ID   PIN4_ASPFU              Reviewed;         129 AA.
AC   Q4WJM6;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase pin4;
DE            Short=PPIase pin4;
DE            EC=5.2.1.8;
DE   AltName: Full=Parvulin-14;
DE            Short=Par14;
GN   Name=pin4; ORFNames=AFUA_1G05450;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAHF01000007; EAL88256.1; -; Genomic_DNA.
DR   RefSeq; XP_750294.1; XM_745201.1.
DR   AlphaFoldDB; Q4WJM6; -.
DR   SMR; Q4WJM6; -.
DR   STRING; 746128.CADAFUBP00000570; -.
DR   PRIDE; Q4WJM6; -.
DR   EnsemblFungi; EAL88256; EAL88256; AFUA_1G05450.
DR   GeneID; 3507550; -.
DR   KEGG; afm:AFUA_1G05450; -.
DR   VEuPathDB; FungiDB:Afu1g05450; -.
DR   eggNOG; KOG3258; Eukaryota.
DR   HOGENOM; CLU_090028_2_0_1; -.
DR   InParanoid; Q4WJM6; -.
DR   OMA; AMSINVR; -.
DR   OrthoDB; 1548618at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
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; PTHR45995; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..129
FT                   /note="Peptidyl-prolyl cis-trans isomerase pin4"
FT                   /id="PRO_0000232932"
FT   DOMAIN          35..127
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   129 AA;  14004 MW;  3FAA718C1B443647 CRC64;
     MAPKNNAKGG DKKGKGKDAS EGDKGKGGGK GLKPATSINV RHILCEKFSK KEEALEKLRN
     GAKFDDVARE YSEDKARQGG SLGWKVRGSL NADFEKAAYE LEPSTTANPK YVEVKTGFGY
     HIIMVEGRK