ID   PPIL4_RHIO9             Reviewed;         446 AA.
AC   P0C1I6; I1C1D9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=cyp13; ORFNames=RO3G_06974;
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
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; CH476736; EIE82269.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C1I6; -.
DR   SMR; P0C1I6; -.
DR   STRING; 936053.P0C1I6; -.
DR   PRIDE; P0C1I6; -.
DR   EnsemblFungi; EIE82269; EIE82269; RO3G_06974.
DR   VEuPathDB; FungiDB:RO3G_06974; -.
DR   eggNOG; KOG0415; Eukaryota.
DR   InParanoid; P0C1I6; -.
DR   OMA; APKCCEN; -.
DR   OrthoDB; 1436035at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
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   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   Isomerase; Nucleus; Reference proteome; RNA-binding; Rotamase.
FT   CHAIN           1..446
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 4"
FT                   /id="PRO_0000244719"
FT   DOMAIN          1..165
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   DOMAIN          242..320
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          375..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  51712 MW;  41EF2BE6EE151974 CRC64;
     MSVLIETSLG DIVIDLYTEE CPKTTLNFLK LCKIKYYNFA PFFNVQKDFM AQTGDPTGKG
     DQGQSVYGIL GGSRYFPAEI HPTLKHVRRG MVSMAVAADA SIETGGVSGS QFFITLGENL
     DYLDGKYTLF GEIAEGFDVL DKINEAYCDE QGRPFRDIRI KHTVVLDDPF PDPDGLVIPD
     ESPLPTKEQL ESMRIGEDED LEEMGDPEEL EKRVRAREAK AHALTLEMIG DLPFAEVKPP
     ENVLFVCKLN PVTRDEDLEM IFSRFGLIHS CEIIRDRQTG DSLSYAFVEF ENKEDAEEAY
     FKMQSVLIDD RRIHVDFSQS VSKLHKDWIA KRTGAGKESM GGFDNLTKRT RYREEGENND
     KRDYDLVFDK GDYKRKRDED SSRDRRRRDG SRDRYSSRRD DERSSRRRDD ERSSRRRDDS
     REKYRRRNDS RDRHSSRRDD DSKRNR