ID A0A286QUQ1_AOTVO Unreviewed; 164 AA. AC A0A286QUQ1; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 12-AUG-2020, entry version 11. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019}; DE Short=PPIase {ECO:0000256|RuleBase:RU363019}; DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019}; OS Aotus vociferans (Spix's owl monkey) (Noisy night monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae; OC Aotus. OX NCBI_TaxID=57176 {ECO:0000313|EMBL:ASR87918.1}; RN [1] {ECO:0000313|EMBL:ASR87918.1} RP NUCLEOTIDE SEQUENCE. RA Meyerson N.R., Sawyer S.L.; RT "The cyclophilin domain of RanBP2 exhibits species-specific interactions RT with lentiviral capsids."; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the CC cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. {ECO:0000256|RuleBase:RU363019}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-peptidylproline (omega=180) = [protein]- CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, CC ChEBI:CHEBI:83834; EC=5.2.1.8; CC Evidence={ECO:0000256|ARBA:ARBA00000971, CC ECO:0000256|RuleBase:RU363019}; CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CC {ECO:0000256|RuleBase:RU363019}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KX774456; ASR87918.1; -; mRNA. DR SMR; A0A286QUQ1; -. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 2.40.100.10; -; 1. DR InterPro; IPR029000; Cyclophilin-like_dom_sf. DR InterPro; IPR024936; Cyclophilin-type_PPIase. DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS. DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom. DR Pfam; PF00160; Pro_isomerase; 1. DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SUPFAM; SSF50891; SSF50891; 1. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. PE 2: Evidence at transcript level; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019}; KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}. FT DOMAIN 7..163 FT /note="PPIase cyclophilin-type" FT /evidence="ECO:0000259|PROSITE:PS50072" SQ SEQUENCE 164 AA; 17897 MW; 120F137484EF44A5 CRC64; MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFDDENFIL KHTGPGILSM ANAGPNTNGS QFFICTVKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIAD CGQL //