ID A0A2T3AR71_AMORE Unreviewed; 181 AA.
AC A0A2T3AR71;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=M430DRAFT_129003 {ECO:0000313|EMBL:PSS08757.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS08757.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS08757.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS08757.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(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|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|RuleBase:RU363019}.
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DR EMBL; KZ679018; PSS08757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3AR71; -.
DR STRING; 857342.A0A2T3AR71; -.
DR InParanoid; A0A2T3AR71; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000241818; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
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 PIRSF; PIRSF001467; Peptidylpro_ismrse; 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:UP000241818};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 28..174
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 181 AA; 19453 MW; 9C1503CC94FE9F26 CRC64;
MTIKTFFDVT WEGPVLDASG KQTGKVAEQS GRINFNLYDD VVPKTAENFR ALCTGEKGFG
YAGSSFHRII PQFMLQGGDF TRGNGTGGKS IYGEKFADEN FVKKHSRPGL LSMANAGPNT
NGSQFFITTV VTSWLDGKHV VFGEVADDES LAVVKALEAT GSGSGKVQYN KKPTIVKSGQ
L
//
