PPIA_NAEFO
ID PPIA_NAEFO Reviewed; 21 AA.
AC P84342;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin;
DE AltName: Full=NF008;
DE AltName: Full=Rotamase;
DE Flags: Fragment;
OS Naegleria fowleri (Brain eating amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5763;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 30214 / Nf 66;
RA Omura M., Endo T., Yagita K., Izumiyama S., Furushima-Shimogawara R.;
RL Submitted (JAN-2005) to UniProtKB.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000305}.
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; Evidence={ECO:0000305};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P84342; -.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR SUPFAM; SSF50891; SSF50891; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Isomerase; Rotamase.
FT CHAIN <1..>21
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000064128"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 21
SQ SEQUENCE 21 AA; 2300 MW; 06D7FBC81DD639B5 CRC64;
ENFKIKHTEP GLLSMANAGK N