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Conserved domains on  [gi|1184681970|ref|WP_085241945|]
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SRPBCC family protein [Mycobacterium europaeum]

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 ...
 2-145 4.84e-17

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: 72.36  E-value: 4.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   2 ADIHGTRTIAARIGDVWETLADFGSISSWAGNVDhSCILYSGPDGadVGTARRVQVK-RDTLVERITEFDPP-RALGYDI 79
Cdd:cd07821     1 AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVA-SCELEGGGPG--VGAVRTVTLKdGGTVRERLLALDDAeRRYSYRI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184681970  80 EGFPRRLRRVSNRWTLAPSAAM-TLVTLTSTVEVGPHATQKAAEHLLCRFLarqsEAMLAGLANRLE 145
Cdd:cd07821    78 VEGPLPVKNYVATIRVTPEGDGgTRVTWTAEFDPPEGLTDELARAFLTGVY----RAGLAALKAALE 140
 
Name Accession Description Interval E-value
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 2-145 4.84e-17

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: 72.36  E-value: 4.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   2 ADIHGTRTIAARIGDVWETLADFGSISSWAGNVDhSCILYSGPDGadVGTARRVQVK-RDTLVERITEFDPP-RALGYDI 79
Cdd:cd07821     1 AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVA-SCELEGGGPG--VGAVRTVTLKdGGTVRERLLALDDAeRRYSYRI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184681970  80 EGFPRRLRRVSNRWTLAPSAAM-TLVTLTSTVEVGPHATQKAAEHLLCRFLarqsEAMLAGLANRLE 145
Cdd:cd07821    78 VEGPLPVKNYVATIRVTPEGDGgTRVTWTAEFDPPEGLTDELARAFLTGVY----RAGLAALKAALE 140
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 7-145 2.67e-15

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: 67.90  E-value: 2.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   7 TRTIAARIGDVWETLADFGSISSWAGNVDHSCILYSGPDGADVGTARRVQVKRDTLVERITEFDP-PRALGYDIeGFPRR 85
Cdd:pfam10604   2 SIEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGGPLRGVVGTLRVGGRRGTVREELVEYDPaPRLLAYRI-VEPLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970  86 LRRVSNRWTLAPSAAMTLVTLTSTVEVGPhATQKAAEHLLCRFLARQSEAMLAGLANRLE 145
Cdd:pfam10604  81 VANYVGTWTVTPAGGGTRVTWTGEFDGPP-LGGPFRDPAAARAVKGDYRAGLDRLKAVLE 139
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-143 1.38e-05

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 42.16  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   1 MADIHGTRTIAARIGDVWETLADFGSISSWAGNVDHSCILYSGPDG--ADVGTARRvqVKRDTLVERITeFDPPRALGYD 78
Cdd:COG2867     1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEvvAELTVSFK--GLRESFTTRNT-LDPPERIDFE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184681970  79 -IEGfPrrLRRVSNRWTLAP-SAAMTLVTLTSTVEVGPHATQKAAEhllcRFLARQSEAMLAGLANR 143
Cdd:COG2867    78 lVDG-P--FKHLEGRWRFEPlGEGGTKVTFDLDFEFKSPLLGALLG----PVFNEAARRMVDAFKKR 137
 
Name Accession Description Interval E-value
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 2-145 4.84e-17

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: 72.36  E-value: 4.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   2 ADIHGTRTIAARIGDVWETLADFGSISSWAGNVDhSCILYSGPDGadVGTARRVQVK-RDTLVERITEFDPP-RALGYDI 79
Cdd:cd07821     1 AKVTVSVTIDAPADKVWALLSDFGGLHKWHPAVA-SCELEGGGPG--VGAVRTVTLKdGGTVRERLLALDDAeRRYSYRI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184681970  80 EGFPRRLRRVSNRWTLAPSAAM-TLVTLTSTVEVGPHATQKAAEHLLCRFLarqsEAMLAGLANRLE 145
Cdd:cd07821    78 VEGPLPVKNYVATIRVTPEGDGgTRVTWTAEFDPPEGLTDELARAFLTGVY----RAGLAALKAALE 140
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 7-145 2.67e-15

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: 67.90  E-value: 2.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   7 TRTIAARIGDVWETLADFGSISSWAGNVDHSCILYSGPDGADVGTARRVQVKRDTLVERITEFDP-PRALGYDIeGFPRR 85
Cdd:pfam10604   2 SIEIAAPPEQVWALLSDFENWPRWHPGVLRVELEGGGGPLRGVVGTLRVGGRRGTVREELVEYDPaPRLLAYRI-VEPLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970  86 LRRVSNRWTLAPSAAMTLVTLTSTVEVGPhATQKAAEHLLCRFLARQSEAMLAGLANRLE 145
Cdd:pfam10604  81 VANYVGTWTVTPAGGGTRVTWTGEFDGPP-LGGPFRDPAAARAVKGDYRAGLDRLKAVLE 139
SRPBCC_4 cd07822
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 4-145 1.91e-07

