ID   A0A1J8QWB6_9AGAM        Unreviewed;       136 AA.
AC   A0A1J8QWB6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, 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=AZE42_03008 {ECO:0000313|EMBL:OJA17673.1};
OS   Rhizopogon vesiculosus.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX   NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA17673.1, ECO:0000313|Proteomes:UP000183567};
RN   [1] {ECO:0000313|EMBL:OJA17673.1, ECO:0000313|Proteomes:UP000183567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA17673.1,
RC   ECO:0000313|Proteomes:UP000183567};
RA   Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA   Barry K., Grigoriev I.V., Spatafora J.W.;
RT   "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT   vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT   divergence of the mating type B locus.";
RL   Submitted (MAR-2016) 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   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC       subfamily. {ECO:0000256|ARBA:ARBA00010242}.
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:OJA17673.1}.
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DR   EMBL; LVVM01001878; OJA17673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J8QWB6; -.
DR   STRING; 180088.A0A1J8QWB6; -.
DR   OrthoDB; 5484803at2759; -.
DR   Proteomes; UP000183567; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR043323; PIN4.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   PANTHER; PTHR45995; -; 1.
DR   PANTHER; PTHR45995:SF1; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 4; 1.
DR   Pfam; PF13616; Rotamase_3; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183567};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014}.
FT   DOMAIN          41..134
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   136 AA;  14538 MW;  63606C6FF48AC9B6 CRC64;
     MGKKQSGSND KKAADKKGGG TKNVDKNDQS EGKGKGGLKA ATAVNVRHIL CEKHSKATEA
     LQKIQEGQRF DKVAQEYSED KAKAGGSLGW MVRGSMVGAF QDAAFALSPS TVDKPTLSPL
     VKTNFGYHII MVEGRR
//