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Q2Y080 (Q2Y080_AOTAZ) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length164 AA.
Sequence statusFragment.
Protein existenceEvidence 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). SAAS SAAS020892

Sequence similarities

Belongs to the cyclophilin-type PPIase family. RuleBase RU004223

Contains PPIase cyclophilin-type domain. SAAS SAAS020892

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-924086,EBI-924086
TRIM5Q9C035-13EBI-924086,EBI-924230From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Experimental info

Non-terminal residue11 EMBL ABA53799.1

Sequences

Sequence LengthMass (Da)Tools
Q2Y080 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 67C8DCFFCDEC596A

FASTA16417,845
        10         20         30         40         50         60 
MVNPTVFFDI AVDGEPLGRV SFELFADKLP KTAENFRALS TGEKGFGYKG SCFHRIIPGF 

        70         80         90        100        110        120 
MCQGGDFTPH NGTGGKSIYG VKFDDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE 

       130        140        150        160 
WLDGKHVVFG KVKEGMNVVE AMERFGCRYG KTSKKITIAD CGQL 

« Hide

References

[1]"Evolution of cyclophilin A and TRIMCyp retrotransposition in New World primates."
Ribeiro I.P., Menezes A.N., Moreira M.A.M., Bonvicino C.R., Seuanez H.N., Soares M.A.
J. Virol. 79:14998-15003(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 04 EMBL ABA53799.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ098854 Genomic DNA. Translation: ABA53799.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ2Y080. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG001065.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ2Y080_AOTAZ
AccessionPrimary (citable) accession number: Q2Y080
Entry history
Integrated into UniProtKB/TrEMBL: December 20, 2005
Last sequence update: December 20, 2005
Last modified: June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)