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Q26548

- PPIE_SCHMA

UniProt

Q26548 - PPIE_SCHMA

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Protein

Peptidyl-prolyl cis-trans isomerase E

Gene
N/A
Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. peptide binding Source: UniProtKB-KW
  3. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW
  4. RNA binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin, RNA-binding

Enzyme and pathway databases

BRENDAi5.2.1.8. 5608.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase E (EC:5.2.1.8)
Short name:
PPIase E
Alternative name(s):
Cyclophilin E
Rotamase E
OrganismiSchistosoma mansoni (Blood fluke)
Taxonomic identifieri6183 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 273273Peptidyl-prolyl cis-trans isomerase EPRO_0000064161Add
BLAST

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi113 – 1208Combined sources
Beta strandi123 – 13210Combined sources
Turni134 – 1363Combined sources
Helixi138 – 14912Combined sources
Turni150 – 1523Combined sources
Beta strandi160 – 1656Combined sources
Turni166 – 1683Combined sources
Beta strandi169 – 1724Combined sources
Turni175 – 1773Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi205 – 2084Combined sources
Beta strandi220 – 2256Combined sources
Helixi228 – 2303Combined sources
Turni231 – 2333Combined sources
Beta strandi236 – 2427Combined sources
Helixi244 – 2496Combined sources
Helixi250 – 2534Combined sources
Beta strandi264 – 2729Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CK1X-ray1.80A102-273[»]
2CMTX-ray1.50A102-273[»]
ProteinModelPortaliQ26548.
SMRiQ26548. Positions 1-53, 110-273.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ26548.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4848RRMPROSITE-ProRule annotationAdd
BLAST
Domaini115 – 271157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR016304. Cyclophilin-type_PPIase_E.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001475. PPI_cyclophilin_E. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q26548-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPMDYQTEKH RGFAFVEFEE VEDAMSAIDN MNESEIFGRT IRVNVARPVR
60 70 80 90 100
IREGWSRPVW SDENWLKKYG SAPLEGRKLD EPDIVNPSDT SENVEDLSDE
110 120 130 140 150
EMRTKKQKRN LPRVFFDIRI GNGDAGRIVM ELRSDIVPRT AENFRALCTG
160 170 180 190 200
ERGFGYHNCC FHRVIPQFMC QGGDFVKGDG TGGKSIYGRK FDDENFQLRH
210 220 230 240 250
EGFGVLSMAN SGPNTNGSQF FICTTKCDWL DGKHVVFGRV VDGQNVVKKM
260 270
ESVGSKSGKV KEPVIISRCG ELI
Length:273
Mass (Da):30,905
Last modified:January 1, 1998 - v2
Checksum:iA3CE71D40CB0CDD1
GO

Sequence cautioni

The sequence AAC47317.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961F → I in AAC47317. (PubMed:8898338)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30265 mRNA. Translation: AAC47543.1.
U50388 mRNA. Translation: AAC47317.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30265 mRNA. Translation: AAC47543.1 .
U50388 mRNA. Translation: AAC47317.1 . Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CK1 X-ray 1.80 A 102-273 [» ]
2CMT X-ray 1.50 A 102-273 [» ]
ProteinModelPortali Q26548.
SMRi Q26548. Positions 1-53, 110-273.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 5.2.1.8. 5608.

Miscellaneous databases

EvolutionaryTracei Q26548.

Family and domain databases

Gene3Di 2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR016304. Cyclophilin-type_PPIase_E.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001475. PPI_cyclophilin_E. 1 hit.
PRINTSi PR00153. CSAPPISMRASE.
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "RNA trans-splicing in flatworms. Analysis of trans-spliced mRNAs and genes in the human parasite, Schistosoma mansoni."
    Davis R.E., Hardwick C., Tavernier P., Hodgson S., Singh H.
    J. Biol. Chem. 270:21813-21819(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 57-273.

Entry informationi

Entry nameiPPIE_SCHMA
AccessioniPrimary (citable) accession number: Q26548
Secondary accession number(s): Q26558
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3