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Conserved domains on  [gi|1002226418|ref|XP_015626787|]
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lachrymatory-factor synthase [Oryza sativa Japonica Group]

Protein Classification

SRPBCC family protein( domain architecture ID 10167503)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

CATH:  3.30.530.20
PubMed:  18922149
SCOP:  3000738

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
37-185 6.60e-25

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.


:

Pssm-ID: 176863 [Multi-domain]  Cd Length: 140  Bit Score: 95.08  E-value: 6.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002226418  37 ATADEAWALLSDFLAFHRWHPRVAKCRPASPSAAAstaaappGSVvRYCEGTPRGdgappdWAHETLLEHDAARRFFRYE 116
Cdd:cd07821    11 APADKVWALLSDFGGLHKWHPAVASCELEGGGPGV-------GAV-RTVTLKDGG------TVRERLLALDDAERRYSYR 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002226418 117 MNDNNMGFGVFVATFRVVPDAGGgdadapGCELRWEFEGDPVRGTPKEALVARLQAGLDGMAARVQEHL 185
Cdd:cd07821    77 IVEGPLPVKNYVATIRVTPEGDG------GTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALKAAL 139
 
Name Accession Description Interval E-value
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
37-185 6.60e-25

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.


Pssm-ID: 176863 [Multi-domain]  Cd Length: 140  Bit Score: 95.08  E-value: 6.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002226418  37 ATADEAWALLSDFLAFHRWHPRVAKCRPASPSAAAstaaappGSVvRYCEGTPRGdgappdWAHETLLEHDAARRFFRYE 116
Cdd:cd07821    11 APADKVWALLSDFGGLHKWHPAVASCELEGGGPGV-------GAV-RTVTLKDGG------TVRERLLALDDAERRYSYR 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002226418 117 MNDNNMGFGVFVATFRVVPDAGGgdadapGCELRWEFEGDPVRGTPKEALVARLQAGLDGMAARVQEHL 185
Cdd:cd07821    77 IVEGPLPVKNYVATIRVTPEGDG------GTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALKAAL 139
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
37-182 3.06e-16

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.


Pssm-ID: 431388  Cd Length: 139  Bit Score: 72.13  E-value: 3.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002226418  37 ATADEAWALLSDFLAFHRWHPRVAKCRpaspsaaastaAAPPGSVVRYCEGTPRGDGAPPdWAHETLLEHDAARRFFRYE 116
Cdd:pfam10604   7 APPEQVWALLSDFENWPRWHPGVLRVE-----------LEGGGGPLRGVVGTLRVGGRRG-TVREELVEYDPAPRLLAYR 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002226418 117 MNDnNMGFGVFVATFRVVPDAGggdadapGCELRW--EFEGDPVRG-----TPKEALVARLQAGLDGMAARVQ 182
Cdd:pfam10604  75 IVE-PLGVANYVGTWTVTPAGG-------GTRVTWtgEFDGPPLGGpfrdpAAARAVKGDYRAGLDRLKAVLE 139
 
Name Accession Description Interval E-value
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
37-185 6.60e-25

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.


Pssm-ID: 176863 [Multi-domain]  Cd Length: 140  Bit Score: 95.08  E-value: 6.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002226418  37 ATADEAWALLSDFLAFHRWHPRVAKCRPASPSAAAstaaappGSVvRYCEGTPRGdgappdWAHETLLEHDAARRFFRYE 116
Cdd:cd07821    11 APADKVWALLSDFGGLHKWHPAVASCELEGGGPGV-------GAV-RTVTLKDGG------TVRERLLALDDAERRYSYR 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002226418 117 MNDNNMGFGVFVATFRVVPDAGGgdadapGCELRWEFEGDPVRGTPKEALVARLQAGLDGMAARVQEHL 185
Cdd:cd07821    77 IVEGPLPVKNYVATIRVTPEGDG------GTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALKAAL 139
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
37-182 3.06e-16

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.


Pssm-ID: 431388  Cd Length: 139  Bit Score: 72.13  E-value: 3.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002226418  37 ATADEAWALLSDFLAFHRWHPRVAKCRpaspsaaastaAAPPGSVVRYCEGTPRGDGAPPdWAHETLLEHDAARRFFRYE 116
Cdd:pfam10604   7 APPEQVWALLSDFENWPRWHPGVLRVE-----------LEGGGGPLRGVVGTLRVGGRRG-TVREELVEYDPAPRLLAYR 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002226418 117 MNDnNMGFGVFVATFRVVPDAGggdadapGCELRW--EFEGDPVRG-----TPKEALVARLQAGLDGMAARVQ 182
Cdd:pfam10604  75 IVE-PLGVANYVGTWTVTPAGG-------GTRVTWtgEFDGPPLGGpfrdpAAARAVKGDYRAGLDRLKAVLE 139
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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