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Database: UniProt
Entry: A0A225B0Y7_9EURO
LinkDB: A0A225B0Y7_9EURO
Original site: A0A225B0Y7_9EURO 
ID   A0A225B0Y7_9EURO        Unreviewed;       190 AA.
AC   A0A225B0Y7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363014};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014};
GN   ORFNames=UA08_03650 {ECO:0000313|EMBL:OKL61639.1};
OS   Talaromyces atroroseus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Trachyspermi.
OX   NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL61639.1, ECO:0000313|Proteomes:UP000214365};
RN   [1] {ECO:0000313|EMBL:OKL61639.1, ECO:0000313|Proteomes:UP000214365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL61639.1,
RC   ECO:0000313|Proteomes:UP000214365};
RA   Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA   Mortensen U.H., Thrane U.;
RT   "Talaromyces atroroseus IBT 11181 draft genome.";
RL   Submitted (JUN-2015) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971,
CC         ECO:0000256|RuleBase:RU363014};
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:OKL61639.1}.
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DR   EMBL; LFMY01000004; OKL61639.1; -; Genomic_DNA.
DR   RefSeq; XP_020121760.1; XM_020265973.1.
DR   AlphaFoldDB; A0A225B0Y7; -.
DR   STRING; 1441469.A0A225B0Y7; -.
DR   GeneID; 31003405; -.
DR   OrthoDB; 417859at2759; -.
DR   Proteomes; UP000214365; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR10657; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR10657:SF4; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   Pfam; PF00639; Rotamase; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214365};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..39
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          65..176
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   190 AA;  21442 MW;  9A0152F838745422 CRC64;
     MSDITGLPDG WEVRHSNSKN LPYYFNASTK ESRWEPPSGT DPEKLKAYMA TYHSGPSGIA
     GLPAEGKIRC AHLLVKHRDS RRPSSWRENN ITRSKEEAIE ILRGHEQRIK SGEIRLADLA
     VSESDCSSAR KKGDLGFFGR GEMQKEFEDA AFALKPGEIS SIVESPSGVH LIERYVDRPE
     DWYHLYPPQN
//
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