CWC27_ASPFU
ID CWC27_ASPFU Reviewed; 559 AA.
AC Q4WE62;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Peptidyl-prolyl isomerase cwc27;
DE Short=PPIase cwc27;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase cwc27;
GN Name=cwc27; ORFNames=AFUA_5G01890;
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. Involved in pre-mRNA splicing (By similarity).
CC {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 -!- SUBUNIT: Associated with the spliceosome. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27
CC subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000011; EAL86115.1; -; Genomic_DNA.
DR RefSeq; XP_748153.1; XM_743060.1.
DR AlphaFoldDB; Q4WE62; -.
DR SMR; Q4WE62; -.
DR STRING; 746128.CADAFUBP00004933; -.
DR EnsemblFungi; EAL86115; EAL86115; AFUA_5G01890.
DR GeneID; 3505738; -.
DR KEGG; afm:AFUA_5G01890; -.
DR VEuPathDB; FungiDB:Afu5g01890; -.
DR eggNOG; KOG0885; Eukaryota.
DR HOGENOM; CLU_012062_14_5_1; -.
DR InParanoid; Q4WE62; -.
DR OMA; GTYGSQF; -.
DR OrthoDB; 1392223at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Rotamase; Spliceosome.
FT CHAIN 1..559
FT /note="Peptidyl-prolyl isomerase cwc27"
FT /id="PRO_0000064181"
FT DOMAIN 11..184
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 201..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 62004 MW; A034433A17795D20 CRC64;
MSAHYTTEPP PTASATLHTT FGPIHIALFA NQTPLTCKNF LQHCLDNYYA GTIFHRIVPD
FIVQGGDPTG TGSGGTSIYE YPEFEYDPEA RDPNEKVVLR DELHSRLRFN RRGLVGMAKS
EDGTYGSQFF ITLANAEREL NGQCTLFGRV EGDSIYNVLK IAEAERVERT ERPVYPVKVV
SCEVGELGPF AGKLKRRETI ATAPAAEEKP AAKKKKKAKG GKTLLSFGGD EGDEDVPLRP
SKPKFNPTLV VDAGIPPAND APKKTSPEAE QQTRKRPRSP SPRRSLSAER KHRPKTPDPL
TQLPLPDPES PARSPPQSPP ARQSILSRTR AEIENLKASM RRTVATGPAD TGRKKSALEA
MIPETAIRGR KRPPPGTVNG AGRGSSTNGV TGFSSAAEDE TLRMFNAFKA KLESADAKSG
PHGKTSISAS DTTKYTSQAK SNTEPEDEEA QLCDLHFIAN CQSCKSWDDT GTAEEAPDDD
DRDWLTHELR FGKDMLGKDL QWKREHPDDV DSLVVIDPRE REKEFVGGKR RGLERDRERD
RKRERVGDQE WDRRRREKP
