ID A0A3B3SAX0_9TELE Unreviewed; 335 AA.
AC A0A3B3SAX0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase E {ECO:0000256|ARBA:ARBA00021137};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
DE AltName: Full=Rotamase E {ECO:0000256|ARBA:ARBA00032204};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000027892.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000027892.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase E
CC subfamily. {ECO:0000256|ARBA:ARBA00009483}.
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 AlphaFoldDB; A0A3B3SAX0; -.
DR Ensembl; ENSPKIT00000008665.1; ENSPKIP00000027892.1; ENSPKIG00000009753.1.
DR GeneTree; ENSGT00940000165717; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd12347; RRM_PPIE; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR016304; PPIE.
DR InterPro; IPR034168; PPIE_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF001475; PPI_cyclophilin_E; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 6..84
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 144..304
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 109..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 37205 MW; F3D79FBB396854B3 CRC64;
MAATKRVLYV GGLAEEVDEK VLHAAFIPFG DITDIQIPLD YETEKHRGFA FIEFESAEDA
AAAIDNMNES ELFGRTIRVN IAKPMRIKEG SSRPVWSDDD WLKKFSGKTA EEAEGAEPAG
EDVSKETQEG EPPAKKGRTN PQVYMDIKIG NKPAGRLRFL LRADVVPMTA ENFRCLCTHE
KGFGYKGSSF HRIIPQFMCQ GGDFTNHNGT GGKSIYGRKF DDENFVLKHT GPGQLSMANS
GPNTNGSQFF LTCDKTDWLD GKHVVFGELM EGQEVLRAME VSGVTFPCGR HRPPPRSLVL
SLVQCFSSRP SGITRQSTFM LLPRQSTFML PPRQS
//
