CYPH_ENCCU
ID CYPH_ENCCU Reviewed; 172 AA.
AC Q8SRE1;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin;
DE Short=CPH;
DE AltName: Full=Rotamase;
GN Name=CPR1; OrderedLocusNames=ECU08_0470;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of peptidyl-prolyl cis-trans isomerase from
RT Encephalitozoon cuniculi at 1.9 A resolution.";
RL Submitted (OCT-2009) to the PDB data bank.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. They catalyze the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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; AL590448; CAD26352.1; -; Genomic_DNA.
DR RefSeq; NP_597176.1; NM_001041785.1.
DR PDB; 3K2C; X-ray; 1.95 A; A/B/C/D=1-172.
DR PDBsum; 3K2C; -.
DR AlphaFoldDB; Q8SRE1; -.
DR SMR; Q8SRE1; -.
DR STRING; 284813.Q8SRE1; -.
DR PRIDE; Q8SRE1; -.
DR GeneID; 859598; -.
DR KEGG; ecu:ECU08_0470; -.
DR VEuPathDB; MicrosporidiaDB:ECU08_0470; -.
DR HOGENOM; CLU_012062_4_3_1; -.
DR InParanoid; Q8SRE1; -.
DR OMA; MRAPIVN; -.
DR OrthoDB; 1403619at2759; -.
DR EvolutionaryTrace; Q8SRE1; -.
DR Proteomes; UP000000819; Chromosome VIII.
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: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 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 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..172
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000383096"
FT DOMAIN 10..168
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:3K2C"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:3K2C"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:3K2C"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:3K2C"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3K2C"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3K2C"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3K2C"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3K2C"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3K2C"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3K2C"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3K2C"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3K2C"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3K2C"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:3K2C"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3K2C"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:3K2C"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3K2C"
SQ SEQUENCE 172 AA; 19047 MW; 89EA397E833BEF31 CRC64;
MAKEASGNVY FDVYANEESL GRIVMKLEDD IVPKTAKNFR TLCERPKGEG YKGSTFHRII
PGFMVQGGDY TAHNGTGGRS IYGEKFPDEN FELKHTKEGI LSMANCGAHT NGSQFFITLG
KTQWLDEKHV VFGEVVEGMD VVHKIAKYGS ESGQVKKGYR IEIRDCGVLG SN
