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Q9P3X9 (PPID_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
41 kDa peptidyl-prolyl cis-trans isomerase

Short name=PPIase
EC=5.2.1.8
Alternative name(s):
Cyclophilin-41
Short name=CyP41
Rotamase
Gene names
Name:cyp-41
ORF Names:NCU03853
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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).

Subunit structure

Interacts with CyPBP37. Ref.1

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.

Contains 1 PPIase cyclophilin-type domain.

Contains 3 TPR repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRepeat
TPR repeat
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein peptidyl-prolyl isomerization

Inferred from electronic annotation. Source: GOC

protein refolding

Inferred from electronic annotation. Source: EnsemblFungi

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-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 – 37537541 kDa peptidyl-prolyl cis-trans isomerase
PRO_0000064156

Regions

Domain15 – 178164PPIase cyclophilin-type
Repeat222 – 25534TPR 1
Repeat274 – 30734TPR 2
Repeat312 – 34534TPR 3

Sequences

Sequence LengthMass (Da)Tools
Q9P3X9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F5A1B3C078800994

FASTA37540,571
        10         20         30         40         50         60 
MSSTDDVKQA RSRVFFDITI GGKAAGRIVF ELYNDIVPKT AENFRALCTG EKGVGKLGKP 

        70         80         90        100        110        120 
LHYKGSTFHR VIKQFMIQGG DFTAGNGTGG ESIYGAKFED ENFQLKHDRP FLLSMANAGP 

       130        140        150        160        170        180 
GTNGSQFFVT TVPTPHLDGK HVVFGEVLSG KSVVRQIENL KTQGDKPTKD AVIADCGELS 

       190        200        210        220        230        240 
GDAAVSADTK TADAYGDEYE DFPEDEATDG QPLSASKILK IATDCKDFGN KAFKAGDLPV 

       250        260        270        280        290        300 
ALDKYQKGLR YLNEDPELDN EPADTKQKLD ALRVSLNSNA ALMNMKLSAW DECIRSADGA 

       310        320        330        340        350        360 
LAVATISDKD RAKALYRRGY AQVRIKDEDS ALTSLEEAKK LAPEDGAIVN ELAAVKKAAA 

       370 
ARMAKEKAAY KKFFS 

« Hide

References

« Hide 'large scale' references
[1]"A novel binding protein for a member of CyP40-type Cyclophilins: N.crassa CyPBP37, a growth and thiamine regulated protein homolog to yeast Thi4p."
Faou P., Tropschug M.
J. Mol. Biol. 333:831-844(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CYPBP37.
Strain: 74A.
[2]"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] [Europe PMC] [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

EMBL
GenBank
DDBJ
AJ292563 mRNA. Translation: CAC00484.1.
AABX02000012 Genomic DNA. Translation: EAA26627.1.
RefSeqXP_955863.1. XM_950770.1.
UniGeneNcr.15757.

3D structure databases

ProteinModelPortalQ9P3X9.
SMRQ9P3X9. Positions 7-370.
ModBaseSearch...

Protein-protein interaction databases

STRING5141.NCU03853.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000003630; EFNCRP00000003630; EFNCRG00000003626.
GeneID3872010.
KEGGncr:NCU03853.

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000065980.
KOK05864.
OMACKLKLSD.
OrthoDBEOG4J9R7J.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPID_NEUCR
AccessionPrimary (citable) accession number: Q9P3X9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2000
Last modified: April 3, 2013
This is version 85 of the entry and version 1 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