FKB70_WHEAT
ID FKB70_WHEAT Reviewed; 559 AA.
AC Q43207;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=70 kDa peptidyl-prolyl isomerase;
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
GN Name=FKBP70;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Atir; TISSUE=Root tip;
RA Oshra B., Breiman A.;
RT "Wheat FKBP70 - a novel heat shock and calmodulin binding PPIase.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIases accelerate the folding of proteins during protein
CC synthesis.
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 -!- SUBUNIT: This PPIase probably binds calmodulin.
CC -!- INDUCTION: By heat shock.
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DR EMBL; X86903; CAA60505.1; -; mRNA.
DR PIR; S55383; S55383.
DR PDB; 3JXV; X-ray; 2.08 A; A=31-386.
DR PDB; 3JYM; X-ray; 2.28 A; A/B=15-391.
DR PDBsum; 3JXV; -.
DR PDBsum; 3JYM; -.
DR SMR; Q43207; -.
DR STRING; 4565.Traes_7BS_0B7C600F6.1; -.
DR PRIDE; Q43207; -.
DR eggNOG; KOG0543; Eukaryota.
DR EvolutionaryTrace; Q43207; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q43207; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 3.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00254; FKBP_C; 3.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 3.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Isomerase; Reference proteome; Repeat;
KW Rotamase; Stress response; TPR repeat.
FT CHAIN 1..559
FT /note="70 kDa peptidyl-prolyl isomerase"
FT /id="PRO_0000075335"
FT DOMAIN 60..148
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 176..265
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 293..384
FT /note="PPIase FKBP-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 401..434
FT /note="TPR 1"
FT REPEAT 450..483
FT /note="TPR 2"
FT REPEAT 484..517
FT /note="TPR 3"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3JYM"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3JYM"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:3JYM"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:3JYM"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3JYM"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:3JYM"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 192..202
FT /evidence="ECO:0007829|PDB:3JXV"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:3JXV"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:3JXV"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3JXV"
FT TURN 234..238
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 295..307
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3JXV"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:3JXV"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:3JXV"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:3JXV"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:3JXV"
FT STRAND 374..384
FT /evidence="ECO:0007829|PDB:3JXV"
SQ SEQUENCE 559 AA; 62058 MW; 5C5DAE70D716B541 CRC64;
MDDDFDIPAG DDMMMGDGMG DFGGAEGPGM KVGEENEIGK QGLKKKLLKE GEGWDTPEVG
DEVEVHYTGT LLDGKKFDSS RDRDDTFKFK LGQGQVIKGW DQGIKTMKKG ENALFTIPPE
LAYGESGSPP TIPANATLQF DVELLSWTSV RDIAKDGGIF KKILKEGDKW ENPKDPDEVF
VKYEARLEDG TVVSKSEGVE FTVKDGHLCP ALAKAVKTMK KGEKVLLAVK PQYGFGEMGR
PAAGEGGAVP PNASLVIDLE LVSWKTVTEI GDDKKILKKV LKEXEGYERP NEGAVVTVKI
TGKLQDGTVF LKKGHDEQEP FEFKTDEEAV IEGLDRAVLN MKKGEVALVT IPPEYAYGST
ESKQDAIVPP NSTVIYEVEL VSFVKDKESW DLNNSEKIEA AGTKKEEGNA LFKSGKYARA
SKRYEKAAKF IEYDTSFSED EKKQSKQLKI TCNLNNAACK LKLKDYKQAE KLCTKVLELD
SRNVKALYRR AQAYTQLADL ELAEVDIKKA LEIDPENRDV KLTYKTLKEK IKEINKKDAK
FYSNMFSKMT KPSAEESKA
