ID U9U0T1_RHIID Unreviewed; 364 AA.
AC U9U0T1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=GLOIN_2v1801361 {ECO:0000313|EMBL:POG80361.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:POG80361.1, ECO:0000313|Proteomes:UP000018888};
RN [1] {ECO:0000313|EMBL:POG80361.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888};
RX PubMed=24277808; DOI=10.1073/pnas.1313452110;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei Dit Frey N., Gianinazzi-Pearson V.,
RA Gilbert L.B., Handa Y., Herr J.R., Hijri M., Koul R., Kawaguchi M.,
RA Krajinski F., Lammers P.J., Masclaux F.G., Murat C., Morin E.,
RA Ndikumana S., Pagni M., Petitpierre D., Requena N., Rosikiewicz P.,
RA Riley R., Saito K., San Clemente H., Shapiro H., van Tuinen D., Becard G.,
RA Bonfante P., Paszkowski U., Shachar-Hill Y.Y., Tuskan G.A., Young P.W.,
RA Sanders I.R., Henrissat B., Rensing S.A., Grigoriev I.V., Corradi N.,
RA Roux C., Martin F.;
RT "Genome of an arbuscular mycorrhizal fungus provides insight into the
RT oldest plant symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20117-20122(2013).
RN [2] {ECO:0000313|EMBL:POG80361.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888};
RX PubMed=29355972;
RA Chen E.C.H., Morin E., Beaudet D., Noel J., Yildirir G., Ndikumana S.,
RA Charron P., St-Onge C., Giorgi J., Kruger M., Marton T., Ropars J.,
RA Grigoriev I.V., Hainaut M., Henrissat B., Roux C., Martin F., Corradi N.;
RT "High intraspecific genome diversity in the model arbuscular mycorrhizal
RT symbiont Rhizophagus irregularis.";
RL New Phytol. 0:0-0(2018).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|ARBA:ARBA00002388}.
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 Evidence={ECO:0000256|ARBA:ARBA00000971};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC subfamily. {ECO:0000256|ARBA:ARBA00010898}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POG80361.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AUPC02000018; POG80361.1; -; Genomic_DNA.
DR AlphaFoldDB; U9U0T1; -.
DR VEuPathDB; FungiDB:GLOIN_2v1801361; -.
DR eggNOG; KOG0546; Eukaryota.
DR HOGENOM; CLU_012062_37_0_1; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000018888; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
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 Pfam; PF13181; TPR_8; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 3.
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; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:POG80361.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018888};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 6..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 364 AA; 40764 MW; 0827073E100CB839 CRC64;
MSVRCFFDID IGDVREGRIV FELFDDLIPN TVENFRALCT GEKGIGKSGY PLHYKGSTFH
RVIKGFMIQG GDFTRGDGTG GESIYGDKFD DESFDVKHDE PFLLSMANAG PNTNGSQFFI
TTGKATHLDD KHVIFGRVLK GKSVVRAIEN NPTGTNDKPI KKVTIVDCGE LKEDEDDGVP
VPADGDTYED WPEDESGSLK PEKLLEIAQK VKDIGNDYFK KGDYLNASKK YTKAIRYLNE
KTTFEDDDPP ELEKKFYSLK ISCYLNKAAC SLKLQNWKNA VDDTTIVLEM SPEYLLDADK
AKALYRRGSA KVGMKDEEEA VKDLQQASKL NPQDAAIAKE IAIAKQKLKA REEKQKKAFA
KMFE
//
