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Reviewed, UniProtKB/Swiss-Prot P20080 (FKB1A_NEUCR)

Last modified September 1, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase fkr-2
      Short name=PPIase fkr-2
    EC=5.2.1.8
Alternative name(s):
    FK506-binding protein 1A
      Short name=FKBP-1A
Gene names
Name: fkr-2
Synonyms: fpr-1a
ORF Names: 9G6.180, NCU04140
OrganismNeurospora crassa [Complete proteome]
Taxonomic identifier5141 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length120 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Subcellular location

Cytoplasm.

Miscellaneous

Binds to the immunosuppressant drug FK506.

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP1 subfamily.

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

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

Chain1 – 120120Peptidyl-prolyl cis-trans isomerase fkr-2
PRO_0000075303

Regions

Domain26 – 11489PPIase FKBP-type

Sequences

Sequence LengthMass (Da)Tools
P20080-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: AF97183C041563B7

FASTA12013,037
        10         20         30         40         50         60 
MTIPQLDGLQ IEVQQEGQGT RETRRGDNVD VHYKGVLTSG KKFDASYDRG EPLNFTVGQG 

        70         80         90        100        110        120 
QVIKGWDEGL LGMKIGEKRK LTIAPHLAYG NRAVGGIIPA NSTLIFETEL VGIKGVQKGE 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding."
Tropschug M., Wachter E., Mayer S., Schoenbrunner E.R., Schmid F.X.
Nature 346:674-677(1990) [PubMed: 1696687] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
Nucleic Acids Res. 31:1944-1954(2003) [PubMed: 12655011] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed: 12712197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases

X55743 Genomic DNA. Translation: CAA39274.1.
AL513463 Genomic DNA. Translation: CAC28766.1.
AABX02000013 Genomic DNA. Translation: EAA32060.2. Different initiation.
PIRS11090.

3D structure databases

HSSPHSSP built from PDB template 1KT1 based on UniProtKB Q9XSH5.
ModBaseSearch...

Protein-protein interaction databases

STRINGP20080.

Genome annotation databases

NMPDRfig|5141.1.peg.1413.

Enzyme and pathway databases

BioCycNCRA-XX3-01:NCRA-XX3-01-007888-MON.
BRENDA5.2.1.8. 266.

Family and domain databases

InterProIPR001179. PPIase_FKBP.
[Graphical view]
PANTHERPTHR10516. PPIase_FKBP. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFKB1A_NEUCR
AccessionPrimary (citable) accession number: P20080
Secondary accession number(s): Q7S7U2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: September 1, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents