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Conserved domains on  [gi|967489507|ref|XP_014977506|]
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stAR-related lipid transfer protein 6 isoform X1 [Macaca mulatta]

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 ...
 1-215 7.72e-140

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 cd08904:

Pssm-ID: 472699  Cd Length: 204  Bit Score: 389.65  E-value: 7.72e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507   1 MDYKAIAQKTVQEVLGYTQDTSGWKVVKISliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESAAKLSDFLYQTG 80
Cdd:cd08904    1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTS-----------KKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  81 ERVTWDKSLQVYDMVHRIDSDTFICHTITQSFAMGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNH 160
Cdd:cd08904   70 HRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNH 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 967489507 161 PCGFVCSPMKENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 215
Cdd:cd08904  150 PCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
 
Name Accession Description Interval E-value
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 1-215 7.72e-140

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: 389.65  E-value: 7.72e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507   1 MDYKAIAQKTVQEVLGYTQDTSGWKVVKISliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESAAKLSDFLYQTG 80
Cdd:cd08904    1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTS-----------KKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  81 ERVTWDKSLQVYDMVHRIDSDTFICHTITQSFAMGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNH 160
Cdd:cd08904   70 HRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNH 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 967489507 161 PCGFVCSPMKENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 215
Cdd:cd08904  150 PCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 52-206 1.20e-26

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 101.74  E-value: 1.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507    52 RKFHGNLYRVEGIIPESAAKLS-DFLYQTGERVTWDKSLQVYDMVHRIDSDTFICHtITQSFAMGSISPRDFIDLVYIKR 130
Cdd:smart00234  39 GRKPGEAFRLVGVVPMVCADLVeELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYH-YVSKFAAGPVSPRDFVFVRYWRE 117

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967489507   131 YEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMKENPaySKLVMFVQTEMRGKLSPSIIEKTMPSNLVNF 206
Cdd:smart00234 118 DEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEF 191
START pfam01852
START domain;
36-196 8.52e-26

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 99.40  E-value: 8.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507   36 FLFPFEKKITVSSKASRKFHGNLYRVEGIIPESAAKL-SDFLYQTGERVTWDKSLQVYDMVHRIDSDTFICHTITQSFAM 114
Cdd:pfam01852  22 VLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLvAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVAALVAP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  115 GSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMKENpaYSKLVMFVQTEMRGKLSPSI 194
Cdd:pfam01852 102 SPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG--PSKVTWVSHADLKGWLPSWL 179


                  ..
gi 967489507  195 IE 196
Cdd:pfam01852 180 LR 181
 
Name Accession Description Interval E-value
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 1-215 7.72e-140

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: 389.65  E-value: 7.72e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507   1 MDYKAIAQKTVQEVLGYTQDTSGWKVVKISliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESAAKLSDFLYQTG 80
Cdd:cd08904    1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTS-----------KKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  81 ERVTWDKSLQVYDMVHRIDSDTFICHTITQSFAMGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNH 160
Cdd:cd08904   70 HRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNH 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 967489507 161 PCGFVCSPMKENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 215
Cdd:cd08904  150 PCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 1-215 5.14e-114

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: 324.42  E-value: 5.14e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507   1 MDYKAIAQKTVQEVLGYTQDTSGWKVVKISliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESAAKLSDFLYQ-- 78
Cdd:cd08867    1 MDFKVIAEKLANEALQYINDTDGWKVLKTV-----------KNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPpc 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  79 TGERVTWDKSLQVYDMVHRIDSDTFICHTITQSFAMGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGY 158
Cdd:cd08867   70 GGLRLKWDKSLKHYEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGY 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 967489507 159 NHPCGFVCSPMKENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 215
Cdd:cd08867  150 NHPCGYFCSPLKGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGVK 206
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 1-216 2.64e-55

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: 175.80  E-value: 2.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507   1 MDYKAIAQKTVQEVLGYTQDTSGWKVVKISliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESAAKLSDFL--YQ 78
Cdd:cd08903    1 MDYAELAESVADKMLLYRRDESGWKTCRRT-----------NEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLkpAA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  79 TGERVTWDKSLQVYDMVHRIDSDTFICHTITQSFAMGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGY 158
Cdd:cd08903   70 GGLRVKWDQNVKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGF 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 967489507 159 NHPCGFVCSPMKENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIKA 216
Cdd:cd08903  150 NHPCGCFCEPVPGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKA 207
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 24-215 7.00e-35

