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Q4WE62 (CWC27_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:
Peptidyl-prolyl isomerase cwc27
Short name=PPIase cwc27
EC=5.2.1.8
Alternative name(s):
Rotamase cwc27
Gene names
Name:cwc27
ORF Names:AFUA_5G01890
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length559 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. Involved in pre-mRNA splicing By similarity.

Catalytic activity

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

Subunit structure

Associated with the spliceosome By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. CWC27 subfamily.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

spliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 559559Peptidyl-prolyl isomerase cwc27
PRO_0000064181

Regions

Domain11 – 184174PPIase cyclophilin-type
Compositional bias237 – 32084Pro-rich
Compositional bias519 – 55638Arg-rich

Sequences

Sequence LengthMass (Da)Tools
Q4WE62 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: A034433A17795D20

FASTA55962,004
        10         20         30         40         50         60 
MSAHYTTEPP PTASATLHTT FGPIHIALFA NQTPLTCKNF LQHCLDNYYA GTIFHRIVPD 

        70         80         90        100        110        120 
FIVQGGDPTG TGSGGTSIYE YPEFEYDPEA RDPNEKVVLR DELHSRLRFN RRGLVGMAKS 

       130        140        150        160        170        180 
EDGTYGSQFF ITLANAEREL NGQCTLFGRV EGDSIYNVLK IAEAERVERT ERPVYPVKVV 

       190        200        210        220        230        240 
SCEVGELGPF AGKLKRRETI ATAPAAEEKP AAKKKKKAKG GKTLLSFGGD EGDEDVPLRP 

       250        260        270        280        290        300 
SKPKFNPTLV VDAGIPPAND APKKTSPEAE QQTRKRPRSP SPRRSLSAER KHRPKTPDPL 

       310        320        330        340        350        360 
TQLPLPDPES PARSPPQSPP ARQSILSRTR AEIENLKASM RRTVATGPAD TGRKKSALEA 

       370        380        390        400        410        420 
MIPETAIRGR KRPPPGTVNG AGRGSSTNGV TGFSSAAEDE TLRMFNAFKA KLESADAKSG 

       430        440        450        460        470        480 
PHGKTSISAS DTTKYTSQAK SNTEPEDEEA QLCDLHFIAN CQSCKSWDDT GTAEEAPDDD 

       490        500        510        520        530        540 
DRDWLTHELR FGKDMLGKDL QWKREHPDDV DSLVVIDPRE REKEFVGGKR RGLERDRERD 

       550 
RKRERVGDQE WDRRRREKP

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAHF01000011 Genomic DNA. Translation: EAL86115.1.
RefSeqXP_748153.1. XM_743060.1.

3D structure databases

ProteinModelPortalQ4WE62.
SMRQ4WE62. Positions 6-186.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00002898; CADAFUAP00002898; CADAFUAG00002898.
GeneID3505738.
GenomeReviewsGene locus cwc27 in contig CM000173_GR.
KEGGafm:AFUA_5G01890.

Phylogenomic databases

eggNOGfuNOG06026.
GeneTreeEFGT00050000000590.
HOGENOMHBG328350.
OMAFIANCQS.
OrthoDBEOG4XD70H.

Family and domain databases

InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KOK12737.
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCWC27_ASPFU
AccessionPrimary (citable) accession number: Q4WE62
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 5, 2005
Last modified: January 25, 2012
This is version 52 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

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