Q2Y080 (Q2Y080_AOTAZ) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Recommended name: Peptidyl-prolyl cis-trans isomerase RuleBase RU000493 EC=5.2.1.8 RuleBase RU000493
Organism	Aotus azarae (Southern owl monkey) (Aotus azarai) EMBL ABA53799.1
Taxonomic identifier	30591 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Platyrrhini › Aotidae › Aotus

Protein attributes

Sequence length	164 AA.
Sequence status	Fragment.
Protein existence	Evidence 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). RuleBase RU000493 SAAS SAAS020892
Sequence similarities	Belongs to the cyclophilin-type PPIase family. RuleBase RU004223 Contains 1 PPIase cyclophilin-type domain. RuleBase RU003420 SAAS SAAS020892

Ontologies

Keywords
Molecular function	Isomerase Rotamase SAAS SAAS020892 RuleBase RU003420
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-924086,EBI-924086
TRIM5	Q9C035-1	3	EBI-924086,EBI-924230	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Experimental info
	Non-terminal residue	1	1	EMBL ABA53799.1

Sequences

	Sequence		Length	Mass (Da)
	Q2Y080 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 67C8DCFFCDEC596A	FASTA	164	17,845
	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

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
ModBase	Search...
Protein-protein interaction databases
IntAct	Q2Y080. 2 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG001065.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PIRSF	PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q2Y080_AOTAZ

Accession

Primary (citable) accession number: Q2Y080

Entry history

Integrated into UniProtKB/TrEMBL:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	March 6, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)