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A8X8D0 (CYP9_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase 9

Short name=PPIase 9
EC=5.2.1.8
Alternative name(s):
Cyclophilin-9
Rotamase 9
Gene names
Name:cyn-9
Synonyms:cyp-9
ORF Names:CBG09202
OrganismCaenorhabditis briggsae
Taxonomic identifier6238 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imid ic peptide bonds in oligopeptides. Thought to function as a catalyst in the folding and modification of cuticle collagens By similarity. UniProtKB Q09637

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0). UniProtKB Q09637

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Sequence caution

The sequence CAB40202.1 differs from that shown. Reason: Erroneous gene model prediction. UniProtKB Q09637

Ontologies

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

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 – 313313Peptidyl-prolyl cis-trans isomerase 9
PRO_0000332946

Regions

Domain9 – 174166PPIase cyclophilin-type

Sequences

Sequence LengthMass (Da)Tools
A8X8D0 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 06AA294B751FFCA3

FASTA31335,787
        10         20         30         40         50         60 
MSSLEKRVFL DMALDEKPIG RIEIKLFTSE APKTCENFRA LCTGEVGMAP NNKARLHYKG 

        70         80         90        100        110        120 
NEIHRVVKKF MIQGGDITDG DGRGGFSIYG RYFDDEKFVL KHSKPYLLSM ANKGPNSNSS 

       130        140        150        160        170        180 
QFFITTAPAP HCNGKHVVFG EVIKGREVVD VLDNLEVDGK SKPIAKVRIF NSGELVKKKK 

       190        200        210        220        230        240 
PSKTKEELAA LEERKRQEAK KDIPDIPKSW LYRDNEERES DFSSKTESSR VRSRSKSPSN 

       250        260        270        280        290        300 
NYETRRGHMA NSRGDRNRRT QRADRKDDFG IAVRGRGGVQ FRRVRYVTPE HWRRNAPSKW 

       310 
QQGSYTHPVD LQP 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics."
Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. expand/collapse author list , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H.
PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AF16.
[2]"A highly conserved nematode protein folding operon in Caenorhabditis elegans and Caenorhabditis briggsae."
Page A.P.
Gene 230:267-275(1999) [PubMed: 10216266] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-249, NUCLEOTIDE SEQUENCE [MRNA] OF 1-141.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CAAC02000487 Genomic DNA. Translation: CAP28891.2.
AJ005807 Genomic DNA. Translation: CAB40202.1. Sequence problems.
AJ005809 mRNA. Translation: CAB40206.1.

3D structure databases

ProteinModelPortalA8X8D0.
SMRA8X8D0. Positions 5-178.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

WormBaseCBG09202; CBP25106; WBGene00030832.

Phylogenomic databases

HOGENOMHBG610621.

Family and domain databases

InterProIPR002130. Cyclophilin-like_PPIase_dom.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. False negative.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYP9_CAEBR
AccessionPrimary (citable) accession number: A8X8D0
Secondary accession number(s): Q9XTP5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 26 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families