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Conserved domains on  [gi|11066458|gb|AAG28595|]
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steroidogenic acute regulatory protein, partial [Xenopus laevis]

Protein Classification

steroidogenic acute regulatory protein( domain architecture ID 10172357)

steroidogenic acute regulatory protein (STAR) plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone

Gene Symbol:  STAR
Gene Ontology:  GO:0008289|GO:0120020|GO:0006694
PubMed:  31927098|18922149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 74-282 1.21e-153

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: 427.33  E-value: 1.21e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  74 DVEMSYIKQGEEALKKSLNILGDQDGWKTEIVMENGDKVLSKVLPDIGKVFKLEAVVEKPLDNVYGELVDNMEKMGEWNP 153
Cdd:cd08905   1 EAEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 154 NVKEVKILQKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKRRGSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLRP 233
Cdd:cd08905  81 NVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 11066458 234 LAEDVSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLRSRMASS 282
Cdd:cd08905 161 LAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRMASS 209
 
Name Accession Description Interval E-value
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 74-282 1.21e-153

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: 427.33  E-value: 1.21e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  74 DVEMSYIKQGEEALKKSLNILGDQDGWKTEIVMENGDKVLSKVLPDIGKVFKLEAVVEKPLDNVYGELVDNMEKMGEWNP 153
Cdd:cd08905   1 EAEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 154 NVKEVKILQKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKRRGSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLRP 233
Cdd:cd08905  81 NVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 11066458 234 LAEDVSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLRSRMASS 282
Cdd:cd08905 161 LAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRMASS 209
START pfam01852
START domain;
82-279 2.25e-59

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 188.00  E-value: 2.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458    82 QGEEALKKSLNILGDQDGWKTEIVMENGDKVLSKVLPDIGKVFKLEAVVEKPLDNVYGELVDNMEKMGEWNPNVKEVKIL 161
Cdd:pfam01852   3 AEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAETL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458   162 QKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKR-RGSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLRPLAEdvSK 240
Cdd:pfam01852  83 EVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRlGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGN--GP 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 11066458   241 TKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLRSRM 279
Cdd:pfam01852 161 SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATL 199
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 82-278 1.64e-55

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 178.39  E-value: 1.64e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458     82 QGEEALKKSLNILGDQDGWKTEIVMENGDKVLSKVLPDI--GKVFKLEAVVEKPLDNVYGELVDNMEKMGEWNPNVKEVK 159
Cdd:smart00234   2 AEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPGRkpGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458    160 ILQKIGKDTVITHEKaAETPGNIVGARDFVSVRCSKR--RGSTCILAGMSTRFGGMPEqKGFVRGENGPTCMVLRPLAEd 237
Cdd:smart00234  82 TLEVIDNGTVIYHYV-SKFAAGPVSPRDFVFVRYWREdeDGSYAVVDVSVTHPTSPPE-SGYVRAENLPSGLLIEPLGN- 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 11066458    238 vSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLRSR 278
Cdd:smart00234 159 -GPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVAT 198
 
Name Accession Description Interval E-value
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 74-282 1.21e-153

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: 427.33  E-value: 1.21e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  74 DVEMSYIKQGEEALKKSLNILGDQDGWKTEIVMENGDKVLSKVLPDIGKVFKLEAVVEKPLDNVYGELVDNMEKMGEWNP 153
Cdd:cd08905   1 EAEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 154 NVKEVKILQKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKRRGSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLRP 233
Cdd:cd08905  81 NVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 11066458 234 LAEDVSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLRSRMASS 282
Cdd:cd08905 161 LAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRMASS 209
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 76-281 1.97e-90

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: 267.30  E-value: 1.97e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  76 EMSYIKQGEEALKKSLNILGDQDgWKTEIVMENGDKVLSKVLPDIGKVFKLEAVVEKPLDNVYGELVDNMEKMGEWNPNV 155
Cdd:cd08868   3 ELEYLKQGAEALARAWSILTDPG-WKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNPTV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 156 KEVKILQKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKRRGSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLRPLA 235
Cdd:cd08868  82 LECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPLP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 11066458 236 EDVSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLRSRMAS 281
Cdd:cd08868 162 NNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIAT 207
START pfam01852
START domain;
82-279 2.25e-59

