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Q5AUG9 (CWC27_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:AN8061
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length558 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 – 558558Peptidyl-prolyl isomerase cwc27
PRO_0000064184

Regions

Domain11 – 184174PPIase cyclophilin-type
Compositional bias274 – 31845Pro-rich

Sequences

Sequence LengthMass (Da)Tools
Q5AUG9 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 6CC2F07401DE6661

FASTA55861,731
        10         20         30         40         50         60 
MSAHYATEPA PTASATLHTT FGPLHIALFA KQTPLTCRNF LQHCMDNYYA GTIFHRVVPD 

        70         80         90        100        110        120 
FIIQGGDPTG TGSGGTSIYE YPEFEYDPDA RDPNEKVVLR DEIHSRLRFN RRGLVGMAKS 

       130        140        150        160        170        180 
EDGSYGSQFF ITLANTEREL NGQCTLFGRL EGDSLYNMLK IAEAERIEGT ERPVYPVKIT 

       190        200        210        220        230        240 
SCEVGDLGPF VDKVKKRQVV ATGPKTEEKP AAKKKKKAKP GKALLSFGGD DEEDEDMPIR 

       250        260        270        280        290        300 
PAKPKFNPML VTDTKLPEKE SSTKGEASQT RKRPRSPSPK RQPQPSAPPK NRPKTPEPTK 

       310        320        330        340        350        360 
QLPLPNPESP ERSPSPPPKQ SFLSRTNAEI ENLKASMRRT AHAPAAETKP KSALEAMIPQ 

       370        380        390        400        410        420 
TAIRGRKRPP PGSVSASTSA PNGITGFSSN SAEAEALKMF NAFRAKLESS DSQPTAAAAK 

       430        440        450        460        470        480 
RLSVAKTDAA EERKETPDED EESQLCDLHF IANCQSCKSW DNDVEGGANN GADDDVNDSG 

       490        500        510        520        530        540 
WLNHQLRFGK DTLGKDLNWK REHQDVDTLM VIDPREKEKE LADSSRPGTK RVKGRGLERD 

       550 
RERERKKGRV GDLEWSKR 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000139 Genomic DNA. Translation: EAA59683.1.
BN001302 Genomic DNA. Translation: CBF73806.1.
RefSeqXP_681330.1. XM_676238.1.

3D structure databases

ProteinModelPortalQ5AUG9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00004087; CADANIAP00004087; CADANIAG00004087.
GeneID2869127.
KEGGani:AN8061.2.

Phylogenomic databases

OMAFIANCQS.
OrthoDBEOG4XD70H.
PhylomeDBQ5AUG9.

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_EMENI
AccessionPrimary (citable) accession number: Q5AUG9
Secondary accession number(s): C8V676
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: April 26, 2005
Last modified: January 25, 2012
This is version 48 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