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Conserved domains on  [gi|1082599077|gb|OFZ29458|]
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polyketide cyclase/dehydrase [Bacteroidetes bacterium RIFOXYC2_FULL_40_12]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 10-144 1.09e-23

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.


The actual alignment was detected with superfamily member cd08862:

Pssm-ID: 472699  Cd Length: 138  Bit Score: 89.34  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  10 VKCSKTITINANSEKVWAVMTNINNWATWQTDISKPKLNGE-LKPETTFDWK-TGGVKIHSTLHTVEPFKKLGWTGKTYG 87
Cdd:cd08862     1 MKFEATIVIDAPPERVWAVLTDVENWPAWTPSVETVRLEGPpPAVGSSFKMKpPGLVRSTFTVTELRPGHSFTWTGPAPG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1082599077  88 LSAVHNWTLTETN-GQTNVSVDESMEGFFAGLLKKPFSKNLEKGMQNWLDLLKQECEK 144
Cdd:cd08862    81 ISAVHRHEFEAKPdGGVRVTTSESLSGPLAFLFGLFVGKKLRALLPEWLEGLKAAAEQ 138
 
Name Accession Description Interval E-value
SRPBCC_Smu440-like cd08862
Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins; This family ...
 10-144 1.09e-23

Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Streptococcus mutans Smu.440 and related proteins. This domain belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Streptococcus mutans is a dental pathogen, and the leading cause of dental caries. In this pathogen, the gene encoding Smu.440 is in the same operon as the gene encoding SMU.441, a member of the MarR protein family of transcriptional regulators involved in multiple antibiotic resistance. It has been suggested that SMU.440 is involved in polyketide-like antibiotic resistance.


Pssm-ID: 176871  Cd Length: 138  Bit Score: 89.34  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  10 VKCSKTITINANSEKVWAVMTNINNWATWQTDISKPKLNGE-LKPETTFDWK-TGGVKIHSTLHTVEPFKKLGWTGKTYG 87
Cdd:cd08862     1 MKFEATIVIDAPPERVWAVLTDVENWPAWTPSVETVRLEGPpPAVGSSFKMKpPGLVRSTFTVTELRPGHSFTWTGPAPG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1082599077  88 LSAVHNWTLTETN-GQTNVSVDESMEGFFAGLLKKPFSKNLEKGMQNWLDLLKQECEK 144
Cdd:cd08862    81 ISAVHRHEFEAKPdGGVRVTTSESLSGPLAFLFGLFVGKKLRALLPEWLEGLKAAAEQ 138
COG4891 COG4891
Uncharacterized conserved protein [Function unknown];
15-144 1.76e-11

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443919  Cd Length: 138  Bit Score: 57.62  E-value: 1.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  15 TITINANSEKVWAVMTNINNWATWQTDIskPKLNGELKPETTFDWKT-----GGVKIHSTLHTVEPFKKLGWTGKTY--G 87
Cdd:COG4891     2 EIEIDAPPERVWQVLTDFPSYPEWNPFI--RSIEGELRVGARLTLRLrppggRPMTFRPRVTEVEPNRELRWRGKLLlpG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082599077  88 L-SAVHNWTLTET-NGQTNVSVDESMEGFFAGLLKKPFSKNLEKGMQ--NWldLLKQECEK 144
Cdd:COG4891    80 LfDGEHYFELEPLgDGRTRFIHRETFSGLLVPLFLKSLREDTRRGFEamNQ--ALKERAEA 138
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 15-143 2.60e-09

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: 52.10  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  15 TITINANSEKVWAVMTNINNWATWQTDISKPKLNGELKPETTFDWKT--GGVK--IHSTLHTVEP-FKKLGWTG--KTYG 87
Cdd:pfam10604   2 SIEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGGPLRGVVGTLrvGGRRgtVREELVEYDPaPRLLAYRIvePLGV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082599077  88 LSAVHNWTLTETNGQTNVSVDESMEG------FFAGLLKKPFSKNLEKGMQNwldlLKQECE 143
Cdd:pfam10604  82 ANYVGTWTVTPAGGGTRVTWTGEFDGpplggpFRDPAAARAVKGDYRAGLDR----LKAVLE 139
 
Name Accession Description Interval E-value
SRPBCC_Smu440-like cd08862
Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins; This family ...
 10-144 1.09e-23

Ligand-binding SRPBCC domain of Streptococcus mutans Smu.440 and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Streptococcus mutans Smu.440 and related proteins. This domain belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Streptococcus mutans is a dental pathogen, and the leading cause of dental caries. In this pathogen, the gene encoding Smu.440 is in the same operon as the gene encoding SMU.441, a member of the MarR protein family of transcriptional regulators involved in multiple antibiotic resistance. It has been suggested that SMU.440 is involved in polyketide-like antibiotic resistance.


