PPIL4_ASPFU
ID PPIL4_ASPFU Reviewed; 459 AA.
AC Q4WAQ9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=AFUA_7G02170;
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 -!- 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; AAHF01000015; EAL84677.1; -; Genomic_DNA.
DR RefSeq; XP_746715.1; XM_741622.1.
DR AlphaFoldDB; Q4WAQ9; -.
DR SMR; Q4WAQ9; -.
DR STRING; 746128.CADAFUBP00008626; -.
DR EnsemblFungi; EAL84677; EAL84677; AFUA_7G02170.
DR GeneID; 3504238; -.
DR KEGG; afm:AFUA_7G02170; -.
DR VEuPathDB; FungiDB:Afu7g02170; -.
DR eggNOG; KOG0415; Eukaryota.
DR HOGENOM; CLU_018791_2_1_1; -.
DR InParanoid; Q4WAQ9; -.
DR OMA; APKCCEN; -.
DR OrthoDB; 1436035at2759; -.
DR Proteomes; UP000002530; Chromosome 7.
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 Isomerase; Nucleus; Reference proteome; RNA-binding; Rotamase.
FT CHAIN 1..459
FT /note="Peptidyl-prolyl cis-trans isomerase-like 4"
FT /id="PRO_0000232974"
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 376..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..413
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 52899 MW; A298EA6F02391133 CRC64;
MSVLLETSLG DIVIDLLVDE SPKACENFLK LCKVKYYNFS PVHSVQKNFT FQTGDPLGPD
SPESDGGSSI WGLLEGPVKR TFSLKLSPKL KHTERGTVSM ATVPSSHDPD ERLAASQFIV
TLEDNLDYLD GKAAIFGKVV EGFDVLEKIN GAFIDDQGRP LKDIRIRHTV ILDDPYDDPP
GLVVPAESPL PSKAQLATVR IADDEELDDN MDEEAMEKLR REREARAQAL TLEMVGDLPF
AEVKPPENVL FVCKLNPVTQ DEDLQLIFSR FGPILSCEVI RDKRTGDSLQ YAFIEFENQK
DCEQAYFKMQ GVLIDDHRIH VDFSQSVSKL SESWRNATIS KRSQRGGFGG VAELEKKRQY
RATDNVREQD AYGMVFDKGE ARRRPVSRER RYSRSPKRSS RRDSRSPKRG LHRNRYRDRS
DSRSPRREDS YRDRNRERSY NDERRDRRDD DRYRERRRR