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: 47.32  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   4 IHGTRTIAARIGDVWETLADFGSISSWagnvdHSCILYSGPDGADVGTARRVQVKRDTL-----VERITEFDPPRALGYD 78
Cdd:cd07822     2 ISTEIEINAPPEKVWEVLTDFPSYPEW-----NPFVRSATGLSLALGARLRFVVKLPGGpprsfKPRVTEVEPPRRLAWR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184681970  79 IEGFPRRLRRVSNRWTLAPSAAMTLVTLTSTVEVGPHAtqKAAEHLLCRFLARQSEAMLAGLANRLE 145
Cdd:cd07822    77 GGLPFPGLLDGEHSFELEPLGDGGTRFVHRETFSGLLA--PLVLLGLGRDLRAGFEAMNEALKARAE 141
SRPBCC_10 cd08865
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 4-145 4.95e-07

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: 176874  Cd Length: 140  Bit Score: 46.12  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   4 IHGTRTIAARIGDVWETLADFGSISSWAGNVDHSCILYSGPDGadVGT----ARRVQVKRDTLVERITEFDPPRalgydi 79
Cdd:cd08865     1 VEESIVIERPVEEVFAYLADFENAPEWDPGVVEVEKITDGPVG--VGTryhqVRKFLGRRIELTYEITEYEPGR------ 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184681970  80 egfpRRLRRVSNrwTLAPSAAMTLVT-------LTSTVEVGPHATQKAAEHLLCRFLARQSEAMLAGLANRLE 145
Cdd:cd08865    73 ----RVVFRGSS--GPFPYEDTYTFEpvgggtrVRYTAELEPGGFARLLDPLMAPAFRRRARAALENLKALLE 139
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 4-144 1.51e-06

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: 45.01  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   4 IHGTRTIAARIGDVWETLADFGSISSWAGNVDHSCILYSGPDGA-DVGTARRVQVKRDTLVERITEFDPPRALGYDIEGF 82
Cdd:cd07812     1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVLGGGEGGVgARFVGGRKGGRRLTLTSEVTEVDPPRPGRFRVTGG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184681970  83 PRRLrRVSNRWTLAPSAAM-TLVTLTSTVEVGPHATQKAAEhLLCRFLARQSEAMLAGLANRL 144
Cdd:cd07812    81 GGGV-DGTGEWRLEPEGDGgTRVTYTVEYDPPGPLLKVFAL-LLAGALKRELAALLRALKARL 141
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 1-143 1.38e-05

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 42.16  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   1 MADIHGTRTIAARIGDVWETLADFGSISSWAGNVDHSCILYSGPDG--ADVGTARRvqVKRDTLVERITeFDPPRALGYD 78
Cdd:COG2867     1 MPTISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGDEvvAELTVSFK--GLRESFTTRNT-LDPPERIDFE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184681970  79 -IEGfPrrLRRVSNRWTLAP-SAAMTLVTLTSTVEVGPHATQKAAEhllcRFLARQSEAMLAGLANR 143
Cdd:COG2867    78 lVDG-P--FKHLEGRWRFEPlGEGGTKVTFDLDFEFKSPLLGALLG----PVFNEAARRMVDAFKKR 137
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 4-112 1.43e-05

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: 42.23  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   4 IHGTRT--IAARIGDVWETLADFGSISSWAGNVDHSCILysgpDGADVGTARRVQVK------RDTLVERITeFDPPRAL 75
Cdd:cd07819     2 IKVSREfeIEAPPAAVMDVLADVEAYPEWSPKVKSVEVL----LRDNDGRPEMVRIGvgaygiKDTYALEYT-WDGAGSV 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1184681970  76 GYDIEGfPRRLRRVSNRWTLAPSAAMTLVTLTSTVEV 112
Cdd:cd07819    77 SWTLVE-GEGNRSQEGSYTLTPKGDGTRVTFDLTVEL 112
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 10-114 2.29e-05

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. The family also includes proteins which are involved in the binding/transport of lipids.


Pssm-ID: 397441  Cd Length: 125  Bit Score: 41.33  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970  10 IAARIGDVWETLADFGSISSWAGNVDHSCILYSGPDGADVGTARrvQVKRDTLVERITEFDPPRALGYDIEGFPRRLRrv 89
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLERDGSLADWRVAF--GGLRRSFTARVTLQPPERIEMVLVDGDFKRLE-- 76

                          90       100
                  ....*....|....*....|....*
gi 1184681970  90 sNRWTLAPSAAMTLVTLTSTVEVGP 114
Cdd:pfam03364  77 -GSWRFEPGGPGTRVKVTLELDFEF 100
YndB COG3832
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ...
 1-123 2.49e-04

