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Q4WP12

- PPIB_ASPFU

UniProt

Q4WP12 - PPIB_ASPFU

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Protein
Peptidyl-prolyl cis-trans isomerase B
Gene
cpr2, AFUA_4G07650
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by cyclosporin A (CsA) By similarity.

GO - Molecular functioni

  1. peptide binding Source: UniProtKB-KW
  2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase B (EC:5.2.1.8)
Short name:
PPIase B
Alternative name(s):
Rotamase B
Gene namesi
Name:cpr2
ORF Names:AFUA_4G07650
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 4

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 209186Peptidyl-prolyl cis-trans isomerase B
PRO_0000233043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi140 – 1401N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ4WP12.

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00008354.

Structurei

3D structure databases

ProteinModelPortaliQ4WP12.
SMRiQ4WP12. Positions 30-197.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 196158PPIase cyclophilin-type
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi206 – 2094Prevents secretion from ER

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0652.
HOGENOMiHOG000065981.
KOiK03768.
OMAiPSVANDK.
OrthoDBiEOG757D7G.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4WP12-1 [UniParc]FASTAAdd to Basket

« Hide

MNFKSLFLSF FLVFAVGLAL VHAEETKEPR GPKITSKVFF DIEHGDKPLG    50
RIVLGLYGKT VPKTAENFRA LATGEKGFGY EGSTFHRVIK SFMIQGGDFT 100
RGDGTGGKSI YGEKFADENF KLRHTRKGLL SMANAGKDTN GSQFFITTVP 150
TPWLDGRHVV FGEVLEGYEV VEQIENVPKG PGDKPAETVK IVKSGQIKDE 200
STKGSHEEL 209
Length:209
Mass (Da):22,960
Last modified:July 5, 2005 - v1
Checksum:i4DF86787CAA2B426
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000005 Genomic DNA. Translation: EAL90022.1.
RefSeqiXP_752060.1. XM_746967.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00008354; CADAFUAP00008354; CADAFUAG00008354.
GeneIDi3509715.
KEGGiafm:AFUA_4G07650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000005 Genomic DNA. Translation: EAL90022.1 .
RefSeqi XP_752060.1. XM_746967.1.

3D structure databases

ProteinModelPortali Q4WP12.
SMRi Q4WP12. Positions 30-197.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00008354.

Proteomic databases

PRIDEi Q4WP12.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00008354 ; CADAFUAP00008354 ; CADAFUAG00008354 .
GeneIDi 3509715.
KEGGi afm:AFUA_4G07650.

Phylogenomic databases

eggNOGi COG0652.
HOGENOMi HOG000065981.
KOi K03768.
OMAi PSVANDK.
OrthoDBi EOG757D7G.

Family and domain databases

Gene3Di 2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSi PR00153. CSAPPISMRASE.
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPPIB_ASPFU
AccessioniPrimary (citable) accession number: Q4WP12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: July 5, 2005
Last modified: June 11, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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