Reviewed, UniProtKB/Swiss-Prot Q4WE62 (CWC27_ASPFU)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl isomerase cwc27
    EC=5.2.1.8

Gene names

Name:	cwc27
ORF Names:	AFUA_5G01890

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	559 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 – 559	559	Peptidyl-prolyl isomerase cwc27		PRO_0000064181
Regions
	Domain	11 – 184	174	PPIase cyclophilin-type
	Compositional bias	237 – 320	84	Pro-rich
	Compositional bias	519 – 556	38	Arg-rich

Sequences

	Sequence		Length	Mass (Da)
	Q4WE62-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: A034433A17795D20	FASTA	559	62,004
	10 20 30 40 50 60 MSAHYTTEPP PTASATLHTT FGPIHIALFA NQTPLTCKNF LQHCLDNYYA GTIFHRIVPD 70 80 90 100 110 120 FIVQGGDPTG TGSGGTSIYE YPEFEYDPEA RDPNEKVVLR DELHSRLRFN RRGLVGMAKS 130 140 150 160 170 180 EDGTYGSQFF ITLANAEREL NGQCTLFGRV EGDSIYNVLK IAEAERVERT ERPVYPVKVV 190 200 210 220 230 240 SCEVGELGPF AGKLKRRETI ATAPAAEEKP AAKKKKKAKG GKTLLSFGGD EGDEDVPLRP 250 260 270 280 290 300 SKPKFNPTLV VDAGIPPAND APKKTSPEAE QQTRKRPRSP SPRRSLSAER KHRPKTPDPL 310 320 330 340 350 360 TQLPLPDPES PARSPPQSPP ARQSILSRTR AEIENLKASM RRTVATGPAD TGRKKSALEA 370 380 390 400 410 420 MIPETAIRGR KRPPPGTVNG AGRGSSTNGV TGFSSAAEDE TLRMFNAFKA KLESADAKSG 430 440 450 460 470 480 PHGKTSISAS DTTKYTSQAK SNTEPEDEEA QLCDLHFIAN CQSCKSWDDT GTAEEAPDDD 490 500 510 520 530 540 DRDWLTHELR FGKDMLGKDL QWKREHPDDV DSLVVIDPRE REKEFVGGKR RGLERDRERD 550 RKRERVGDQE WDRRRREKP

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000011 Genomic DNA. Translation: EAL86115.1.
RefSeq	XP_748153.1.
3D structure databases
SMR	Q4WE62. Positions 6-186.
ModBase	Search...
Genome annotation databases
GeneID	3505738.
KEGG	afm:AFUA_5G01890.
Phylogenomic databases
eggNOG	fuNOG06026.
HOGENOM	HBG328350.
OMA	LGMANEG.
OrthoDB	EOG9T1K3P.
PhylomeDB	Q4WE62.
Enzyme and pathway databases
BRENDA	5.2.1.8. 18841.
Family and domain databases
InterPro	IPR015891. Cyclophilin-like. IPR020892. Pep-Pro_Isoase_cyclophilin_CS. IPR002130. PPIase_cyclophilin. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CWC27_ASPFU

Accession

Primary (citable) accession number: Q4WE62

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	July 5, 2005
Last modified:	February 9, 2010
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)