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


Pssm-ID: 443044 [Multi-domain]  Cd Length: 142  Bit Score: 38.87  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   1 MADIHGTRTIAARIGDVWETLADFGSISSWAGNvDHSCILYSGPdgADVGTARRVQVKRDTLVE-----RITEFDPPRAL 75
Cdd:COG3832     5 DRTITIEREIDAPPERVWRAWTDPELLARWFGP-KGWATVAEFD--LRVGGRFRFRMRGPDGEEfgfegEVLEVEPPERL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184681970  76 GY--DIEGFPRRLRRVsnRWTLAPSAAMTLVTLTSTVEVGPHATQKAAEH 123
Cdd:COG3832    82 VFtwGFEDDPEGESTV--TVTLEPEGGGTRLTLTHTGFSAEDRDAVLAEG 129
SRPBCC_1 cd07818
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 7-142 2.63e-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: 38.79  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   7 TRTIAARIGDVWETLADF---GSISSWAgNVDHSCIL-YSGPD---GA--------DVGTARrvqvkrdtlvERITEFDP 71
Cdd:cd07818     7 SIVINAPPEEVFPYVNDLknwPEWSPWE-KLDPDMKRtYSGPDsgvGAsyswegndKVGEGE----------MEITESVP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184681970  72 PRALGYDIEgFPRRLRRVSN-RWTLAPSAAMTLVTLTSTVEVGPhatqkaaeHLLCRFLARQSEAML-----AGLAN 142
Cdd:cd07818    76 NERIEYELR-FIKPFEATNDvEFTLEPVGGGTKVTWGMSGELPF--------PLKLMYLFLDMDKMIgkdfeKGLAN 143
SRPBCC_6 cd07824
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 3-112 4.04e-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: 176866  Cd Length: 146  Bit Score: 38.45  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   3 DIHGTRTIAARIGDVWETLADFGSISSWAGNVDHSCILYSGpDGADVGTARRVQVK-----RDTLVERITEFDPPRAL-- 75
Cdd:cd07824     2 RFHTVWRIPAPPEAVWDVLVDAESWPDWWPGVERVVELEPG-DEAGIGARRRYTWRgllpyRLRFELRVTRIEPLSLLev 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1184681970  76 --GYDIEGfprrlrrvSNRWTLAPSAAMTLVTLTSTVEV 112
Cdd:cd07824    81 raSGDLEG--------VGRWTLAPDGSGTVVRYDWEVRT 111
SRPBCC_CalC_Aha1-like_6 cd08899
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 7-121 7.85e-04

Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins; SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.


Pssm-ID: 176908 [Multi-domain]  Cd Length: 157  Bit Score: 37.66  E-value: 7.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   7 TRTIAARIGDVWETLADFGSISSWAGNVDhscilysgpdgADVGTARRVQVK-----RDTLVERITEFDPPRALGY--DI 79
Cdd:cd08899    16 ERLLPAPIEDVWAALTDPERLARWFAPGT-----------GDLRVGGRVEFVmddeeGPNATGTILACEPPRLLAFtwGE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1184681970  80 EGFPRRLrrvsnRWTLAPSAAMTLVTLTSTVEVGPHATQKAA 121
Cdd:cd08899    85 GGGESEV-----RFELAPEGDGTRLTLTHRLLDERFGAGAVG 121
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 3-123 1.96e-03

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: 36.19  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   3 DIHGTRTIAARIGDVWETLADFGSISSWAGNVDHSCIlysgpDGADVGTARRVQVKRDTLVE----RITEFDPPRALGY- 77
Cdd:cd07814     1 TITIEREFDAPPELVWRALTDPELLAQWFGPTTTAEM-----DLRVGGRWFFFMTGPDGEEGwvsgEVLEVEPPRRLVFt 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1184681970  78 DIEGFPRRLRRVSNRWTLAPSAAMTLVTLTSTVEVGPHATQKAAEH 123
Cdd:cd07814    76 WAFSDETPGPETTVTVTLEETGGGTRLTLTHSGFPEEDAEQEAREG 121
SRPBCC_7 cd07825
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 7-145 7.01e-03

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: 176867  Cd Length: 144  Bit Score: 34.63  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184681970   7 TRTIAARIGDVWETLADFGSISSW--AGNVdHSCIlySGPDGADVGTARRVQVKRD----TLVERITEFDPPRALGY--- 77
Cdd:cd07825     5 SRTVDAPAEAVFAVLADPRRHPEIdgSGTV-REAI--DGPRILAVGDVFRMAMRLDggpyRITNHVVAFEENRLIAWrpg 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184681970  78 --DIEGFPRRLrrvsnRWTLAPSA-AMTLVTLTSTVevgpHATQKAAEHL-LCRFLARQSEAMLAGLANRLE 145
Cdd:cd07825    82 paGQEPGGHRW-----RWELEPIGpGRTRVTETYDW----SAVTDLKELLgFPAFPEVQLEASLDRLATLAE 144
 
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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