ID   PPIE_HAECO              Reviewed;         324 AA.
AC   Q4G338;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase E {ECO:0000250|UniProtKB:Q9QZH3, ECO:0000303|PubMed:15830208};
DE            Short=PPIase E {ECO:0000250|UniProtKB:Q9QZH3};
DE            EC=5.2.1.8 {ECO:0000269|PubMed:15830208};
DE   AltName: Full=Cyclophiline 33 {ECO:0000250|UniProtKB:Q9QZH3};
DE            Short=HcCYP {ECO:0000303|PubMed:15830208};
DE   AltName: Full=Cyclophiline E {ECO:0000250|UniProtKB:Q9QZH3};
DE   AltName: Full=Rotamase E {ECO:0000250|UniProtKB:Q9QZH3};
OS   Haemonchus contortus (Barber pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Haemonchidae; Haemonchus.
OX   NCBI_TaxID=6289;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAW82658.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, RNA-BINDING, SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=15830208; DOI=10.1007/s00436-005-1329-3;
RA   Valle C., Troiani A.R., Lazzaretti P., Bouvier J., Cioli D., Klinkert M.Q.;
RT   "Molecular and biochemical characterization of a protein cyclophilin from
RT   the nematode Haemonchus contortus.";
RL   Parasitol. Res. 96:199-205(2005).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Combines RNA-binding and PPIase activities.
CC       {ECO:0000269|PubMed:15830208}.
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:0000269|PubMed:15830208};
CC   -!- ACTIVITY REGULATION: Inhibited by cyclosporin A.
CC       {ECO:0000269|PubMed:15830208}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15830208}.
CC   -!- DOMAIN: The N-terminal RRM domain binds to nucleic acids including
CC       single-stranded DNA and RNA homopolymers poly(A), poly(G) and poly(U),
CC       but not to poly(C) nor double-stranded DNA. Binds most strongly to G-
CC       rich RNA species. {ECO:0000269|PubMed:15830208}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase E
CC       subfamily. {ECO:0000255}.
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DR   EMBL; AY754868; AAW82658.1; -; mRNA.
DR   AlphaFoldDB; Q4G338; -.
DR   SMR; Q4G338; -.
DR   BRENDA; 5.2.1.8; 2523.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
DR   GO; GO:0042277; F:peptide binding; IDA:UniProtKB.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0018208; P:peptidyl-proline modification; IDA:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IC:UniProtKB.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR   CDD; cd12347; RRM_PPIE; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 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   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; SSF50891; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Nucleus; RNA-binding; Rotamase.
FT   CHAIN           1..324
FT                   /note="Peptidyl-prolyl cis-trans isomerase E"
FT                   /id="PRO_0000423621"
FT   DOMAIN          12..90
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          137..293
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          291..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   324 AA;  35631 MW;  A9010A5BCF9F0D3B CRC64;
     MAASNFPHNK KRTLYVGGFG EEVTEKVLMA AFITFGDIVA ISIPMDYETG KHRGFGFVEF
     ELAEDAAAAI DNMNESELFG RTIRCNFARP PKATERSSRP VWADDEWLKR YGKGSGIADA
     KESNGSASTA KGLPRVYLGV KIGIRYIGRI VIELRSDVVP RTAENFRCLC TGEKGFGYEG
     SSFHRIIPKF MLQGGDFTKG DGTGGKSIYG PKFEDENFKL KHLMPGTVSM ANCGPNTNGS
     QFFICAEKTD WLDGKHVVFG HVVEGMNVVR QVEQQGTPSG KPQMVVKIVE CGELDPVPQT
     EPQENEENSD PQTPMDVEPQ KETA