ID A0A286QUQ1_AOTVO Unreviewed; 164 AA. AC A0A286QUQ1; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 28-MAR-2018, entry version 5. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Aotidae; 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 RT interactions with lentiviral capsids."; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. {ECO:0000256|RuleBase:RU363019}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). {ECO:0000256|RuleBase:RU363019, CC ECO:0000256|SAAS:SAAS00339244}. 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 PANTHER; PTHR11071; PTHR11071; 1. 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|PROSITE-ProRule:PRU00156, KW ECO:0000256|RuleBase:RU363019, ECO:0000256|SAAS:SAAS00495831}; KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00156, KW ECO:0000256|RuleBase:RU363019, ECO:0000256|SAAS:SAAS00495895}. FT DOMAIN 7 163 PPIase cyclophilin-type. FT {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 //