ID A0A3B6GTL8_WHEAT Unreviewed; 240 AA.
AC A0A3B6GTL8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN ORFNames=CFC21_046707 {ECO:0000313|EMBL:KAF7035926.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS3D02G159000.1};
RN [1] {ECO:0000313|EMBL:KAF7035926.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7035926.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS3D02G159000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3D02G159000.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS3D02G159000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7035926.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7035926.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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. {ECO:0000256|RuleBase:RU363019}.
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 ECO:0000256|RuleBase:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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DR EMBL; CM022219; KAF7035926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6GTL8; -.
DR SMR; A0A3B6GTL8; -.
DR STRING; 4565.A0A3B6GTL8; -.
DR EnsemblPlants; TraesCS3D02G159000.1; TraesCS3D02G159000.1; TraesCS3D02G159000.
DR Gramene; TraesCAD_scaffold_027885_01G000100.1; TraesCAD_scaffold_027885_01G000100.1; TraesCAD_scaffold_027885_01G000100.
DR Gramene; TraesCLE_scaffold_129984_01G000100.1; TraesCLE_scaffold_129984_01G000100.1; TraesCLE_scaffold_129984_01G000100.
DR Gramene; TraesCS3D02G159000.1; TraesCS3D02G159000.1; TraesCS3D02G159000.
DR Gramene; TraesCS3D03G0339300.1; TraesCS3D03G0339300.1.CDS; TraesCS3D03G0339300.
DR Gramene; TraesKAR3D01G0099930.1; cds.TraesKAR3D01G0099930.1; TraesKAR3D01G0099930.
DR Gramene; TraesPAR_scaffold_045517_01G000100.1; TraesPAR_scaffold_045517_01G000100.1; TraesPAR_scaffold_045517_01G000100.
DR Gramene; TraesROB_scaffold_026304_01G000100.1; TraesROB_scaffold_026304_01G000100.1; TraesROB_scaffold_026304_01G000100.
DR Gramene; TraesWEE_scaffold_016297_01G000100.1; TraesWEE_scaffold_016297_01G000100.1; TraesWEE_scaffold_016297_01G000100.
DR OMA; CVNATDN; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000019116; Chromosome 3D.
DR Proteomes; UP000815260; Chromosome 3D.
DR GO; GO:0005737; C:cytoplasm; 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 CDD; cd01926; cyclophilin_ABH_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
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 SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 78..235
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 240 AA; 25698 MW; A870F551B72E6FDD CRC64;
MACRPAVSNP SALTPAPRRC VVPGRSSTRG RVDCPLRSSS AGAVRLGARR APAAAFVVRA
AAAEGDLDLQ AKVTSKCFFD VEIGGERAGK VVIGLFGEVV PKTVDNFRAL CTGDKGYGYK
GCSFHRIIKD FMIQGGDFQN NNGTGGRSIY GECFDDENFT LKHVGPGVLS MANAGPDTNG
SQFFICTVKT PWLDNRHVVF GHVLEGMDVV RELESQETSR SDIPKQPCRI VDCGELPLDG
//
