ID C6TKH9_SOYBN Unreviewed; 370 AA.
AC C6TKH9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 03-MAY-2023, entry version 65.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:ACU23419.1};
RN [1] {ECO:0000313|EMBL:ACU23419.1}
RP NUCLEOTIDE SEQUENCE.
RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|PROSITE-
CC ProRule:PRU00277};
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DR EMBL; BT098191; ACU23419.1; -; mRNA.
DR AlphaFoldDB; C6TKH9; -.
DR HOGENOM; CLU_013615_4_0_1; -.
DR ExpressionAtlas; C6TKH9; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR039663; AIP/AIPL1/TTC9.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11242; ARYL HYDROCARBON RECEPTOR INTERACTING PROTEIN RELATED; 1.
DR PANTHER; PTHR11242:SF11; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP42; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS50005; TPR; 1.
PE 2: Evidence at transcript level;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 343..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..163
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REPEAT 268..301
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 42270 MW; FE921542C53909A5 CRC64;
MEELQGSQTQ SSLGQEDENE VITESSAFVK GEPAPEFSSN PPKVDSEVEV LHEKVTKQII
KEGHGQKPSK YSTCFFHYRA WAEKSEHKFE DTWLEQRPIE MVLGKEKKEM TGLSVGVASM
KAGERALVRV GWELGYGEEG SFSFPNVPPK ADLVYEVELI GFDETKEGKA RSDMTVEERI
GAADRRKMDG NALYQEEKLE EAMQQYEMAI AYMGDDFMFQ LFGKYRDMAL AVKNPCHLNM
AACLIKLNRY EEAIGQCNTV LGEDENNVKA LFRRGKARAT FGQTDAARED FLKATKYAPQ
DKAIAKELRL LAEHDKAVYQ KQKEIYKGIF GPRPQPVPKP RNWLILIWQW LLSVFYGLVT
LFKRERHKSD
//