ID A0A0C3CAU4_PILCF Unreviewed; 116 AA.
AC A0A0C3CAU4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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};
DE Flags: Fragment;
GN ORFNames=PILCRDRAFT_46441 {ECO:0000313|EMBL:KIM86822.1};
OS Piloderma croceum (strain F 1598).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Piloderma.
OX NCBI_TaxID=765440 {ECO:0000313|EMBL:KIM86822.1, ECO:0000313|Proteomes:UP000054166};
RN [1] {ECO:0000313|EMBL:KIM86822.1, ECO:0000313|Proteomes:UP000054166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F 1598 {ECO:0000313|EMBL:KIM86822.1,
RC ECO:0000313|Proteomes:UP000054166};
RG DOE Joint Genome Institute;
RA Kuo A., Tarkka M., Buscot F., Kohler A., Nagy L.G., Floudas D.,
RA Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F 1598 {ECO:0000313|Proteomes:UP000054166};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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|ARBA:ARBA00000971,
CC ECO:0000256|RuleBase:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|RuleBase:RU363019}.
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DR EMBL; KN832981; KIM86822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3CAU4; -.
DR STRING; 765440.A0A0C3CAU4; -.
DR HOGENOM; CLU_012062_4_5_1; -.
DR InParanoid; A0A0C3CAU4; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000054166; 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; 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; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000054166};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 1..116
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIM86822.1"
FT NON_TER 116
FT /evidence="ECO:0000313|EMBL:KIM86822.1"
SQ SEQUENCE 116 AA; 13118 MW; DE9D96448A891958 CRC64;
VLFRLYDEVV PITANNFWML VISQQGYGYH GTVFSHVIPE FIIQAGDCDK GVGGGSRSIY
GSASKVFFFL DKNFKMKHWV KSLLSMVNFS NASQFLIHMN ANRFLDRSNV VFGQAI
//
