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Q4IN00 (FKBP2_GIBZE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FK506-binding protein 2

EC=5.2.1.8
Alternative name(s):
Peptidyl-prolyl cis-trans isomerase
Short name=PPIase
Rotamase
Gene names
Name:FPR2
ORF Names:FGSG_01408
OrganismGibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum) [Reference proteome]
Taxonomic identifier229533 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.

Catalytic activity

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

Enzyme regulation

Inhibited by both FK506 and rapamycin By similarity.

Subcellular location

Endoplasmic reticulum By similarity.

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP2 subfamily.

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 195176FK506-binding protein 2
PRO_0000233069

Regions

Domain39 – 12789PPIase FKBP-type
Motif192 – 1954Prevents secretion from ER Potential

Sequences

Sequence LengthMass (Da)Tools
Q4IN00 [UniParc].

Last modified April 18, 2006. Version 2.
Checksum: 4CDDCC233DFCBF51

FASTA19520,421
        10         20         30         40         50         60 
MKAALFLSAL ASTAVGVVAE ELKIDVTLPV ICERKTQKGD GVHMHYRGTL KDSGKQFDAS 

        70         80         90        100        110        120 
YDRGTPLSFK VGAGQVIKGW DEGLLDMCIG EKRVLTIPPE FGYGQRAIGP IPAGSTLVFE 

       130        140        150        160        170        180 
TELVGIDGVP KPEKIETKVV EGAESAAEAI SEATEAAATA SQKVAGKVAE AIVDAAKAAK 

       190 
TIIADTDDAP EHEEL 

« Hide

References

« Hide 'large scale' references
[1]"The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization."
Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S. expand/collapse author list , Goswami R.S., Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.
Science 317:1400-1402(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.
[2]"Comparative genomics reveals mobile pathogenicity chromosomes in Fusarium."
Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., Antoniw J., Baker S.E. expand/collapse author list , Bluhm B.H., Breakspear A., Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., Rep M.
Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.
[3]"Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires."
Pemberton T.J.
BMC Genomics 7:244-244(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVISION OF GENE MODEL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS231663 Genomic DNA. Translation: ESU06720.1.

3D structure databases

ProteinModelPortalQ4IN00.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5518.FG01408.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiFGSG_01408T0; FGSG_01408P0; FGSG_01408.

Phylogenomic databases

eggNOGCOG0545.
OrthoDBEOG77WWQ3.

Family and domain databases

InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFKBP2_GIBZE
AccessionPrimary (citable) accession number: Q4IN00
Secondary accession number(s): V6R4C2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: April 18, 2006
Last modified: May 14, 2014
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families