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Protein

Peptidyl-prolyl cis-trans isomerase E

Gene

cyp33

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 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. Combines RNA-binding and PPIase activities (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  • mRNA binding Source: FlyBase
  • nucleotide binding Source: InterPro
  • peptidyl-prolyl cis-trans isomerase activity Source: GO_Central

GO - Biological processi

  • mRNA splicing, via spliceosome Source: FlyBase
  • phagocytosis Source: FlyBase
  • protein folding Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-DME-6781823. Formation of TC-NER Pre-Incision Complex.
R-DME-6782135. Dual incision in TC-NER.
R-DME-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

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 33
Cyclophilin E
Rotamase E
Gene namesi
Name:cyp33
ORF Names:CG4886
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0028382. cyp33.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: FlyBase
  • nucleus Source: FlyBase
  • precatalytic spliceosome Source: FlyBase
  • Prp19 complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 300300Peptidyl-prolyl cis-trans isomerase EPRO_0000064159Add
BLAST

Proteomic databases

PaxDbiQ9V3G3.
PRIDEiQ9V3G3.

Expressioni

Gene expression databases

BgeeiQ9V3G3.
GenevisibleiQ9V3G3. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
trxP206592EBI-128445,EBI-591327

Protein-protein interaction databases

BioGridi62673. 1 interaction.
DIPiDIP-21959N.
IntActiQ9V3G3. 3 interactions.
MINTiMINT-1643160.
STRINGi7227.FBpp0086101.

Structurei

3D structure databases

ProteinModelPortaliQ9V3G3.
SMRiQ9V3G3. Positions 5-82, 139-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 8479RRMPROSITE-ProRule annotationAdd
BLAST
Domaini142 – 298157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi60 – 634Poly-Ala

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0111. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
InParanoidiQ9V3G3.
KOiK09564.
OMAiAFIEFEL.
OrthoDBiEOG79GT7W.
PhylomeDBiQ9V3G3.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR016304. Cyclophilin-type_PPIase_E.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001475. PPI_cyclophilin_E. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF50891. SSF50891. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9V3G3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNDKRTIYV GGLADEVTER LLNNAFIPFG DIADIQMPAD YESQRHRGFA
60 70 80 90 100
FIEYEQSEDA AAAIDNMNDS ELCGRTIRVN LAKPVRVKED SFKPIWADDD
110 120 130 140 150
WLQKHAGATL QPEGEPEAEK VETPSTGPAV IEKAEKRNPQ VFFDIRIGGN
160 170 180 190 200
DAGRIVMLLR ADVVPKTAEN FRQLCTHEQG YGYKGCSFHR VIPEFMCQGG
210 220 230 240 250
DFTNNNGTGG KSIYGKKFND ENFNLKHNSF GTLSMANSGA NTNGSQFFIC
260 270 280 290 300
TTKTDWLDNK HVVFGHVISG AEVVRKMERC GSKSGTPSQK IVIYSCGELK
Length:300
Mass (Da):33,276
Last modified:May 1, 2000 - v1
Checksum:iCEAC7156EE8632D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182826 mRNA. Translation: AAF01031.1.
AE013599 Genomic DNA. Translation: AAF57839.1.
AY061421 mRNA. Translation: AAL28969.1.
RefSeqiNP_523773.1. NM_079049.4.
UniGeneiDm.2854.

Genome annotation databases

EnsemblMetazoaiFBtr0086945; FBpp0086101; FBgn0028382.
GeneIDi36984.
KEGGidme:Dmel_CG4886.
UCSCiCG4886-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182826 mRNA. Translation: AAF01031.1.
AE013599 Genomic DNA. Translation: AAF57839.1.
AY061421 mRNA. Translation: AAL28969.1.
RefSeqiNP_523773.1. NM_079049.4.
UniGeneiDm.2854.

3D structure databases

ProteinModelPortaliQ9V3G3.
SMRiQ9V3G3. Positions 5-82, 139-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62673. 1 interaction.
DIPiDIP-21959N.
IntActiQ9V3G3. 3 interactions.
MINTiMINT-1643160.
STRINGi7227.FBpp0086101.

Proteomic databases

PaxDbiQ9V3G3.
PRIDEiQ9V3G3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086945; FBpp0086101; FBgn0028382.
GeneIDi36984.
KEGGidme:Dmel_CG4886.
UCSCiCG4886-RA. d. melanogaster.

Organism-specific databases

CTDi36984.
FlyBaseiFBgn0028382. cyp33.

Phylogenomic databases

eggNOGiKOG0111. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
InParanoidiQ9V3G3.
KOiK09564.
OMAiAFIEFEL.
OrthoDBiEOG79GT7W.
PhylomeDBiQ9V3G3.

Enzyme and pathway databases

ReactomeiR-DME-6781823. Formation of TC-NER Pre-Incision Complex.
R-DME-6782135. Dual incision in TC-NER.
R-DME-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Miscellaneous databases

GenomeRNAii36984.
PROiQ9V3G3.

Gene expression databases

BgeeiQ9V3G3.
GenevisibleiQ9V3G3. DM.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR016304. Cyclophilin-type_PPIase_E.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001475. PPI_cyclophilin_E. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF50891. SSF50891. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new family of cyclophilins with an RNA recognition motif that interact with members of the trx/MLL protein family in Drosophila and human cells."
    Anderson M., Fair K., Amero S., Nelson S., Harte P.J., Diaz M.O.
    Dev. Genes Evol. 212:107-113(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.

Entry informationi

Entry nameiPPIE_DROME
AccessioniPrimary (citable) accession number: Q9V3G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.