O42941 (CYP7_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidylprolyl isomerase cyp7
Short name=PPIase cyp7
EC=5.2.1.8

Alternative name(s):
Complexed with cdc5 protein 27
Cyclophilin 7
Rotamase cyp7

Gene names

Name:	cyp7
Synonyms:	cwf27
ORF Names:	SPBC16H5.05c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in pre-mRNA splicing.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Belongs to the 40S cdc5-associated complex (or cwf complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5, cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27, cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16, cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26, cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10, prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1, smd1, smd3, smf1, smg1 and syf2.
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 Reference proteome
Gene Ontology (GO)
Biological process	nuclear mRNA cis splicing, via spliceosome Inferred by curator. Source: GeneDB_Spombe protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complex Inferred from direct assay. Source: GeneDB_Spombe
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 – 463	463	Peptidylprolyl isomerase cyp7		PRO_0000064178
Regions
	Domain	11 – 166	156	PPIase cyclophilin-type
	Compositional bias	235 – 318	84	Ser-rich

Sequences

	Sequence		Length	Mass (Da)
	O42941 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: D7A3148A3CD74A83	FASTA	463	52,174
	10 20 30 40 50 60 MATLTNLEPL ATGTVILKTT RGDIQIELWC KEVPKACRNF IQLCLEGYYD GTIVHRVVPE 70 80 90 100 110 120 FLIQGGDPTG TGMGGESIYG EPFAVETHPR LRFIRRGLVG MACTENEGNN SQFFITLGPT 130 140 150 160 170 180 PEWNGKQTLF GRVVGDTIYN VVRISELELD ANQRPVFPPK IISTEVIDNY FTDIKPRSTK 190 200 210 220 230 240 EEREKIANEL AHQEKQKERN KLLKSGRRNK AVLSFGDEVD MPIVKKPLRQ KTPVSRSSDT 250 260 270 280 290 300 TTELSKDLIS SSSSIHSTYS SAQTGLTSAK VSSDEYARQV DTLDTKLNSS SKSKVQEEIS 310 320 330 340 350 360 RLKSELRDLE KSGGSSNSKP VVVRPKKRNI LTEELEKYKK SKKVVLGKRK NLENDEESTL 370 380 390 400 410 420 RALSSFQSKI RNAEDEDVMD SQYGSKIEDT PCSLHNVPGC FSCFDRLGEK NITETNSNWF 430 440 450 460 AHRLVAENDP TRRTEELRIQ RAEELKDVPS ARPKKLLMKR DII

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs." Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L. Mol. Cell. Biol. 22:2011-2024(2002) [PubMed: 11884590] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE CWF COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA17903.1.
PIR	T39621.
RefSeq	NP_595943.1. NM_001021851.1.
3D structure databases
ProteinModelPortal	O42941.
SMR	O42941. Positions 8-171.
ModBase	Search...
Protein-protein interaction databases
IntAct	O42941. 1 interaction.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC16H5.05c.1; SPBC16H5.05c.1:pep; SPBC16H5.05c.
GeneID	2540067.
GenomeReviews	Gene locus cyp7 in contig CU329671_GR.
KEGG	spo:SPBC16H5.05c.
NMPDR	fig|4896.1.peg.1809.
Organism-specific databases
GeneDB_Spombe	SPBC16H5.05c.
Phylogenomic databases
eggNOG	fuNOG06026.
GeneTree	EFGT00050000000590.
HOGENOM	HBG735081.
OMA	MACTENE.
OrthoDB	EOG4XD70H.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004008-MONOMER.
Gene expression databases
ArrayExpress	O42941.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KO	K12737.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYP7_SCHPO

Accession

Primary (citable) accession number: O42941

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program