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 188.00  E-value: 2.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458    82 QGEEALKKSLNILGDQDGWKTEIVMENGDKVLSKVLPDIGKVFKLEAVVEKPLDNVYGELVDNMEKMGEWNPNVKEVKIL 161
Cdd:pfam01852   3 AEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAETL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458   162 QKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKR-RGSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLRPLAEdvSK 240
Cdd:pfam01852  83 EVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRlGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGN--GP 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 11066458   241 TKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLRSRM 279
Cdd:pfam01852 161 SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATL 199
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 76-280 6.14e-57

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: 181.98  E-value: 6.14e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  76 EMSYIKQGEEALKKSLNILGDQDGWKTEIVMENGDKVLSKVLPDIGKVFKLEAVVEKPLDNVYGELVDNMEKMGEWNPNV 155
Cdd:cd08906   3 EREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNKTV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 156 KEVKILQKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKRRGSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLRPLA 235
Cdd:cd08906  83 SACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLKSA 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 11066458 236 EDVSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLRSRMA 280
Cdd:cd08906 163 SNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIR 207
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 82-278 1.64e-55

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 178.39  E-value: 1.64e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458     82 QGEEALKKSLNILGDQDGWKTEIVMENGDKVLSKVLPDI--GKVFKLEAVVEKPLDNVYGELVDNMEKMGEWNPNVKEVK 159
Cdd:smart00234   2 AEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPGRkpGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458    160 ILQKIGKDTVITHEKaAETPGNIVGARDFVSVRCSKR--RGSTCILAGMSTRFGGMPEqKGFVRGENGPTCMVLRPLAEd 237
Cdd:smart00234  82 TLEVIDNGTVIYHYV-SKFAAGPVSPRDFVFVRYWREdeDGSYAVVDVSVTHPTSPPE-SGYVRAENLPSGLLIEPLGN- 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 11066458    238 vSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLRSR 278
Cdd:smart00234 159 -GPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVAT 198
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 84-276 9.30e-35

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: 124.37  E-value: 9.30e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  84 EEALKKSLNILGDQDGWKtEIVMENGDKVLSKVLPDIG-KVFKLEAVVEKPLDNVYgELVDNMEKMGEWNPNVKEVKILQ 162
Cdd:cd00177   1 EEAIEELLELLEEPEGWK-LVKEKDGVKIYTKPYEDSGlKLLKAEGVIPASPEQVF-ELLMDIDLRKKWDKNFEEFEVIE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 163 KIGKDTVITHekAAETPGNIVGARDFVSVR-CSKRRGSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLRPLAEDvsKT 241
Cdd:cd00177  79 EIDEHTDIIY--YKTKPPWPVSPRDFVYLRrRRKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPG--KT 154

                       170       180       190
                ....*....|....*....|....*....|....*
gi 11066458 242 KLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLR 276
Cdd:cd00177 155 KVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLR 189
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 77-276 1.92e-21

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: 89.44  E-value: 1.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  77 MSYIKQGEEALKKSLNILGDQDGWKteIVME-NGDKVLSKVLPDI-GKVFKLEAVVEKPLDNVYGELVDNMEKM-GEWNP 153
Cdd:cd08867   1 MDFKVIAEKLANEALQYINDTDGWK--VLKTvKNITVSWKPSTEFtGHLYRAEGIVDALPEKVIDVIIPPCGGLrLKWDK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 154 NVKEVKILQKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKR-RGSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLR 232
Cdd:cd08867  79 SLKHYEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRyEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCS 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 11066458 233 PLAEDVSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLR 276
Cdd:cd08867 159 PLKGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLV 202
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 77-275 1.02e-16

