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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

CYP11

Organism
Leishmania major
Status
Unreviewed-Annotation score: Annotation score: 2 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.UniRule annotation

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).UniRule annotationSAAS annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, RotamaseUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomeraseUniRule annotation (EC:5.2.1.8UniRule annotationImported)
Gene namesi
Name:CYP11Imported
ORF Names:LMJF_23_0050Imported
OrganismiLeishmania majorImported
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
ProteomesiUP000000542 Componenti: Chromosome 23

Interactioni

Protein-protein interaction databases

STRINGi5664.LmjF.23.0050.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HQJX-ray2.00A22-199[»]
ProteinModelPortaliQ4QBH1.
SMRiQ4QBH1. Positions 22-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4QBH1.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.UniRule annotation
Contains 1 PPIase cyclophilin-type domain.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000065980.
InParanoidiQ4QBH1.
KOiK01802.
OMAiLGCLSMA.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4QBH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRTSVPPKV GQRPGIGVEK TTNPKVFFDI SIDNKAAGRI VMELYADTVP
60 70 80 90 100
KTAENFRALC TGEKGKGRSG KPLHYKSSVF HRVIPNFMIQ GGDFTRGNGT
110 120 130 140 150
GGESIYGTTF RDESFSGKAG RHTGLGCLSM ANAGPNTNGS QFFICTAATP
160 170 180 190 200
WLDGKHVVFG RVIDGLDVVK KVERLGSSSG KTRSRIVVSD CGEVAADKSK
210 220 230 240 250
GQRPPQQQHQ PAKASADMKR AADKKAVAEK LLASSPAAEG QKALSAKKET
260 270 280 290
PPQVAAPSEA KKRMRAVDEE ETRLARLREK KAKLAALRSS AAGNE
Length:295
Mass (Da):31,497
Last modified:July 19, 2005 - v1
Checksum:i69AAC0FBD9533143
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796419 Genomic DNA. Translation: CAJ03831.1.
RefSeqiXP_001683327.1. XM_001683275.1.

Genome annotation databases

EnsemblProtistsiLmjF.23.0050:mRNA; LmjF.23.0050:pep; LmjF.23.0050.
GeneIDi5651954.
KEGGilma:LMJF_23_0050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796419 Genomic DNA. Translation: CAJ03831.1.
RefSeqiXP_001683327.1. XM_001683275.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HQJX-ray2.00A22-199[»]
ProteinModelPortaliQ4QBH1.
SMRiQ4QBH1. Positions 22-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5664.LmjF.23.0050.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiLmjF.23.0050:mRNA; LmjF.23.0050:pep; LmjF.23.0050.
GeneIDi5651954.
KEGGilma:LMJF_23_0050.

Phylogenomic databases

HOGENOMiHOG000065980.
InParanoidiQ4QBH1.
KOiK01802.
OMAiLGCLSMA.

Miscellaneous databases

EvolutionaryTraceiQ4QBH1.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of the kinetoplastid parasite, Leishmania major."
    Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G.
    , Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B., Myler P.J.
    Science 309:436-442(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MHOM/IL/81/FriedlinImported.
  2. "Cyclophilin from Leishmania major."
    Arakaki T.L., Merritt E.A.
    Submitted (JUL-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 22-199.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FriedlinImported.

Entry informationi

Entry nameiQ4QBH1_LEIMA
AccessioniPrimary (citable) accession number: Q4QBH1
Entry historyi
Integrated into UniProtKB/TrEMBL: July 19, 2005
Last sequence update: July 19, 2005
Last modified: July 22, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.