Q4WHY9 (Q4WHY9_ASPFU) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase RuleBase RU000493
EC=5.2.1.8 RuleBase RU000493

Gene names

ORF Names:

AFUA_2G03720 EMBL EAL87466.1

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome] EMBL EAL87466.1

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Neosartorya fumigata

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins By similarity. RuleBase RU000493 PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity. RuleBase RU004223
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0). RuleBase RU000493 SAAS SAAS020892
Sequence similarities	Belongs to the cyclophilin-type PPIase family. RuleBase RU004223 Contains 1 PPIase cyclophilin-type domain. RuleBase RU003420 SAAS SAAS020892
Caution	The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. EMBL EAL87466.1

Ontologies

Keywords
Molecular function	Isomerase Rotamase SAAS SAAS020892 RuleBase RU003420
Technical term	3D-structure PDB 2C3B Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q4WHY9 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 28B077F443AA78D8	FASTA	205	22,290
	10 20 30 40 50 60 MSQVFFDVEY APVGTAETSA RNCAQSGLDA FGLQSILSIL FTDGILLRAV TAKVGRIVFN 70 80 90 100 110 120 LFDKDVPKTA KNFRELCKRP AGEGYRESTF HRIIPNFMIQ GGDFTRGNGT GGRSIYGDKF 130 140 150 160 170 180 ADENFSRKHD KKGILSMANA GPNTNGSQFF ITTAVTSWLD GKHVVFGEVA DEKSYSVVKE 190 200 IEALGSSSGS VRSNTRPKIV NCGEL

References

	« Hide 'large scale' referencesShow 'large scale' 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[2]	"The crystal structure of Aspergillus fumigatus cyclophilin reveals 3D domain swapping of a central element." Limacher A., Kloer D.P., Fluckiger S., Folkers G., Crameri R., Scapozza L. Structure 14:185-195(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AAHF01000008 Genomic DNA. Translation: EAL87466.1.

RefSeq

XP_749504.1. XM_744411.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C3B	X-ray	1.85	A/B	1-205	[»]

ProteinModelPortal

Q4WHY9.

SMR

Q4WHY9. Positions 1-205.

ModBase

Search...

Protein-protein interaction databases

STRING

5085.CADAFUAP00003559.

Proteomic databases

PRIDE

Q4WHY9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

CADAFUAT00003559; CADAFUAP00003559; CADAFUAG00003559.

GeneID

3506781.

KEGG

afm:AFUA_2G03720.

Phylogenomic databases

HOGENOM

HOG000065981.

KO

K01802.

OMA

NFRELCK.

OrthoDB

EOG4DZ54P.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PIRSF

PIRSF001467. Peptidylpro_ismrse. 1 hit.

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...

Other

EvolutionaryTrace

Q4WHY9.

Entry information

Entry name

Q4WHY9_ASPFU

Accession

Primary (citable) accession number: Q4WHY9

Entry history

Integrated into UniProtKB/TrEMBL:	July 5, 2005
Last sequence update:	July 5, 2005
Last modified:	April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)