ID A0A4T0GNX8_WALIC Unreviewed; 160 AA.
AC A0A4T0GNX8;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=E3P86_02407 {ECO:0000313|EMBL:TIB36785.1}, E3P90_01068
GN {ECO:0000313|EMBL:TIB14885.1};
OS Wallemia ichthyophaga.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=245174 {ECO:0000313|EMBL:TIB36785.1, ECO:0000313|Proteomes:UP000310689};
RN [1] {ECO:0000313|Proteomes:UP000306954, ECO:0000313|Proteomes:UP000310689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-6200 {ECO:0000313|EMBL:TIB36785.1,
RC ECO:0000313|Proteomes:UP000310689}, and EXF-8621
RC {ECO:0000313|EMBL:TIB14885.1, ECO:0000313|Proteomes:UP000306954};
RA Gostincar C.;
RT "Sequencing 23 genomes of Wallemia ichthyophaga.";
RL Submitted (MAR-2019) 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. PPIL1
CC subfamily. {ECO:0000256|ARBA:ARBA00038147}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TIB36785.1}.
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DR EMBL; SPOF01000009; TIB14885.1; -; Genomic_DNA.
DR EMBL; SPOI01000120; TIB36785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4T0GNX8; -.
DR EnsemblFungi; TIA74241; TIA74241; E3P91_01018.
DR OMA; ELYNDHA; -.
DR Proteomes; UP000306954; Unassembled WGS sequence.
DR Proteomes; UP000310689; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 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 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; PS00170; CSA_PPIASE_1; 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:UP000310689};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 1..155
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT BINDING 45..56
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 61..62
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 90..95
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 100..104
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 110
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
FT BINDING 116
FT /ligand="cyclosporin A"
FT /ligand_id="ChEBI:CHEBI:4031"
FT /evidence="ECO:0000256|PIRSR:PIRSR001467-1"
SQ SEQUENCE 160 AA; 17601 MW; A2D3AAA9E7BF4AAF CRC64;
MATVIQLKTS QGDIDLELYV NHAPKTCNNF SQLVQRGYYN GVAFHRIVQD FMIQGGDPTG
TGRGGTSVYG GKFEDEINPE LRFTGAGILA MANAGPNTNG SQFFITLSPT PYLDGKHTIF
GRVLRGMRVV QRMANVVVDK ADRPIEDVKI YNASIQQMIE
//