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 489500730  41 PPIKEVRDQTGAwDSVGQARVITMVGGGRVREELTSVDPP-RSFGYTLTDikGPLaPLVALVeGKWSFAPADT-GTTVTW 118
Cdd:cd07821   31 PAVASCELEGGG-PGVGAVRTVTLKDGGTVRERLLALDDAeRRYSYRIVE--GPL-PVKNYV-ATIRVTPEGDgGTRVTW 105

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489500730 119 QWTIHPRSALAApvlPVFARMWRGYARGVLEKLSALL 155
Cdd:cd07821  106 TAEFDPPEGLTD---ELARAFLTGVYRAGLAALKAAL 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 489500730  41 PPIKEVRDQTGAwDSVGQARVITMVGGGRVREELTSVDPP-RSFGYTLTDikGPLaPLVALVeGKWSFAPADT-GTTVTW 118
Cdd:cd07821   31 PAVASCELEGGG-PGVGAVRTVTLKDGGTVRERLLALDDAeRRYSYRIVE--GPL-PVKNYV-ATIRVTPEGDgGTRVTW 105

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489500730 119 QWTIHPRSALAApvlPVFARMWRGYARGVLEKLSALL 155
Cdd:cd07821  106 TAEFDPPEGLTD---ELARAFLTGVYRAGLAALKAAL 139

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the 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
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489500730  65 VGGGRVreELTSVDPPRSFGYTLTDIKgplaPLVALVEGKWSFAPADTGTTVTWQ 119
Cdd:cd07818   63 VGEGEM--EITESVPNERIEYELRFIK----PFEATNDVEFTLEPVGGGTKVTWG 111

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the 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 489500730  34 SHWYgliPPIKEVRDQTGAWDSVG-QARVITMVGGGRV--REELTSVDPPRSfgYTLTDIKGPLAplvalVEGKWSFAPA 110
Cdd:cd08865   25 PEWD---PGVVEVEKITDGPVGVGtRYHQVRKFLGRRIelTYEITEYEPGRR--VVFRGSSGPFP-----YEDTYTFEPV 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489500730 111 DTGTTVTWQWTIHPrSALAAPVLPVFARMWRGYARGVLEKLSALL 155
Cdd:cd08865   95 GGGTRVRYTAELEP-GGFARLLDPLMAPAFRRRARAALENLKALL 138