ID B0EQC0_ENTDS Unreviewed; 252 AA.
AC B0EQC0;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=EDI_243150 {ECO:0000313|EMBL:EDR23275.1};
OS Entamoeba dispar (strain ATCC PRA-260 / SAW760).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370354 {ECO:0000313|Proteomes:UP000008076};
RN [1] {ECO:0000313|Proteomes:UP000008076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PRA-260 / SAW760 {ECO:0000313|Proteomes:UP000008076};
RA Lorenzi H., Inman J., Schobel S., Amedeo P., Caler E.;
RT "Annotation of Entamoeba dispar SAW760.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|PROSITE-
CC ProRule:PRU00277};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577}.
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DR EMBL; DS550368; EDR23275.1; -; Genomic_DNA.
DR RefSeq; XP_001740314.1; XM_001740262.1.
DR AlphaFoldDB; B0EQC0; -.
DR EnsemblProtists; EDR23275; EDR23275; EDI_243150.
DR GeneID; 5885483; -.
DR KEGG; edi:EDI_243150; -.
DR VEuPathDB; AmoebaDB:EDI_243150; -.
DR eggNOG; KOG0543; Eukaryota.
DR OMA; GCLIKRI; -.
DR OrthoDB; 11153at2759; -.
DR Proteomes; UP000008076; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46512; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR46512:SF1; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:EDR23275.1}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 16..99
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REPEAT 199..232
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 252 AA; 29486 MW; F5C21394D44B5064 CRC64;
MVEIQCIEES KGQVISDRME IKIQYSIQSN LTKEENEIQF VIGEGSVLPF IENFVINKRI
GEKYQIITKG KEIFGEEGFG ERIKSEEEVK IIIKILEGKE IKKPKAFEEC IKEIIKTKEK
GKEKITKKEY KEAIKIYQEC AAELHNLIDD INYQKYNEEI KKQLLLIHSN MALCWLKLEN
WNETKQQSEE VLKFDPVNVK ALYRIGVVLN KKEQYSLALN YLKKAMTLAE QDGLIRKEYN
FAANNINKIT KK
//
