ID A0A0R3S3X6_9BILA Unreviewed; 306 AA.
AC A0A0R3S3X6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase E {ECO:0000256|ARBA:ARBA00021137, ECO:0000256|PIRNR:PIRNR001475};
DE Short=PPIase E {ECO:0000256|PIRNR:PIRNR001475};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PIRNR:PIRNR001475};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000948001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000948001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- FUNCTION: Catalyzes the cis-trans isomerization of proline imidic
CC peptide bonds in proteins. {ECO:0000256|PIRNR:PIRNR001475}.
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|PIRNR:PIRNR001475};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase E
CC subfamily. {ECO:0000256|ARBA:ARBA00009483,
CC ECO:0000256|PIRNR:PIRNR001475}.
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DR AlphaFoldDB; A0A0R3S3X6; -.
DR STRING; 1147741.A0A0R3S3X6; -.
DR WBParaSite; EEL_0000948001-mRNA-1; EEL_0000948001-mRNA-1; EEL_0000948001.
DR Proteomes; UP000050640; 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, ECO:0000256|PIRNR:PIRNR001475};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PIRNR:PIRNR001475}.
FT DOMAIN 13..91
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 146..295
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 306 AA; 34008 MW; 969AEB876C8A0F1B CRC64;
MSLATNFPHN KKRTLYVGGF GEEVNEKVLQ AGFVPFGEIV SISIPLDYET GKHRGFGFVE
YELAEDAAAA IDNMNDSELF GRTIRCNFAR PPKANERSQR PVWADDEWLK TYGTGEGTSK
EFDKGSDAIS EESAIGPVRL SLPRVYLGIR IGIRYIGRIV IELRSDVVPK TAENFRQLCT
GEKGFGYEGS HFHRIIPRFM IQAGDFTKGD GTGGKSIYGS KFADENFKLK HTMAGVVSMA
NCGPDTNGSQ FFICTEKTDW LDNKHVVFGH VVEGMNIVKQ VEQQGSKSGK PMMQVCSFFQ
LIIKCD
//
