CWC27_USTMA
ID CWC27_USTMA Reviewed; 485 AA.
AC Q4P7H2; A0A0D1DZC2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=UMAG_03941;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003150; KIS67885.1; -; Genomic_DNA.
DR RefSeq; XP_011390410.1; XM_011392108.1.
DR AlphaFoldDB; Q4P7H2; -.
DR SMR; Q4P7H2; -.
DR STRING; 5270.UM03941P0; -.
DR EnsemblFungi; KIS67885; KIS67885; UMAG_03941.
DR GeneID; 23564258; -.
DR KEGG; uma:UMAG_03941; -.
DR VEuPathDB; FungiDB:UMAG_03941; -.
DR eggNOG; KOG0885; Eukaryota.
DR HOGENOM; CLU_012062_14_4_1; -.
DR InParanoid; Q4P7H2; -.
DR OMA; VWHRIVP; -.
DR OrthoDB; 1392223at2759; -.
DR Proteomes; UP000000561; Chromosome 11.
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..485
FT /note="Peptidyl-prolyl isomerase CWC27"
FT /id="PRO_0000064187"
FT DOMAIN 11..167
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 173..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 54023 MW; B3F21234EC915BAE CRC64;
MTSQYVTEPP SSGLVDLVTS KGTISIALFP TQAPLACRNF LTLALEGFYD NLVFHRLIPN
FILQTGDPSA TGTGGESIYG EPFPIESHSR LKFNRRGLLG MAANQDRTNE SQFFLTLDAT
PELTGKHTLM GKVEGKSIYT LVELVEGVEL VDGDRPRYPI KLHEVRVVEN PFDDLQPRTT
KKQRIAEERR KKHEMETRVA EEQKRKRSKA KKNTGLLSFG AEEEAEDEVA LKGPKSSHDL
LKDDKHLSRQ TIETSKSTKA NTPAVSANIS SKEKRFLAQS SSSTTPPAVT KQASKDGTSD
APHPTATLKS EHSGPSDQKA SSSTGRDFLA SQRAKYLSSS HPSTAKQDDS YSALLSFQSR
LRTRPSSTTP IAKPLPSVGV DEVEEEAGEY GASDDDDDWR SHRLDAGGQP LVAGQNAGKD
TLEDYEVLDP RDHTDRERNP KAESSRDGKR GRDWVEHDRK YQNDRSRRHR EHDKHPQQRR
QRSII
