ID A0A2K3MA26_TRIPR Unreviewed; 249 AA.
AC A0A2K3MA26;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
DE Flags: Fragment;
GN ORFNames=L195_g043730 {ECO:0000313|EMBL:PNX87637.1};
OS Trifolium pratense (Red clover).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX NCBI_TaxID=57577 {ECO:0000313|EMBL:PNX87637.1, ECO:0000313|Proteomes:UP000236291};
RN [1] {ECO:0000313|EMBL:PNX87637.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNX87637.1};
RX PubMed=24500806; DOI=10.3732/ajb.1300340;
RA Istvanek J., Jaros M., Krenek A., Repkova J.;
RT "Genome assembly and annotation for red clover (Trifolium pratense;
RT Fabaceae).";
RL Am. J. Bot. 101:327-337(2014).
RN [2] {ECO:0000313|EMBL:PNX87637.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNX87637.1};
RX PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT (Trifolium pratense) Breeding.";
RL Front. Plant Sci. 8:367-367(2017).
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|RuleBase:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|RuleBase:RU363019}.
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:PNX87637.1}.
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DR EMBL; ASHM01054360; PNX87637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3MA26; -.
DR STRING; 57577.A0A2K3MA26; -.
DR Proteomes; UP000236291; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
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; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46512; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00515; TPR_1; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF48452; TPR-like; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000236291};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT DOMAIN 1..65
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REPEAT 105..138
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 191..224
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT NON_TER 249
FT /evidence="ECO:0000313|EMBL:PNX87637.1"
SQ SEQUENCE 249 AA; 27877 MW; 112821C1F1590AF0 CRC64;
MANTGPNTNG SQFFISTTRT AHLDGKNVVF GKVVKGMGVV RSIEHVMTGD EDRPVLDIKI
VDCGEIPEGE DDGITNFFKD GDTYPDWPVD LAESPSELEW WLKSVDSIKA LGNEYYKKQD
YKMAIRKYRK ALRYLDICWE KEGIDEDKSS GLRKTKSQIF TNSSACKLKL GDINGALLDT
EFAMREGINN AKALFRQGQA YMVLNDIDAA VESFKKALTL EPNDGGIKKE LAAARKKISN
RTDLEKKAY
//
