Reviewed, UniProtKB/Swiss-Prot O74942 (CYP9_SCHPO)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase 9
      Short name=PPIase cyp9
      Short name=Rotamase cyp9
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin 9

Gene names

Name:	cyp9
ORF Names:	SPCC553.04

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	610 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subcellular location	Nucleus. Ref.2
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain. Contains 3 WD repeats.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat WD repeat
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Ref.2 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 – 610	610	Peptidyl-prolyl cis-trans isomerase 9		PRO_0000358863
Regions
	Repeat	45 – 83	39	WD 1
	Repeat	88 – 127	40	WD 2
	Repeat	177 – 216	40	WD 3
	Domain	453 – 607	155	PPIase cyclophilin-type
Amino acid modifications
	Modified residue	13	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O74942-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 28D06D189C76DF3B	FASTA	610	69,048
	10 20 30 40 50 60 MMDGASPVDR DVSPVGLPKK RIKQNHDQVF LHNLPDAPRY TKSYMHNAEI YKCFPTKSNY 70 80 90 100 110 120 ILSVSYDGYV KFWHKTPNGV EYIKEFHAHN AMLLSAELSQ DERLFITGAD DKSLKVFDVE 130 140 150 160 170 180 SIDLVNIIDL EFLPKAICCF NSPSLKTSLI AVSSAESPLI FFFESGGDGE VLYTVKKHTA 190 200 210 220 230 240 PVHCLRYLST LDCFLSIDIG GMVEYWSPEE PFQKPDTAEL FNMKSQTDLY IFKKQKSVPT 250 260 270 280 290 300 SLEVSHFENF WSTISYPDCK VRVFDTKSGR AILELDENPS NAAKKVEALF EKEDTESSYY 310 320 330 340 350 360 MSHVELGRRI AIERDIEKHG LTVGTTAIFD ESEKYLLYGS IVGIKVVSID NGTVVRIYGK 370 380 390 400 410 420 DEAVRFTRLS LYQQAPKKSN LPSLDVIASN NPLVEESFQK DPTLFATAWK KQRFYLFSNM 430 440 450 460 470 480 STKFTLSDRD VYNEQVLPVT NNEGRQENGN ILLGKAAIIH TTQGDISIKL YPEEAPKAVQ 490 500 510 520 530 540 NFTTHAENGY YDNTIFHRII KNFMIQGGDP LGDGTGGESI WKKDFEDEIS PNLKHDRPFT 550 560 570 580 590 600 VSMANSGPNT NGSQFFITTD LTPWLDGKHT IFARAYAGLD VVHRIEQGET DKYDRPLEPT 610 KIINISIVYT

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: ATCC 38366 / 972.
[2]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAA19257.1.
PIR	T41399.
RefSeq	NP_587769.1.
3D structure databases
HSSP	HSSP built from PDB template 1IST based on UniProtKB P14832.
ModBase	Search...
Genome annotation databases
GeneID	2539557.
GenomeReviews	Gene locus cyp9 in contig CU329672_GR.
KEGG	spo:SPCC553.04.
NMPDR	fig|4896.1.peg.107.
Organism-specific databases
GeneDB_Spombe	SPCC553.04.
Phylogenomic databases
OMA	HTIFARA.
Gene expression databases
ArrayExpress	O74942.
Family and domain databases
InterPro	IPR002130. PPIase_cyclophilin. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR019782. WD40_repeat_2. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. IPR019781. WD40_repeat_sg. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit. G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
Pfam	PF00160. Pro_isomerase. 1 hit. PF00400. WD40. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SMART	SM00320. WD40. 4 hits. [Graphical view]
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. 1 hit. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYP9_SCHPO

Accession

Primary (citable) accession number: O74942

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	November 1, 1998
Last modified:	November 3, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)