ID D8M5J6_BLAHO Unreviewed; 159 AA.
AC D8M5J6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN ORFNames=GSBLH_T00003225001 {ECO:0000313|EMBL:CBK23335.2};
OS Blastocystis hominis.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK23335.2};
RN [1] {ECO:0000313|EMBL:CBK23335.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK23335.2};
RA Wincker P.;
RT "Sequencing and annotation of the Blastocystis hominis genome.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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:0000256|RuleBase:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|RuleBase:RU363019}.
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DR EMBL; FN668661; CBK23335.2; -; Genomic_DNA.
DR RefSeq; XP_012897383.1; XM_013041929.1.
DR AlphaFoldDB; D8M5J6; -.
DR EnsemblProtists; CBK23335; CBK23335; GSBLH_T00003225001.
DR GeneID; 24920333; -.
DR InParanoid; D8M5J6; -.
DR OMA; PNYTQFG; -.
DR OrthoDB; 554597at2759; -.
DR Proteomes; UP000008312; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000008312};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 11..158
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT BINDING 48..59
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 64..65
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 93..98
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 103..107
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 113
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 119
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
SQ SEQUENCE 159 AA; 17849 MW; 848CDE993F6951BB CRC64;
MSKQVTHIQF ETSVGPFVLE LYYNHAPKTC ENFIGLVKKG FYNGIKFHRI IPNFMIQGGD
PTGTGRYSES IWGHPFEDEI TRTLRFTGAG ILAMANSGPN TNGCQFFITL APTPWLDGKH
TIFGRVSEGM KTINHLGRIP TDSNDRPLQD IKILRAYCL
//
