Q6BWH6 (CWC27_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl isomerase CWC27
Short name=PPIase CWC27
EC=5.2.1.8

Alternative name(s):
Rotamase CWC27

Gene names

Name:	CWC27
Ordered Locus Names:	DEHA2B11308g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Molecular function	Isomerase Rotamase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	RNA 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 component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 327	327	Peptidyl-prolyl isomerase CWC27		PRO_0000064183
Regions
	Domain	8 – 158	151	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	Q6BWH6 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 2C4F4D829F337B2F	FASTA	327	37,319
	10 20 30 40 50 60 MSSLEPATTA KVALITTKGP IEIELWAKEV PNITRVFIQN CLDKKYIGTT FNKVIKDYLV 70 80 90 100 110 120 QTSKIKEPAT LKLKDEFHSR LKFNKRGLVG AVHDDKRNSN NVDSLFITLK PTPEFNNNYV 130 140 150 160 170 180 LFGKIMGDSI YNVVKINESE LKSEETPMYP AEITDIKILV QYFDDLVESK EHIAEPAKKK 190 200 210 220 230 240 AKKAKKPRVK LDYTLEDEED TGFKMKSAHD LLSDSKLSNK LYANKKKGPS ENNEKQKTIE 250 260 270 280 290 300 KAQDSSMETK KIVPERPDYK GSEEIENETK ITSSENMNHE TKQDKPNYKA KLDRNPNIDS 310 320 DYDSDLDLSS SESIDLFAFK QSNFQSS

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382134 Genomic DNA. Translation: CAG85447.1.
RefSeq	XP_457443.1. XM_457443.1.
3D structure databases
ProteinModelPortal	Q6BWH6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2913378.
GenomeReviews	Gene locus DEHA2B11308g in contig CR382134_GR.
KEGG	dha:DEHA2B11308g.
Phylogenomic databases
eggNOG	fuNOG06026.
OMA	IELWAKE.
OrthoDB	EOG4XD70H.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KO	K12737.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. False negative. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CWC27_DEBHA

Accession

Primary (citable) accession number: Q6BWH6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program