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Database: UniProt
Entry: A0A4T0GNX8_WALIC
LinkDB: A0A4T0GNX8_WALIC
Original site: A0A4T0GNX8_WALIC 
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
//
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