PPID_RHIO9
ID PPID_RHIO9 Reviewed; 364 AA.
AC P0C1I1; I1BHX4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase D;
DE Short=PPIase D;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin D;
DE AltName: Full=Rotamase D;
GN Name=cyp12; ORFNames=RO3G_00508;
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
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; CH476732; EIE75804.1; -; Genomic_DNA.
DR AlphaFoldDB; P0C1I1; -.
DR SMR; P0C1I1; -.
DR STRING; 936053.P0C1I1; -.
DR PRIDE; P0C1I1; -.
DR EnsemblFungi; EIE75804; EIE75804; RO3G_00508.
DR VEuPathDB; FungiDB:RO3G_00508; -.
DR eggNOG; KOG0546; Eukaryota.
DR InParanoid; P0C1I1; -.
DR OMA; CKDFGNK; -.
DR OrthoDB; 1403619at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
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:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
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; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF13181; TPR_8; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 3.
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; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT CHAIN 1..364
FT /note="Peptidyl-prolyl cis-trans isomerase D"
FT /id="PRO_0000244714"
FT DOMAIN 7..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 208..241
FT /note="TPR 1"
FT REPEAT 261..294
FT /note="TPR 2"
FT REPEAT 301..334
FT /note="TPR 3"
SQ SEQUENCE 364 AA; 40405 MW; 199C543FF41A3354 CRC64;
MSNPRVYFDI TIGNKPEGRI VFELFKDIVP KTAENFRALC TGEKGEGKSG KPLSYQGSLF
HRIIKNFMIQ GGDFTAGNGT GGESIYGEKF EDENFVLKHE KPFLLSMANA GPGTNGSQFF
ITTVPTPHLD GKHVVFGKVL KGKAVVRALE NLETVSDRPV EDAVIAKCGE LAEGEDDGIR
ASEDGDVYEE YPDDHEGPKE PNDVLQIATH LKDIGNTYFK KGDHANAAKK YLKAIRYLNE
KPAFDENDPK ELEGKFAAIK IPCYLNRSMC ALKLGEYSEC VKVTTTVLEY DSKYLKPTDI
TKAYFRRGSA KMNTRDFEGA IEDFEKAHEK DPEDAGIKKE LANAKAKLAA KKQKEKSAYA
KMFA