Pssm-ID: 176871  Cd Length: 138  Bit Score: 89.34  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  10 VKCSKTITINANSEKVWAVMTNINNWATWQTDISKPKLNGE-LKPETTFDWK-TGGVKIHSTLHTVEPFKKLGWTGKTYG 87
Cdd:cd08862     1 MKFEATIVIDAPPERVWAVLTDVENWPAWTPSVETVRLEGPpPAVGSSFKMKpPGLVRSTFTVTELRPGHSFTWTGPAPG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1082599077  88 LSAVHNWTLTETN-GQTNVSVDESMEGFFAGLLKKPFSKNLEKGMQNWLDLLKQECEK 144
Cdd:cd08862    81 ISAVHRHEFEAKPdGGVRVTTSESLSGPLAFLFGLFVGKKLRALLPEWLEGLKAAAEQ 138
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 13-143 1.19e-16

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.


Pssm-ID: 176864  Cd Length: 141  Bit Score: 71.20  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  13 SKTITINANSEKVWAVMTNINNWATWQTDIskPKLNG-ELKPETTFDWKT-----GGVKIHSTLHTVEPFKKLGWTGK-- 84
Cdd:cd07822     3 STEIEINAPPEKVWEVLTDFPSYPEWNPFV--RSATGlSLALGARLRFVVklpggPPRSFKPRVTEVEPPRRLAWRGGlp 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082599077  85 -TYGLSAVHNWTLTETN-GQTNVSVDESMEGFFAGLLKKPFSKNLEKGMQNWLDLLKQECE 143
Cdd:cd07822    81 fPGLLDGEHSFELEPLGdGGTRFVHRETFSGLLAPLVLLGLGRDLRAGFEAMNEALKARAE 141
COG4891 COG4891
Uncharacterized conserved protein [Function unknown];
15-144 1.76e-11

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443919  Cd Length: 138  Bit Score: 57.62  E-value: 1.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  15 TITINANSEKVWAVMTNINNWATWQTDIskPKLNGELKPETTFDWKT-----GGVKIHSTLHTVEPFKKLGWTGKTY--G 87
Cdd:COG4891     2 EIEIDAPPERVWQVLTDFPSYPEWNPFI--RSIEGELRVGARLTLRLrppggRPMTFRPRVTEVEPNRELRWRGKLLlpG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082599077  88 L-SAVHNWTLTET-NGQTNVSVDESMEGFFAGLLKKPFSKNLEKGMQ--NWldLLKQECEK 144
Cdd:COG4891    80 LfDGEHYFELEPLgDGRTRFIHRETFSGLLVPLFLKSLREDTRRGFEamNQ--ALKERAEA 138
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 14-144 1.39e-09

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.


Pssm-ID: 176856 [Multi-domain]  Cd Length: 139  Bit Score: 52.75  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  14 KTITINANSEKVWAVMTNINNWATWQTDISKPklNGELKP--ETTFDWKTGGVK---IHSTLHTVEPFKKLGWT----GK 84
Cdd:cd07814     4 IEREFDAPPELVWRALTDPELLAQWFGPTTTA--EMDLRVggRWFFFMTGPDGEegwVSGEVLEVEPPRRLVFTwafsDE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  85 TYGLSAVHNWTLTETNGQTNVSVDESmeGFFAGLLKKPFSKNLEKGMQNWLDLLKQECEK 144
Cdd:cd07814    82 TPGPETTVTVTLEETGGGTRLTLTHS--GFPEEDAEQEAREGMEEGWTGTLDRLKALLEK 139
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 15-143 2.60e-09

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: 52.10  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  15 TITINANSEKVWAVMTNINNWATWQTDISKPKLNGELKPETTFDWKT--GGVK--IHSTLHTVEP-FKKLGWTG--KTYG 87
Cdd:pfam10604   2 SIEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGGPLRGVVGTLrvGGRRgtVREELVEYDPaPRLLAYRIvePLGV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082599077  88 LSAVHNWTLTETNGQTNVSVDESMEG------FFAGLLKKPFSKNLEKGMQNwldlLKQECE 143
Cdd:pfam10604  82 ANYVGTWTVTPAGGGTRVTWTGEFDGpplggpFRDPAAARAVKGDYRAGLDR----LKAVLE 139
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 15-142 1.15e-07

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.


