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Conserved domains on  [gi|808688327|ref|NP_001294988|]
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stAR-related lipid transfer protein 4 isoform c [Homo sapiens]

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 ...
 1-123 3.44e-93

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 cd08902:

Pssm-ID: 472699  Cd Length: 202  Bit Score: 267.21  E-value: 3.44e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327   1 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRPEFVRGYNHPCGWFCVPLKD 80
Cdd:cd08902   79 MTSMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKD 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 808688327  81 NPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:cd08902  159 NPSHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKAL 201
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 1-123 3.44e-93

Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4 and related domains. It belongs to the START domain family, and in turn 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. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7alpha-hydroxycholesterol. STARD4 is ubiquitously expressed, with highest levels in liver and kidney.


Pssm-ID: 176911  Cd Length: 202  Bit Score: 267.21  E-value: 3.44e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327   1 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRPEFVRGYNHPCGWFCVPLKD 80
Cdd:cd08902   79 MTSMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKD 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 808688327  81 NPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:cd08902  159 NPSHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKAL 201
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 1-123 1.12e-09

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 53.59  E-value: 1.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327     1 MTSLDILENFEENCCVMRYTTAGQlWNIISPREFVDFSYT-VGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV- 76
Cdd:smart00234  77 VAKAETLEVIDNGTVIYHYVSKFA-AGPVSPRDFVFVRYWrEDEDGSYAVVDVSVTHPTSPPEsgYVRAENLPSG-LLIe 154

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 808688327    77 PLKDNPnqSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:smart00234 155 PLGNGP--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATL 199
START pfam01852
START domain;
1-123 3.84e-08

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 49.32  E-value: 3.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327    1 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSY-TVGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV- 76
Cdd:pfam01852  76 VRSAETLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYwRRLGGGVYVIVDRSVTHPQFPPSsgYVRAERLPSG-YLIq 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 808688327   77 PLKDNPnqSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:pfam01852 155 PCGNGP--SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATL 199
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 1-123 3.44e-93

Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4 and related domains. It belongs to the START domain family, and in turn 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. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7alpha-hydroxycholesterol. STARD4 is ubiquitously expressed, with highest levels in liver and kidney.


Pssm-ID: 176911  Cd Length: 202  Bit Score: 267.21  E-value: 3.44e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327   1 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRPEFVRGYNHPCGWFCVPLKD 80
Cdd:cd08902   79 MTSMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKD 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 808688327  81 NPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:cd08902  159 NPSHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKAL 201
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 1-123 4.15e-67

Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4, -5, and -6. 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. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7a-hydroxycholesterol. STARD4 and STARD5 are ubiquitously expressed, with highest levels in liver and kidney. STRAD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176876  Cd Length: 206  Bit Score: 201.15  E-value: 4.15e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327   1 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEG-LLSCGISLDWDEKRP--EFVRGYNHPCGWFCVP 77
Cdd:cd08867   80 LKHYEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNqWSSSGKSVDIPERPPtpGFVRGYNHPCGYFCSP 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 808688327  78 LKDNPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:cd08867  160 LKGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGV 205
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 1-123 4.94e-28

Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD5, and related domains. It belongs to the START domain family, and in turn 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. STARD5 is ubiquitously expressed, with highest levels in liver and kidney. STARD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy.


Pssm-ID: 176912  Cd Length: 208  Bit Score: 101.84  E-value: 4.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327   1 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEG-LLSCGISLDWDEKRPE--FVRGYNHPCGWFCVP 77
Cdd:cd08903   80 VKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGtISSNATNVEHPLCPPQagFVRGFNHPCGCFCEP 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 808688327  78 LKDNPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:cd08903  160 VPGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAV 205
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 1-123 1.76e-23

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: 89.70  E-value: 1.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327   1 MTSLDILENFEENCCVMRYTTAGQLwnIISPREFVDFSYTVGYKEGL-LSCGISLDWD--EKRPEFVRGYNHPCGWFCVP 77
Cdd:cd00177   71 FEEFEVIEEIDEHTDIIYYKTKPPW--PVSPRDFVYLRRRRKLDDGTyVIVSKSVDHDshPKEKGYVRAEIKLSGWIIEP 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 808688327  78 LkdNPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:cd00177  149 L--DPGKTKVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAK 192
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 29-120 2.55e-23

Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD6 and related domains. It belongs to the START domain family, and in turn 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. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176913  Cd Length: 204  Bit Score: 89.58  E-value: 2.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327  29 ISPREFVDFSYtVGYKEGLLS--CGISLDWDEKRPE--FVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDLRGMIPQSAV 104
Cdd:cd08904  106 ISPRDFVDLVH-IKRYEGNMNivSSVSVEYPQCPPSsnYIRGYNHPCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVI 184

                         90
                 ....*....|....*.
gi 808688327 105 DTAMASTLTNFYGDLR 120
Cdd:cd08904  185 EKTMPTNLVNLILDAK 200
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 2-121 7.72e-20

Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). 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. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176877  Cd Length: 208  Bit Score: 80.48  E-value: 7.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327   2 TSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDE--KRPEFVRGYNHPCGWFCVPLK 79
Cdd:cd08868   82 LECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAmpPTKNYVRGENGPGCWILRPLP 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 808688327  80 DNPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRK 121
Cdd:cd08868  162 NNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRK 203
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 1-123 8.16e-16

Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD3 (also known as metastatic lymph node 64/MLN64) and related proteins. It belongs to the START domain family, and in turn 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. STARD3 has a high affinity for cholesterol. It may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176915  Cd Length: 209  Bit Score: 69.89  E-value: 8.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327   1 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRP--EFVRGYNHPCGWFCVPL 78
Cdd:cd08906   82 VSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPlsKYVRGENGPGGFVVLKS 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 808688327  79 KDNPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:cd08906  162 ASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRI 206
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 6-123 1.08e-11

Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and related proteins. It belongs to the START domain family, and in turn 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. STARD1 has a high affinity for cholesterol. It can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads.


Pssm-ID: 176914  Cd Length: 209  Bit Score: 59.08  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327   6 ILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRP--EFVRGYNHPCGWFCVPLKDNPN 83
Cdd:cd08905   87 ILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEqkGFIRAENGPTCIVLRPLAGDPS 166

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 808688327  84 QSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:cd08905  167 KTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRM 206
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 1-123 1.12e-09

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 53.59  E-value: 1.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327     1 MTSLDILENFEENCCVMRYTTAGQlWNIISPREFVDFSYT-VGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV- 76
Cdd:smart00234  77 VAKAETLEVIDNGTVIYHYVSKFA-AGPVSPRDFVFVRYWrEDEDGSYAVVDVSVTHPTSPPEsgYVRAENLPSG-LLIe 154

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 808688327    77 PLKDNPnqSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:smart00234 155 PLGNGP--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATL 199
START pfam01852
START domain;
1-123 3.84e-08

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 49.32  E-value: 3.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688327    1 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSY-TVGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV- 76
Cdd:pfam01852  76 VRSAETLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYwRRLGGGVYVIVDRSVTHPQFPPSsgYVRAERLPSG-YLIq 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 808688327   77 PLKDNPnqSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 123
Cdd:pfam01852 155 PCGNGP--SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATL 199
 
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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