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Entry: C6TKH9_SOYBN
LinkDB: C6TKH9_SOYBN
Original site: C6TKH9_SOYBN 
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
//
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