Pssm-ID: 176854  Cd Length: 141  Bit Score: 47.70  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  15 TITINANSEKVWAVMTNINNWATWQTDI--SKPKLNGELKPETTFDWKTGGVKIHSTLHTV------EPFkKLGWTGKTY 86
Cdd:cd07812     4 SIEIPAPPEAVWDLLSDPERWPEWSPGLerVEVLGGGEGGVGARFVGGRKGGRRLTLTSEVtevdppRPG-RFRVTGGGG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1082599077  87 GLSAVHNWTLTET-NGQTNVSVDESME--GFFAGLLKKPFSKNLEKGMQNWLDLLKQEC 142
Cdd:cd07812    83 GVDGTGEWRLEPEgDGGTRVTYTVEYDppGPLLKVFALLLAGALKRELAALLRALKARL 141
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 15-139 1.23e-05

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 42.33  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  15 TITINANSEKVWAVMTN---INNWatWQTDISKPKLNGELKPETTFDWKTGG-----VKIHSTLHTVEPFKKLGWT---- 82
Cdd:COG3832    11 EREIDAPPERVWRAWTDpelLARW--FGPKGWATVAEFDLRVGGRFRFRMRGpdgeeFGFEGEVLEVEPPERLVFTwgfe 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1082599077  83 GKTYGLSAVHnWTLTETNGQTNVSVDEsmEGFFAGLLKKPFSKNLEKGMQNWLDLLK 139
Cdd:COG3832    89 DDPEGESTVT-VTLEPEGGGTRLTLTH--TGFSAEDRDAVLAEGMEEGWTESLDRLK 142
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 10-129 4.57e-04

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.


Pssm-ID: 176861  Cd Length: 140  Bit Score: 37.99  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  10 VKCSKTITINANSEKVWAVMTNINNWATWQTDISKpklngeLKPETTFD---W-------KTGGVK-IHSTLHTVEPFKK 78
Cdd:cd07819     2 IKVSREFEIEAPPAAVMDVLADVEAYPEWSPKVKS------VEVLLRDNdgrPemvrigvGAYGIKdTYALEYTWDGAGS 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082599077  79 LGWTG-KTYGLSAVH-NWTLTETNGQTNVSVDESME------GFF----AGLLKKPFSKNLEK 129
Cdd:cd07819    76 VSWTLvEGEGNRSQEgSYTLTPKGDGTRVTFDLTVEltvplpGFLkrkaEPLVLDEALKGLKK 138
SRPBCC_1 cd07818
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 13-144 6.33e-04

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.


Pssm-ID: 176860  Cd Length: 150  Bit Score: 37.63  E-value: 6.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  13 SKTITINANSEKVWAVMTNINNWATWQtdiskPKLNGELKPETTFDWKTGGV--------------------------KI 66
Cdd:cd07818     5 ERSIVINAPPEEVFPYVNDLKNWPEWS-----PWEKLDPDMKRTYSGPDSGVgasyswegndkvgegemeitesvpneRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  67 HSTLHTVEPFKKlgwtgktyglSAVHNWTLTETNGQTNVSVdeSMEG---------FFAGLLKKPFSKNLEKGMQNwldl 137
Cdd:cd07818    80 EYELRFIKPFEA----------TNDVEFTLEPVGGGTKVTW--GMSGelpfplklmYLFLDMDKMIGKDFEKGLAN---- 143


                  ....*..
gi 1082599077 138 LKQECEK 144
Cdd:cd07818   144 LKAVLEK 150
COG5637 COG5637
Uncharacterized protein, contains SRPBCC domain [Function unknown];
13-143 1.32e-03

Uncharacterized protein, contains SRPBCC domain [Function unknown];


Pssm-ID: 444363  Cd Length: 154  Bit Score: 36.81  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082599077  13 SKTITINANSEKVWAVMTNINNWATWQTDISkpklngELKP--ETTFDWKT---GGVKIHSTLHTVE--PFKKLGWTGKT 85
Cdd:COG5637     5 EKSITINAPVEEVYAYWRDFENLPRFMKGVE------SVTVldDTRSHWVAkgpLGVTVEWDAEITEqvPGERIAWRSVE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082599077  86 YGLSavHNWTLT---ETNGQTNVSVdeSME-----GFFAGLLKKPFSKNLEKGMQNWLDLLKQECE 143
Cdd:COG5637    79 GDIP--NAGVVRfepAGGRGTRVTV--TIEydppgGLLGKALAKLFGGVPERQLREDLERFKQLIE 140
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 10-56 4.19e-03

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: 35.38  E-value: 4.19e-03
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                  ....*....|....*....|....*....|....*....|....*...
gi 1082599077  10 VKCSKTITINANSEKVWAVMTNINNWATWQTDISKPKL-NGELKPETT 56
Cdd:cd07821     1 AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVASCELeGGGPGVGAV 48
 
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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