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: 76.80  E-value: 1.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  77 MSYIKQGEEALKKSLNILGDQDGWKTeivMENGDKVLSKVLPDI---GKVFKLEAVVEKPLDNVYgELVDNmEKMG---E 150
Cdd:cd08903   1 MDYAELAESVADKMLLYRRDESGWKT---CRRTNEVAVSWRPSAefaGNLYKGEGIVYATLEQVW-DCLKP-AAGGlrvK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 151 WNPNVKEVKILQKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKRRGSTCILAGMS-TRFGGMPEQKGFVRGENGPTCM 229
Cdd:cd08903  76 WDQNVKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATnVEHPLCPPQAGFVRGFNHPCGC 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 11066458 230 VLRPLAEDVSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHL 275
Cdd:cd08903 156 FCEPVPGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNL 201
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 77-271 4.21e-14

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: 69.55  E-value: 4.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  77 MSYIKQGEEALKKSLNILGDQDGWKteiVMENGDKVLSKVLPDI---GKVFKLEAVV-EKPldnvyGELVDNM---EKMG 149
Cdd:cd08904   1 MDFKKIAQETSQEVLGYSRDTSGWK---VVKTSKKITVSWKPSRkyhGNLYRVEGIIpESP-----AKLIQFMyqpEHRI 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 150 EWNPNVKEVKILQKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKR-RGSTCILAGMSTRFGGMPEQKGFVRGENGPTC 228
Cdd:cd08904  73 KWDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRyEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCG 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 11066458 229 MVLRPLAEDVSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDF 271
Cdd:cd08904 153 YVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNL 195
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 90-267 6.21e-12

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: 63.06  E-value: 6.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  90 SLNILGDQDGWKTeIVMENGDKVLSKVLPDIG-KVFKLEAVVEKPLDNVyGELVDNMEKMGEWNPNVKEVKILQKIGKDT 168
Cdd:cd08876   9 AGAALAPDGDWQL-VKDKDGIKVYTRDVEGSPlKEFKAVAEVDASIEAF-LALLRDTESYPQWMPNCKESRVLKRTDDNE 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 169 VITHEK-AAETPgniVGARDFVS-VRCSKR--RGSTCILAGMSTRFGgmPEQKGFVRGENGPTCMVLRPLAEDvsKTKLT 244
Cdd:cd08876  87 RSVYTViDLPWP---VKDRDMVLrSTTEQDadDGSVTITLEAAPEAL--PEQKGYVRIKTVEGQWTFTPLGNG--KTRVT 159

                       170       180
                ....*....|....*....|...
gi 11066458 245 WLLSIDLKGWLPKSIINQVLSQT 267
Cdd:cd08876 160 YQAYADPGGSIPGWLANAFAKDA 182
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 121-276 3.04e-08

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: 52.65  E-value: 3.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 121 GKVFKLEAVVEkpldNVYGELVDNMeKMG----EWNPNVKEVKILQKIGKDTVITHEKAAETPGNIVGARDFVSVRCSKR 196
Cdd:cd08902  46 GYLYKAQGVVE----DVYNRIVDHI-RPGpyrlDWDSLMTSMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQ 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 197 RGSTCILAGMSTRFGGM-PEqkgFVRGENGPTCMVLRPLAEDVSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHL 275
Cdd:cd08902 121 YEDGLLSCGVSIEYEEArPN---FVRGFNHPCGWFCVPLKDNPSHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDL 197


                .
gi 11066458 276 R 276
Cdd:cd08902 198 K 198
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 96-263 8.48e-07

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). 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. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


Pssm-ID: 176880  Cd Length: 222  Bit Score: 48.79  E-value: 8.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  96 DQDGWKTEiVMENGDKVLSKVLPDIG-KVFKLEAVVEK-PLDNVYGELVDNmEKMGEWNPNVKEVKILQKIGKDTVITHe 173
Cdd:cd08871  21 STDGWKLK-YNKNNVKVWTKNPENSSiKMIKVSAIFPDvPAETLYDVLHDP-EYRKTWDSNMIESFDICQLNPNNDIGY- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 174 KAAETPgNIVGARDFVSVRCSKRRGSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLRPLAEdvSKTKLTWLLSIDLKG 253
Cdd:cd08871  98 YSAKCP-KPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP--KGCTLTYVTQNDPKG 174

                       170
                ....*....|
gi 11066458 254 WLPKSIINQV 263
Cdd:cd08871 175 SLPKWVVNKA 184
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 99-281 1.19e-04

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. 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. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.


