ID PPID_USTMA Reviewed; 398 AA.
AC Q4P0V4; A0A0D1CFS2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase D;
DE Short=PPIase D;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase D;
GN Name=CPR6; ORFNames=UMAG_06259;
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 (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: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC subfamily. {ECO:0000305}.
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DR EMBL; CM003161; KIS65883.1; -; Genomic_DNA.
DR RefSeq; XP_011392601.1; XM_011394299.1.
DR AlphaFoldDB; Q4P0V4; -.
DR SMR; Q4P0V4; -.
DR STRING; 237631.Q4P0V4; -.
DR EnsemblFungi; KIS65883; KIS65883; UMAG_06259.
DR GeneID; 23565907; -.
DR KEGG; uma:UMAG_06259; -.
DR VEuPathDB; FungiDB:UMAG_06259; -.
DR eggNOG; KOG0546; Eukaryota.
DR HOGENOM; CLU_012062_37_0_1; -.
DR InParanoid; Q4P0V4; -.
DR OMA; EMEQNCN; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000000561; Chromosome 22.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT CHAIN 1..398
FT /note="Peptidyl-prolyl cis-trans isomerase D"
FT /id="PRO_0000232951"
FT DOMAIN 21..185
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 229..262
FT /note="TPR 1"
FT REPEAT 282..323
FT /note="TPR 2"
FT REPEAT 335..368
FT /note="TPR 3"
SQ SEQUENCE 398 AA; 43637 MW; A19C5AA4245907BD CRC64;
MSSTNTTPKP GNPIVYLDLA FGSSPASRPG SNRIVLELYA DRVPRTAENF RVLCTNTSKL
ASTGQPLSFR NSIFHRVIPK FMIQGGDFTR ADGTGGESIY GEKFQDEDLT GKHDVPFLLS
MANAGANTNG SQFFITTVPT PHLDGKHVVF GRVLKGKGVV RRVESVETVA SDRPKEDVKI
VDCGELTGDE VSNQTYGIEQ DDTGDQYEDF PEDQDDKLES DVSATYHIGL ALKNMANTQF
SKANFDIALE KYSKALRYLQ LHPILPEDTP ADLAANYTTL KTSIQLNACL CALKTTPAQP
RVAISNATAV ISNLTSNKAP STEQADKNKY HSDLAKAFYR RASAYVAQKD DERAEADLKH
ALENAPEDAG VKRELQALAR RKEAKLKGMR AAYSKMFS
//
