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Reviewed, UniProtKB/Swiss-Prot Q4WLV6 (FKB1A_ASPFU)

Last modified February 9, 2010. Version 32. 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:
    FK506-binding protein 1A
      Short name=FKBP
    EC=5.2.1.8
Alternative name(s):
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
    Rapamycin-binding protein
Gene names
Name: fpr1A
ORF Names: AFUA_6G12170
OrganismAspergillus fumigatus (Sartorya fumigata) [Complete proteome]
Taxonomic identifier5085 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length112 AA.
Sequence statusComplete.
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

Cytoplasm By similarity.

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 – 112112FK506-binding protein 1A
PRO_0000233318

Regions

Domain20 – 10889PPIase FKBP-type

Sequences

Sequence LengthMass (Da)Tools
Q4WLV6-1 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: FE59C09795C8E07E

FASTA11212,130
        10         20         30         40         50         60 
MGVTKELKSP GNGVDFPKKG DFVTIHYTGR LTDGSKFDSS VDRNEPFQTQ IGTGRVIKGW 

        70         80         90        100        110 
DEGVPQMSLG EKAVLTITPD YGYGARGFPP VIPGNSTLIF EVELLGINNK RA 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000006 Genomic DNA. Translation: EAL89058.1.
RefSeqXP_751096.1.

3D structure databases

SMRQ4WLV6. Positions 9-108.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4WLV6.

Genome annotation databases

GeneID3508401.
KEGGafm:AFUA_6G12170.

Phylogenomic databases

eggNOGfuNOG09243.
HOGENOMHBG731200.
OMAMTADYAY.
OrthoDBEOG9PNZZZ.
PhylomeDBQ4WLV6.

Enzyme and pathway databases

BRENDA5.2.1.8. 18841.

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_ASPFU
AccessionPrimary (citable) accession number: Q4WLV6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 5, 2005
Last modified: February 9, 2010
This is version 32 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