ID A0A4S4KZZ9_9AGAM Unreviewed; 334 AA.
AC A0A4S4KZZ9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=EW145_g5437 {ECO:0000313|EMBL:THH04559.1};
OS Phellinidium pouzarii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Hymenochaetaceae; Phellinidium.
OX NCBI_TaxID=167371 {ECO:0000313|EMBL:THH04559.1, ECO:0000313|Proteomes:UP000308199};
RN [1] {ECO:0000313|EMBL:THH04559.1, ECO:0000313|Proteomes:UP000308199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 108285 {ECO:0000313|EMBL:THH04559.1,
RC ECO:0000313|Proteomes:UP000308199};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Phellinidium pouzarii.";
RL Submitted (FEB-2019) 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 -!- 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:THH04559.1}.
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DR EMBL; SGPK01000332; THH04559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S4KZZ9; -.
DR Proteomes; UP000308199; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 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 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000308199};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..334
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020392932"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..201
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 205..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 36720 MW; 19007A14207E87C3 CRC64;
MYAKLFFSLF VVSLAALLSA RSAEAAKGPR ITHKVYFDIQ HGEEKLGRIT MGLYGGTVPK
TVENFRALAT GVRKDGTPLE EGMGYKGSKF HRVIKDFMIQ GGDFTKGDGT GGKSIYGNKF
ADENFKLKHT GPGTLSMANA GKDTNGSQFF ICTVITSWLD GRHVVFGKVI DGMDIVHKIE
DFPKGRNDRP VEDVVIIDSG ELEINEVDED GNQDDELDVP TTSSEVEAKT KTDIKTEKVQ
ETSESSTVPV DADVPAPTST ETKGTPVDED VSKEDVYHVS TSPLRILFVG FILLIIPATL
FVYCGGLQWT RRMFKRSSLS KGQYKRVGDQ DLEK
//
