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Conserved domains on  [gi|1063730285|ref|NP_001332440|]
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polyketide cyclase/dehydrase/lipid transport superfamily protein [Arabidopsis thaliana]

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 ...
 1-186 1.06e-55

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 cd08877:

Pssm-ID: 472699  Cd Length: 215  Bit Score: 182.11  E-value: 1.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730285   1 MYREGLDGsPFHTLLVEGYMDGPIHECLCVSWESTLYKKWWPqyafppFRILKSTCLQKvGVGEQICLARMKVPWPLTER 80
Cdd:cd08877    36 YYKFEPDG-SLLSLRMEGEIDGPLFNLLALLNEVELYKTWVP------FCIRSKKVKQL-GRADKVCYLRVDLPWPLSNR 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730285  81 EMILHYFSFEYF-KDGLVVILLNTISDLNSIGvSSTDIIIPESP--DAVRMDLVGGFVLQKVTPQRSYFRTIGDMDIKLD 157
Cdd:cd08877   108 EAVFRGFGVDRLeENGQIVILLKSIDDDPEFL-KLTDLDIPSTSakGVRRIIKYYGFVITPISPTKCYLRFVANVDPKMS 186

                         170       180
                  ....*....|....*....|....*....
gi 1063730285 158 LMPPSLMNFISRQLIGNGFRLYKKSVASV 186
Cdd:cd08877   187 LVPKSLLNFVARKFAGLLFEKIQKAAKNV 215
 
Name Accession Description Interval E-value
START_2 cd08877
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 1-186 1.06e-55

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain 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. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176886  Cd Length: 215  Bit Score: 182.11  E-value: 1.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730285   1 MYREGLDGsPFHTLLVEGYMDGPIHECLCVSWESTLYKKWWPqyafppFRILKSTCLQKvGVGEQICLARMKVPWPLTER 80
Cdd:cd08877    36 YYKFEPDG-SLLSLRMEGEIDGPLFNLLALLNEVELYKTWVP------FCIRSKKVKQL-GRADKVCYLRVDLPWPLSNR 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730285  81 EMILHYFSFEYF-KDGLVVILLNTISDLNSIGvSSTDIIIPESP--DAVRMDLVGGFVLQKVTPQRSYFRTIGDMDIKLD 157
Cdd:cd08877   108 EAVFRGFGVDRLeENGQIVILLKSIDDDPEFL-KLTDLDIPSTSakGVRRIIKYYGFVITPISPTKCYLRFVANVDPKMS 186

                         170       180
                  ....*....|....*....|....*....
gi 1063730285 158 LMPPSLMNFISRQLIGNGFRLYKKSVASV 186
Cdd:cd08877   187 LVPKSLLNFVARKFAGLLFEKIQKAAKNV 215
 
Name Accession Description Interval E-value
START_2 cd08877
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 1-186 1.06e-55

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain 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. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176886  Cd Length: 215  Bit Score: 182.11  E-value: 1.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730285   1 MYREGLDGsPFHTLLVEGYMDGPIHECLCVSWESTLYKKWWPqyafppFRILKSTCLQKvGVGEQICLARMKVPWPLTER 80
Cdd:cd08877    36 YYKFEPDG-SLLSLRMEGEIDGPLFNLLALLNEVELYKTWVP------FCIRSKKVKQL-GRADKVCYLRVDLPWPLSNR 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730285  81 EMILHYFSFEYF-KDGLVVILLNTISDLNSIGvSSTDIIIPESP--DAVRMDLVGGFVLQKVTPQRSYFRTIGDMDIKLD 157
Cdd:cd08877   108 EAVFRGFGVDRLeENGQIVILLKSIDDDPEFL-KLTDLDIPSTSakGVRRIIKYYGFVITPISPTKCYLRFVANVDPKMS 186

                         170       180
                  ....*....|....*....|....*....
gi 1063730285 158 LMPPSLMNFISRQLIGNGFRLYKKSVASV 186
Cdd:cd08877   187 LVPKSLLNFVARKFAGLLFEKIQKAAKNV 215
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 1-173 1.70e-08

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This 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. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 53.88  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730285   1 MYREGLDGSPFHTLLVEGYMDGPIHECLCVSWESTLYKKWWPQyafppfrILKSTCLQKVGVGEQICLARMKVPWPLTER 80
Cdd:cd00177    28 IYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKN-------FEEFEVIEEIDEHTDIIYYKTKPPWPVSPR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730285  81 EMILhYFSFEYFKDGLVVIllntisdlnsIGVSSTDIIIPESPDAVRMDL-VGGFVLQKVTPQRSYFRTIGDMDIKLDLm 159
Cdd:cd00177   101 DFVY-LRRRRKLDDGTYVI----------VSKSVDHDSHPKEKGYVRAEIkLSGWIIEPLDPGKTKVTYVLQVDPKGSI- 168

                         170
                  ....*....|....*
gi 1063730285 160 PPSLMN-FISRQLIG 173
Cdd:cd00177   169 PKSLVNsAAKKQLAS 183
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 74-177 6.63e-05

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain 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. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176885  Cd Length: 195  Bit Score: 43.41  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730285  74 PWPLTEREMILHyFSFEY-FKDGLVVILLNTISDLnsigvsstdiiIPESPDAVRMDLVGG-FVLQKVTPQRSYFRTIGD 151
Cdd:cd08876    96 PWPVKDRDMVLR-STTEQdADDGSVTITLEAAPEA-----------LPEQKGYVRIKTVEGqWTFTPLGNGKTRVTYQAY 163

                          90       100
                  ....*....|....*....|....*.
gi 1063730285 152 MDIKLDLmPPSLMNFISRQLIGNGFR 177
Cdd:cd08876   164 ADPGGSI-PGWLANAFAKDAPYNTLE 188
 
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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