PPID_ASHGO
ID PPID_ASHGO Reviewed; 369 AA.
AC Q75A33;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 117.
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; OrderedLocusNames=ADR087C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52007.1; -; Genomic_DNA.
DR RefSeq; NP_984183.1; NM_209536.2.
DR AlphaFoldDB; Q75A33; -.
DR SMR; Q75A33; -.
DR STRING; 33169.AAS52007; -.
DR EnsemblFungi; AAS52007; AAS52007; AGOS_ADR087C.
DR GeneID; 4620332; -.
DR KEGG; ago:AGOS_ADR087C; -.
DR eggNOG; KOG0546; Eukaryota.
DR HOGENOM; CLU_012062_37_0_1; -.
DR InParanoid; Q75A33; -.
DR OMA; CKDFGNK; -.
DR Proteomes; UP000000591; Chromosome IV.
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:0043022; F:ribosome binding; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR Gene3D; 1.25.40.10; -; 1.
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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50891; SSF50891; 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; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT CHAIN 1..369
FT /note="Peptidyl-prolyl cis-trans isomerase D"
FT /id="PRO_0000232941"
FT DOMAIN 8..173
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 218..251
FT /note="TPR 1"
FT REPEAT 269..302
FT /note="TPR 2"
FT REPEAT 306..339
FT /note="TPR 3"
SQ SEQUENCE 369 AA; 39990 MW; FC53B22D48A0F191 CRC64;
MTERQKTYFD LSIGGKPAGR VVFEVYSDVT PKTAENFVRL CAGDAGECRT KPGVPLCYQG
SLFHRVIKGF MCQFGDFTNG DGTGGESIYG EKFEDENFAR KHDRPFLLSM ANAGPNTNGS
QCFITCAPTP HLDGKHVVFG EVIQGKRVVR AIERQETAAD RPLADVRIDA CGILPASYEV
PADAEATPAD EYGDDYEETL ADDAKVDLAD PRSVIRAVEA VKAIGTAQLQ AARFDVAVQK
YAKAAGFLQE YFPDDLPDAD VAALEQLKVA VHLNLALAAL KAGNHQRVLS AASEVLHGAA
DDKAKAKALY RRGLAYHHLK DPEMALTDLE LAATYQPGDA GIAQAIVNAR ALKQKLREQQ
KKALSKMFS