Pssm-ID: 176883  Cd Length: 205  Bit Score: 42.21  E-value: 1.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  99 GWKTEiVMENGDKVLSKVLPDIGKVFKLEAVVEKPLDNVYGeLVDNMEKMGEWNPNVKEVKILQKIGKDTVITHEKAAET 178
Cdd:cd08874  23 GWSYQ-CLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWK-AVKDPRTRFLYDTMIKTARIHKTFTEDICLVYLVHETP 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 179 PGNIVGARDFVSVRCSKRRGSTCILAGMSTRFGGMPEQ-KGFVRGENGPTCMVLRPLAEDVSK-TKLTWLLSIDLKGWLP 256
Cdd:cd08874 101 LCLLKQPRDFCCLQVEAKEGELSVVACQSVYDKSMPEPgRSLVRGEILPSAWILEPVTVEGNQyTRVIYIAQVALCGPDV 180

                       170       180
                ....*....|....*....|....*
gi 11066458 257 KSIINQVLSQTQVDFAKHLRSRMAS 281
Cdd:cd08874 181 PAQLLSSLSKRQPLVIARLALFLEA 205
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 85-245 1.89e-04

Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974), STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114), and related domains. 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. STARD14/ACOT11 and STARD15/ACOT12 are type II acetyl-CoA thioesterases; they catalyze the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, STARD14 and STARD15 each have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice. Human STARD15 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176882  Cd Length: 235  Bit Score: 41.81  E-value: 1.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458  85 EALKKslniLGDQDGW-------KTEIVMENGDKVLSkvlpdigkvFKLEAVVEKPLDNVYgELVDNMEKMGEWNPNVKE 157
Cdd:cd08873  46 TALKR----LAAKSDWtvassttSVTLYTLEQDGVLS---------FCVELKVQTCASDAF-DLLSDPFKRPEWDPHGRS 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 158 VKILQKIGKDTVITH----EKAAETPgnivgaRDFVsVRCSKRR----GSTCILAGMSTRFGGMPEQKGFVRGENGPTCM 229
Cdd:cd08873 112 CEEVKRVGEDDGIYHttmpSLTSEKP------NDFV-LLVSRRKpatdGDPYKVAFRSVTLPRVPQTPGYSRTEVACAGF 184

                       170
                ....*....|....*.
gi 11066458 230 VLRplAEDVSKTKLTW 245
Cdd:cd08873 185 VIR--QDCGTCTEVSY 198
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 124-245 1.30e-03

Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974) 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. STARD14/ACOT11 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice.


Pssm-ID: 176921  Cd Length: 240  Bit Score: 39.46  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 124 FKLEAVVEKPLDNVYgELVDNMEKMGEWNPNVKEVKILQKIGKDTVITHekaAETP--GNIVGARDFVsVRCSKR----R 197
Cdd:cd08913  83 FKVEMVVHVDAAQAF-LLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYH---VTSPslSGHGKPQDFV-ILASRRkpcdN 157

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 11066458 198 GSTCILAGMSTRFGGMPEQKGFVRGENGPTCMVLRPLAEDVskTKLTW 245
Cdd:cd08913 158 GDPYVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQL--TKVSY 203
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 124-276 5.88e-03

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: 36.53  E-value: 5.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11066458 124 FKLEAVVEKPLDNVYgELVDNMEKMGEWNPNVKEVKILqkigkdtvithekaaETPGNIVGARDFVSVRCSKRRGSTCIL 203
Cdd:cd07812   1 VEASIEIPAPPEAVW-DLLSDPERWPEWSPGLERVEVL---------------GGGEGGVGARFVGGRKGGRRLTLTSEV 64

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11066458 204 AGMSTrfgGMPEQKGFVRGENGPTCMV---LRPLAEDvsKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFAKHLR 276
Cdd:cd07812  65 TEVDP---PRPGRFRVTGGGGGVDGTGewrLEPEGDG--GTRVTYTVEYDPPGPLLKVFALLLAGALKRELAALLR 135
 
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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