PPIE_SCHMA
ID PPIE_SCHMA Reviewed; 273 AA.
AC Q26548; Q26558;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase E;
DE Short=PPIase E;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin E;
DE AltName: Full=Rotamase E;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7665603; DOI=10.1074/jbc.270.37.21813;
RA Davis R.E., Hardwick C., Tavernier P., Hodgson S., Singh H.;
RT "RNA trans-splicing in flatworms. Analysis of trans-spliced mRNAs and genes
RT in the human parasite, Schistosoma mansoni.";
RL J. Biol. Chem. 270:21813-21819(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 57-273.
RX PubMed=8898338; DOI=10.1016/0166-6851(96)02692-8;
RA Klinkert M.-Q., Bugli F., Cruz J., Engels B., Cioli D.;
RT "Sequence conservation of schistosome cyclophilins.";
RL Mol. Biochem. Parasitol. 81:239-242(1996).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
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 -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase E
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC47317.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U30265; AAC47543.1; -; mRNA.
DR EMBL; U50388; AAC47317.1; ALT_INIT; mRNA.
DR PDB; 2CK1; X-ray; 1.80 A; A=102-273.
DR PDB; 2CMT; X-ray; 1.50 A; A=102-273.
DR PDBsum; 2CK1; -.
DR PDBsum; 2CMT; -.
DR AlphaFoldDB; Q26548; -.
DR SMR; Q26548; -.
DR STRING; 6183.Smp_094810.1; -.
DR EnsemblMetazoa; Smp_094810.1; Smp_094810.1; Smp_094810.
DR WBParaSite; Smp_094810.1; Smp_094810.1; Smp_094810.
DR eggNOG; KOG0111; Eukaryota.
DR HOGENOM; CLU_012062_27_0_1; -.
DR BRENDA; 5.2.1.8; 5608.
DR EvolutionaryTrace; Q26548; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
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; 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 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 3D-structure; Cytoplasm; Isomerase; Reference proteome; RNA-binding;
KW Rotamase.
FT CHAIN 1..273
FT /note="Peptidyl-prolyl cis-trans isomerase E"
FT /id="PRO_0000064161"
FT DOMAIN 1..48
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 115..271
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 77..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 196
FT /note="F -> I (in Ref. 2; AAC47317)"
FT /evidence="ECO:0000305"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:2CMT"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:2CMT"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2CMT"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:2CMT"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2CMT"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2CMT"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2CMT"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2CMT"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:2CMT"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2CMT"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:2CMT"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:2CMT"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2CMT"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:2CMT"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:2CMT"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:2CMT"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:2CMT"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:2CMT"
SQ SEQUENCE 273 AA; 30905 MW; A3CE71D40CB0CDD1 CRC64;
MPMDYQTEKH RGFAFVEFEE VEDAMSAIDN MNESEIFGRT IRVNVARPVR IREGWSRPVW
SDENWLKKYG SAPLEGRKLD EPDIVNPSDT SENVEDLSDE EMRTKKQKRN LPRVFFDIRI
GNGDAGRIVM ELRSDIVPRT AENFRALCTG ERGFGYHNCC FHRVIPQFMC QGGDFVKGDG
TGGKSIYGRK FDDENFQLRH EGFGVLSMAN SGPNTNGSQF FICTTKCDWL DGKHVVFGRV
VDGQNVVKKM ESVGSKSGKV KEPVIISRCG ELI
