ID   PPIL4_ASPOR             Reviewed;         461 AA.
AC   Q2U256;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 4;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   Name=cyp6; ORFNames=AO090038000594;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AP007169; BAE64359.1; -; Genomic_DNA.
DR   RefSeq; XP_001825492.1; XM_001825440.2.
DR   AlphaFoldDB; Q2U256; -.
DR   SMR; Q2U256; -.
DR   STRING; 510516.Q2U256; -.
DR   PRIDE; Q2U256; -.
DR   EnsemblFungi; BAE64359; BAE64359; AO090038000594.
DR   GeneID; 5997587; -.
DR   KEGG; aor:AO090038000594; -.
DR   VEuPathDB; FungiDB:AO090038000594; -.
DR   HOGENOM; CLU_018791_2_1_1; -.
DR   OMA; APKCCEN; -.
DR   Proteomes; UP000006564; Chromosome 6.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   CDD; cd01921; cyclophilin_RRM; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR035542; CRIP.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR035538; Cyclophilin_PPIL4.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR45843; PTHR45843; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Isomerase; Nucleus; Reference proteome; RNA-binding; Rotamase.
FT   CHAIN           1..461
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 4"
FT                   /id="PRO_0000232975"
FT   DOMAIN          1..171
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   DOMAIN          248..326
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          341..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          205..234
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        358..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  52913 MW;  91A136EAB7CED5A9 CRC64;
     MSVLLETSLG DIVIDLLVDE CPKACENFLK LCKVKYYNFS PVHSVQKNFT FQTGDPLGPD
     SSESDGGSSI WGLLEGPPKR TFSLEPPPKL KHDERGTVSM ATVPSPHDPD QRIAASQFIV
     TLGENLDYLD GKAVIFGKVV EGFDVLEKVN EAFIDDRGRP LKDIRIRHTV ILDDPFDDPP
     GLVAPAESPL PSKAQLATVR IADDEELDDN MDEESMEKLR REREARAQAL TLEMVGDLPF
     AEVKPPENVL FVCKLNPVTQ DEDLHLIFSR FGTILSCEVI RDKRTGDSLQ YAFIEFENQK
     DCEQAYFKMQ GVLIDDHRIH VDFSQSVSKL SESWRNATIS KRSGQRGGFG GVASLEKKRQ
     YRASDNAREK ENDYTLVFDK GDKAPRRRSY SRSPQRSSNR DRRASRSPRR DSYRDPYRRR
     PGDRSHSRSP ARGEYRDKDR GRYNHRERRR DDERYRERRR R