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 822022815   5 QKINIVQEFDAPVDKVFAALSEHENLSILFAPAKVTRISNGKDarnGVGSARKMSIPFTPSFVETNLVYKENE-LIEYAI 83
Cdd:cd07821    1 AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGGP---GVGAVRTVTLKDGGTVRERLLALDDAErRYSYRI 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 822022815  84 TSGISPIKAHRGVMQFTDLGNNRTRLNYTISFKGRVPFIGPIIKAALQNGVSRGLKKLK 142
Cdd:cd07821   78 VEGPLPVKNYVATIRVTPEGDGGTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALK 136

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 822022815   5 QKINIVQEFDAPVDKVFAALSEHENLSILFAPAKVTRISNGKDarnGVGSARKMSIPFTPSFVETNLVYKENE-LIEYAI 83
Cdd:cd07821    1 AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGGP---GVGAVRTVTLKDGGTVRERLLALDDAErRYSYRI 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 822022815  84 TSGISPIKAHRGVMQFTDLGNNRTRLNYTISFKGRVPFIGPIIKAALQNGVSRGLKKLK 142
Cdd:cd07821   78 VEGPLPVKNYVATIRVTPEGDGGTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALK 136

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822022815   1 MLKTQKINIVQEFDAPVDKVFAALSEHENLSILFAPAKVTRISNGkDARNGvGSAR-KMSIP--FTPSFVETNLVYKENE 77
Cdd:COG3832    2 DAEDRTITIEREIDAPPERVWRAWTDPELLARWFGPKGWATVAEF-DLRVG-GRFRfRMRGPdgEEFGFEGEVLEVEPPE 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 822022815  78 LIEYAITSGISPIKAHRGVMQFTDLGnNRTRLNYTISF 115
Cdd:COG3832   80 RLVFTWGFEDDPEGESTVTVTLEPEG-GGTRLTLTHTG 116

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 822022815   5 QKINIVQEFDAPVDKVFAALSEHENLSILFAPAKVTRISNGKDarnGVGSARKMSIPFTPSFVETNLVYKENE-LIEYAI 83
Cdd:cd07821    1 AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVASCELEGGGP---GVGAVRTVTLKDGGTVRERLLALDDAErRYSYRI 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 822022815  84 TSGISPIKAHRGVMQFTDLGNNRTRLNYTISFKGRVPFIGPIIKAALQNGVSRGLKKLK 142
Cdd:cd07821   78 VEGPLPVKNYVATIRVTPEGDGGTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALK 136

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822022815   1 MLKTQKINIVQEFDAPVDKVFAALSEHENLSILFAPAKVTRISNGkDARNGvGSAR-KMSIP--FTPSFVETNLVYKENE 77
Cdd:COG3832    2 DAEDRTITIEREIDAPPERVWRAWTDPELLARWFGPKGWATVAEF-DLRVG-GRFRfRMRGPdgEEFGFEGEVLEVEPPE 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 822022815  78 LIEYAITSGISPIKAHRGVMQFTDLGnNRTRLNYTISF 115
Cdd:COG3832   80 RLVFTWGFEDDPEGESTVTVTLEPEG-GGTRLTLTHTG 116

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 822022815  12 EFDAPVDKVFAALSEHENLSILFAPAKVTRISNGKDARNGVGSARKMSIPFTPSFVETNLVYKENELIEYAITSGISPIK 91
Cdd:cd07812    6 EIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGRRLTLTSEVTEVDPPRPGRFRVTGGGGGVD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 822022815  92 AhRGVMQFTDLGNNRTRLNYTISFKGRVPF---IGPIIKAALQNGVSRGLKKLK 142
Cdd:cd07812   86 G-TGEWRLEPEGDGGTRVTYTVEYDPPGPLlkvFALLLAGALKRELAALLRALK 138

Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822022815   7 INIVQEFDAPVDKVFAALSEHENLSILFAPAKVTRIsngkDARNGvGSARKMSIPFTPSFVETNLVYKE---NELIEYai 83
Cdd:cd07814    2 ITIEREFDAPPELVWRALTDPELLAQWFGPTTTAEM----DLRVG-GRWFFFMTGPDGEEGWVSGEVLEvepPRRLVF-- 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 822022815  84 TSGISPIKAHRG---VMQFTDLGnNRTRLNYTISF 115
Cdd:cd07814   75 TWAFSDETPGPEttvTVTLEETG-GGTRLTLTHSG 108

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 822022815  12 EFDAPVDKVFAALSEHENLSILFAPAKVTRISNGkDARNGVGS--ARKMSIPFTPSFVeTNLV--YKENELIEYAITSGI 87
Cdd:cd07825    7 TVDAPAEAVFAVLADPRRHPEIDGSGTVREAIDG-PRILAVGDvfRMAMRLDGGPYRI-TNHVvaFEENRLIAWRPGPAG 84

                         90       100
                 ....*....|....*....|....*
gi 822022815  88 SPIKAHRGVMQFTDLGNNRTRLNYT 112
Cdd:cd07825   85 QEPGGHRWRWELEPIGPGRTRVTET 109