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Conserved domains on  [gi|1034643615|ref|XP_016864532|]
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stAR-related lipid transfer protein 4 isoform X3 [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 ...
 1-107 2.40e-80

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: 233.69  E-value: 2.40e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615   1 MRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRPEFVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDLR 80
Cdd:cd08902    95 MRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKDNPSHSLLTGYIQTDLR 174

                          90       100
                  ....*....|....*....|....*..
gi 1034643615  81 GMIPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:cd08902   175 GMLPQSAVDTAMASTLVNFYSDLKKAL 201
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 1-107 2.40e-80

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: 233.69  E-value: 2.40e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615   1 MRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRPEFVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDLR 80
Cdd:cd08902    95 MRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKDNPSHSLLTGYIQTDLR 174

                          90       100
                  ....*....|....*....|....*..
gi 1034643615  81 GMIPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:cd08902   175 GMLPQSAVDTAMASTLVNFYSDLKKAL 201
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 3-107 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: 52.82  E-value: 1.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615    3 YTTAGQLWNIISPREFVDFSYT-VGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV-PLKDNPnqSLLTGYIQTD 78
Cdd:smart00234  94 HYVSKFAAGPVSPRDFVFVRYWrEDEDGSYAVVDVSVTHPTSPPEsgYVRAENLPSG-LLIePLGNGP--SKVTWVSHAD 170

                           90       100
                   ....*....|....*....|....*....
gi 1034643615   79 LRGMIPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:smart00234 171 LKGWLPHWLVRSLIKSGLAEFAKTLVATL 199
START pfam01852
START domain;
3-107 7.40e-08

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 48.17  E-value: 7.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615   3 YTTAGQLWNIISPREFVDFSY-TVGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV-PLKDNPnqSLLTGYIQTD 78
Cdd:pfam01852  94 YVAALVAPSPLSPRDFVFLRYwRRLGGGVYVIVDRSVTHPQFPPSsgYVRAERLPSG-YLIqPCGNGP--SKVTWVSHAD 170

                          90       100
                  ....*....|....*....|....*....
gi 1034643615  79 LRGMIPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:pfam01852 171 LKGWLPSWLLRSLYKSGMPEGAKTWVATL 199
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 1-107 2.40e-80

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: 233.69  E-value: 2.40e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615   1 MRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRPEFVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDLR 80
Cdd:cd08902    95 MRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKDNPSHSLLTGYIQTDLR 174

                          90       100
                  ....*....|....*....|....*..
gi 1034643615  81 GMIPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:cd08902   175 GMLPQSAVDTAMASTLVNFYSDLKKAL 201
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 1-107 3.00e-57

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: 175.34  E-value: 3.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615   1 MRYTTAGQLWNIISPREFVDFSYTVGYKEG-LLSCGISLDWDEKRP--EFVRGYNHPCGWFCVPLKDNPNQSLLTGYIQT 77
Cdd:cd08867    96 GRTITPSAAMGLISPRDFVDLVYVKRYEDNqWSSSGKSVDIPERPPtpGFVRGYNHPCGYFCSPLKGSPDKSFLVLYVQT 175

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034643615  78 DLRGMIPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:cd08867   176 DLRGMIPQSLVESAMPSNLVNFYTDLVKGV 205
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 2-107 6.36e-26

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: 95.67  E-value: 6.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615   2 RYTTAGQLWNIISPREFVDFSYTVGYKEG-LLSCGISLDWDEKRPE--FVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTD 78
Cdd:cd08903    97 RTVTPSAAMKIISPRDFVDVVLVKRYEDGtISSNATNVEHPLCPPQagFVRGFNHPCGCFCEPVPGEPDKTQLVSFFQTD 176

