Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid receptors (RCARs), and related proteins; The PYR/PYL/RCAR-like family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. PYR/PYL/RCAR plant proteins are receptors involved in signal transduction. They bind abscisic acid (ABA) and mediate its signaling. ABA is a vital plant hormone, which regulates plant growth, development, and response to environmental stresses. Upon binding ABA, these plant proteins interact with a type 2C protein phosphatase (PP2C), such as ABI1 and ABI2, and inhibit their activity. When ABA is bound, a loop (designated the gate/CL2 loop) closes over the ligand binding pocket, resulting in the weakening of the inactive PYL dimer and facilitating type 2C protein phosphatase binding. In the ABA:PYL1:ABI1 complex, the gate blocks substrate access to the phosphatase active site. A conserved Trp from PP2C inserts into PYL to lock the receptor in a closed formation. This group also contains Methylobacterium extorquens AM1 MxaD. The mxaD gene is located within the mxaFJGIR(S)ACKLDEHB cluster which encodes proteins involved in methanol oxidation. MxaD may participate in the periplasmic electron transport chain for oxidation of methanol. Mutants lacking MxaD exhibit a reduced growth on methanol, and a lower rate of respiration with methanol.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1982796496   4 VITIQKEFNAPLSDVFNLLSKHAAYNTAFAPlqvvrVKDSADPERPDGVGSVRRMGFGVIKPLKEEITHL-EENKRIEYK 82
Cdd:cd07821     2 KVTVSVTIDAPADKVWALLSDFGGLHKWHPA-----VASCELEGGGPGVGAVRTVTLKDGGTVRERLLALdDAERRYSYR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1982796496  83 LIDNPL-VKHHLGRIEFSEITPYITLVTYRIELTAKAPVVSKLILAQLKLAITLGFSRLAKAF 144
Cdd:cd07821    77 IVEGPLpVKNYVATIRVTPEGDGGTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALKAAL 139

Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid receptors (RCARs), and related proteins; The PYR/PYL/RCAR-like family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. PYR/PYL/RCAR plant proteins are receptors involved in signal transduction. They bind abscisic acid (ABA) and mediate its signaling. ABA is a vital plant hormone, which regulates plant growth, development, and response to environmental stresses. Upon binding ABA, these plant proteins interact with a type 2C protein phosphatase (PP2C), such as ABI1 and ABI2, and inhibit their activity. When ABA is bound, a loop (designated the gate/CL2 loop) closes over the ligand binding pocket, resulting in the weakening of the inactive PYL dimer and facilitating type 2C protein phosphatase binding. In the ABA:PYL1:ABI1 complex, the gate blocks substrate access to the phosphatase active site. A conserved Trp from PP2C inserts into PYL to lock the receptor in a closed formation. This group also contains Methylobacterium extorquens AM1 MxaD. The mxaD gene is located within the mxaFJGIR(S)ACKLDEHB cluster which encodes proteins involved in methanol oxidation. MxaD may participate in the periplasmic electron transport chain for oxidation of methanol. Mutants lacking MxaD exhibit a reduced growth on methanol, and a lower rate of respiration with methanol.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1982796496   4 VITIQKEFNAPLSDVFNLLSKHAAYNTAFAPlqvvrVKDSADPERPDGVGSVRRMGFGVIKPLKEEITHL-EENKRIEYK 82
Cdd:cd07821     2 KVTVSVTIDAPADKVWALLSDFGGLHKWHPA-----VASCELEGGGPGVGAVRTVTLKDGGTVRERLLALdDAERRYSYR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1982796496  83 LIDNPL-VKHHLGRIEFSEITPYITLVTYRIELTAKAPVVSKLILAQLKLAITLGFSRLAKAF 144
Cdd:cd07821    77 IVEGPLpVKNYVATIRVTPEGDGGTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALKAAL 139

Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1982796496   1 MRNVITIQKEFNAPLSDVFNLLSKHAAYNTAFAPLQVVRVKDSaDPErpdgVGSVRRMGF----GVIKPLKEEITHLEEN 76
Cdd:COG3832     4 EDRTITIEREIDAPPERVWRAWTDPELLARWFGPKGWATVAEF-DLR----VGGRFRFRMrgpdGEEFGFEGEVLEVEPP 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1982796496  77 KRIEYklidnplvkhhlgRIEFSEITPYITLVTYRIE 113
Cdd:COG3832    79 ERLVF-------------TWGFEDDPEGESTVTVTLE 102

Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid receptors (RCARs), and related proteins; The PYR/PYL/RCAR-like family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. PYR/PYL/RCAR plant proteins are receptors involved in signal transduction. They bind abscisic acid (ABA) and mediate its signaling. ABA is a vital plant hormone, which regulates plant growth, development, and response to environmental stresses. Upon binding ABA, these plant proteins interact with a type 2C protein phosphatase (PP2C), such as ABI1 and ABI2, and inhibit their activity. When ABA is bound, a loop (designated the gate/CL2 loop) closes over the ligand binding pocket, resulting in the weakening of the inactive PYL dimer and facilitating type 2C protein phosphatase binding. In the ABA:PYL1:ABI1 complex, the gate blocks substrate access to the phosphatase active site. A conserved Trp from PP2C inserts into PYL to lock the receptor in a closed formation. This group also contains Methylobacterium extorquens AM1 MxaD. The mxaD gene is located within the mxaFJGIR(S)ACKLDEHB cluster which encodes proteins involved in methanol oxidation. MxaD may participate in the periplasmic electron transport chain for oxidation of methanol. Mutants lacking MxaD exhibit a reduced growth on methanol, and a lower rate of respiration with methanol.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1982796496   4 VITIQKEFNAPLSDVFNLLSKHAAYNTAFAPlqvvrVKDSADPERPDGVGSVRRMGFGVIKPLKEEITHL-EENKRIEYK 82
Cdd:cd07821     2 KVTVSVTIDAPADKVWALLSDFGGLHKWHPA-----VASCELEGGGPGVGAVRTVTLKDGGTVRERLLALdDAERRYSYR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1982796496  83 LIDNPL-VKHHLGRIEFSEITPYITLVTYRIELTAKAPVVSKLILAQLKLAITLGFSRLAKAF 144
Cdd:cd07821    77 IVEGPLpVKNYVATIRVTPEGDGGTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALKAAL 139

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1982796496   5 ITIQKEFNAPLSDVFNLLSKHAAYNTAFAPLQVVRVKDsaDPERPDGVGSVRRMGFGVIKPLKEEITHLEENKRIEYKLI 84
Cdd:cd07812     1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLG--GGEGGVGARFVGGRKGGRRLTLTSEVTEVDPPRPGRFRVT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1982796496  85 DNPLVKHHLGRIEFSEITPYITLVTYRIELTAKAPVVSKL 124
Cdd:cd07812    79 GGGGGVDGTGEWRLEPEGDGGTRVTYTVEYDPPGPLLKVF 118