – 1335Combined sources
Beta strandi143 – 1464Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IX5NMR-A4-154[»]
ProteinModelPortaliO52980.
SMRiO52980. Positions 4-154.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO52980.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 112102PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

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. 1 hit.
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
Entry Method Resolution (Å) Chain Positions PDBsum
1IX5 NMR - A 4-154 [» ]
ProteinModelPortali O52980.
SMRi O52980. Positions 4-154.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 5.2.1.8. 3266.

Miscellaneous databases

EvolutionaryTracei O52980.

Family and domain databases

InterProi IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view ]
PANTHERi PTHR10516. PTHR10516. 1 hit.
Pfami PF00254. FKBP_C. 1 hit.
[Graphical view ]
PROSITEi PS50059. FKBP_PPIASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Biochemical and genetic characterization of an FK506-sensitive peptidyl prolyl cis-trans isomerase from a thermophilic archaeon, Methanococcus thermolithotrophicus."
    Furutani M., Iida T., Yamano S., Kamino K., Maruyama T.
    J. Bacteriol. 180:388-394(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: ATCC 35097 / DSM 2095 / JCM 10549 / OCM 138 / SN-1.

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 26, 2014
This is version 62 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

External Data

Dasty 3