                          90       100
                  ....*....|....*....|....*....
gi 1034643615  79 LRGMIPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:cd08903   177 LSGYLPQTVVDSFFPASMAEFYNNLTKAV 205
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 13-104 1.94e-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: 89.20  E-value: 1.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615  13 ISPREFVDFSYtVGYKEGLLS--CGISLDWDEKRPE--FVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDLRGMIPQSAV 88
Cdd:cd08904   106 ISPRDFVDLVH-IKRYEGNMNivSSVSVEYPQCPPSsnYIRGYNHPCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVI 184

                          90
                  ....*....|....*.
gi 1034643615  89 DTAMASTLTNFYGDLR 104
Cdd:cd08904   185 EKTMPTNLVNLILDAK 200
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 12-107 2.00e-20

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: 80.85  E-value: 2.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615  12 IISPREFVDFSYTVGYKEGL-LSCGISLDWD--EKRPEFVRGYNHPCGWFCVPLkdNPNQSLLTGYIQTDLRGMIPQSAV 88
Cdd:cd00177    96 PVSPRDFVYLRRRRKLDDGTyVIVSKSVDHDshPKEKGYVRAEIKLSGWIIEPL--DPGKTKVTYVLQVDPKGSIPKSLV 173

                          90
                  ....*....|....*....
gi 1034643615  89 DTAMASTLTNFYGDLRKAL 107
Cdd:cd00177   174 NSAAKKQLASFLKDLRKAK 192
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 5-105 3.80e-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: 3.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615   5 TAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDE--KRPEFVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDLRGM 82
Cdd:cd08868   101 AAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAmpPTKNYVRGENGPGCWILRPLPNNPNKCNFTWLLNTDLKGW 180

                          90       100
                  ....*....|....*....|...
gi 1034643615  83 IPQSAVDTAMASTLTNFYGDLRK 105
Cdd:cd08868   181 LPQYLVDQALASVLLDFMKHLRK 203
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 5-107 3.48e-14

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: 64.88  E-value: 3.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615   5 TAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRP--EFVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDLRGM 82
Cdd:cd08906   102 AAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPlsKYVRGENGPGGFVVLKSASNPSVCTFIWILNTDLKGR 181

                          90       100
                  ....*....|....*....|....*
gi 1034643615  83 IPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:cd08906   182 LPRYLIHQSLAATMFEFASHLRQRI 206
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 2-107 1.77e-10

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: 55.23  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615   2 RYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRP--EFVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDL 79
Cdd:cd08905    99 HEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEqkGFIRAENGPTCIVLRPLAGDPSKTKLTWLLSIDL 178

                          90       100
                  ....*....|....*....|....*...
gi 1034643615  80 RGMIPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:cd08905   179 KGWLPKSIINQVLSQTQVDFANHLRQRM 206
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 3-107 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: 52.82  E-value: 1.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615    3 YTTAGQLWNIISPREFVDFSYT-VGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV-PLKDNPnqSLLTGYIQTD 78
Cdd:smart00234  94 HYVSKFAAGPVSPRDFVFVRYWrEDEDGSYAVVDVSVTHPTSPPEsgYVRAENLPSG-LLIePLGNGP--SKVTWVSHAD 170

                           90       100
                   ....*....|....*....|....*....
gi 1034643615   79 LRGMIPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:smart00234 171 LKGWLPHWLVRSLIKSGLAEFAKTLVATL 199
START pfam01852
START domain;
3-107 7.40e-08

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 48.17  E-value: 7.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643615   3 YTTAGQLWNIISPREFVDFSY-TVGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV-PLKDNPnqSLLTGYIQTD 78
Cdd:pfam01852  94 YVAALVAPSPLSPRDFVFLRYwRRLGGGVYVIVDRSVTHPQFPPSsgYVRAERLPSG-YLIqPCGNGP--SKVTWVSHAD 170

                          90       100
                  ....*....|....*....|....*....
gi 1034643615  79 LRGMIPQSAVDTAMASTLTNFYGDLRKAL 107
Cdd:pfam01852 171 LKGWLPSWLLRSLYKSGMPEGAKTWVATL 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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