PPIL4_NEUCR
ID PPIL4_NEUCR Reviewed; 494 AA.
AC Q871A4; Q7RZ18;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=cyp-6; ORFNames=B8G12.450, NCU07179;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; BX294027; CAD71104.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA28168.2; -; Genomic_DNA.
DR RefSeq; XP_957404.2; XM_952311.3.
DR AlphaFoldDB; Q871A4; -.
DR SMR; Q871A4; -.
DR STRING; 5141.EFNCRP00000007196; -.
DR PRIDE; Q871A4; -.
DR EnsemblFungi; EAA28168; EAA28168; NCU10166.
DR GeneID; 3873579; -.
DR KEGG; ncr:NCU10166; -.
DR VEuPathDB; FungiDB:NCU10166; -.
DR HOGENOM; CLU_018791_2_1_1; -.
DR InParanoid; Q871A4; -.
DR OMA; APKCCEN; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:1901407; P:regulation of phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
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..494
FT /note="Peptidyl-prolyl cis-trans isomerase-like 4"
FT /id="PRO_0000232979"
FT DOMAIN 1..172
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT DOMAIN 253..331
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 176..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 206..240
FT /evidence="ECO:0000255"
SQ SEQUENCE 494 AA; 56500 MW; 425EF8837804DC56 CRC64;
MSVLLETSAG DIVIDLLVDY APKMCENFLK LCKVKYYNFS PIHSIQKSFS FQTGDPLGPL
SSESDGGQSI WGLLSGDPSE KTFPALFHPK LKHLERGTVS MATVPHPSDP DTRLAGSQFI
VTLGDNTDYL DGKAAIFGKV VEGFDVLEKI NDAIVDERGH PLVDIRIKHT VILDDPYPDP
AGMREPSASP PPSKAQLATV RITEGEELLD VEASEEAAAE AERRRREREA AAQALTLEMM
GDLPFAEVKP PENVLFVCKL NPVTTDEDLE LIFSRFGKIL SCEVIRDQKT GDSLQYAFIE
FEDKKSCEEA YSKMDSVLID DRRIHVDFSQ SVSKLSDVWR SETNSKRKSA ARRGGGGWGG
VDELEKWRKY RDEDVEWRND DSYQMVHGVE DLKGRHDGDK PPVRDSRPDV GGGRDRSTSR
RSRSPRRDRD RRDDRDNRRG PRDADRRRDD RDLDRRDRRG DRSRDRYRDR DYNDRDHRRG
RDRDNRGRDD YRRR