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: 123.14  E-value: 7.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  24 WKVVKISliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESAAKLSDFLYQTGERVTWDKSLQVYDMVHRIDSDTF 103
Cdd:cd08902   25 WRVAKKS-----------KDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMTSMDIIEEFEENCC 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507 104 ICHTITQSFAMGSISPRDFIDLVYIKRYEGNMnIISSKSVDFPEYPPssNYIRGYNHPCGFVCSPMKENPAYSKLVMFVQ 183
Cdd:cd08902   94 VMRYTTAGQLLNIISPREFVDFSYTTQYEDGL-LSCGVSIEYEEARP--NFVRGFNHPCGWFCVPLKDNPSHSLLTGYIQ 170

                        170       180       190
                 ....*....|....*....|....*....|..
gi 967489507 184 TEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 215
Cdd:cd08902  171 TDLRGMLPQSAVDTAMASTLVNFYSDLKKALK 202
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 7-207 2.08e-34

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: 121.68  E-value: 2.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507   7 AQKTVQEVLgytQDTSGWKVVKIsliicgflfpfEKKITVSSKASRKFHGNLYRVEGIIPESAAKLSDFLYQTGERVTWD 86
Cdd:cd00177    3 AIEELLELL---EEPEGWKLVKE-----------KDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWD 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  87 KSLQVYDMVHRIDSDTFICHTITQSFAMgsISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVC 166
Cdd:cd00177   69 KNFEEFEVIEEIDEHTDIIYYKTKPPWP--VSPRDFVYLRRRRKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWII 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 967489507 167 SPMkeNPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFI 207
Cdd:cd00177  147 EPL--DPGKTKVTYVLQVDPKGSIPKSLVNSAAKKQLASFL 185
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 1-217 7.21e-32

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: 115.53  E-value: 7.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507   1 MDYKAIAQKTVQEVLGYTQDtSGWKVVKISliicgflfpfEKKITVSSKaSRKFHGNLYRVEGIIPESAAKL-SDFLYQT 79
Cdd:cd08868    4 LEYLKQGAEALARAWSILTD-PGWKLEKNT----------TWGDVVYSR-NVPGVGKVFRLTGVLDCPAEFLyNELVLNV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  80 GERVTWDKSLQVYDMVHRIDSDTFICHTITQSFAMGSISPRDFIDLVYIKRYEgNMNIISSKSVDFPEYPPSSNYIRGYN 159
Cdd:cd08868   72 ESLPSWNPTVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRE-NCYLSSGVSVEHPAMPPTKNYVRGEN 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 967489507 160 HPCGFVCSPMKENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIKAH 217
Cdd:cd08868  151 GPGCWILRPLPNNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL 208
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 52-206 1.20e-26

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 101.74  E-value: 1.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507    52 RKFHGNLYRVEGIIPESAAKLS-DFLYQTGERVTWDKSLQVYDMVHRIDSDTFICHtITQSFAMGSISPRDFIDLVYIKR 130
Cdd:smart00234  39 GRKPGEAFRLVGVVPMVCADLVeELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYH-YVSKFAAGPVSPRDFVFVRYWRE 117

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967489507   131 YEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMKENPaySKLVMFVQTEMRGKLSPSIIEKTMPSNLVNF 206
Cdd:smart00234 118 DEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEF 191
START pfam01852
START domain;
36-196 8.52e-26

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 99.40  E-value: 8.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507   36 FLFPFEKKITVSSKASRKFHGNLYRVEGIIPESAAKL-SDFLYQTGERVTWDKSLQVYDMVHRIDSDTFICHTITQSFAM 114
Cdd:pfam01852  22 VLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLvAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVAALVAP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  115 GSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMKENpaYSKLVMFVQTEMRGKLSPSI 194
Cdd:pfam01852 102 SPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG--PSKVTWVSHADLKGWLPSWL 179


                  ..
gi 967489507  195 IE 196
Cdd:pfam01852 180 LR 181
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 53-215 1.77e-24

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: 96.08  E-value: 1.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  53 KFHGNLYRVEGIIPESAAKL-SDFLYQTGERVTWDKSLQVYDMVHRIDSDTFICHTITQSFAMGSISPRDFIDLVYIKRY 131
Cdd:cd08906   45 PFHGKTFILKAFMQCPAELVyQEVILQPEKMVLWNKTVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507 132 eGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMKENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAK 211
Cdd:cd08906  125 -RDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLKSASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLR 203


                 ....
gi 967489507 212 DGIK 215
Cdd:cd08906  204 QRIR 207
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 1-207 1.45e-18

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: 80.65  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507   1 MDYKAIAQKTVQEVLGYTQDTSGWKVVKISliicgflfpfEKKITVSSKASRKFhGNLYRVEGIIPESA----AKLSDFL 76
Cdd:cd08905    4 MSYIKQGEEALQKSLSILQDQEGWKTEIVA----------ENGDKVLSKVVPDI-GKVFRLEVVVDQPLdnlySELVDRM 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  77 YQTGErvtWDKSLQVYDMVHRIDSDTFICHTITQSFAMGSISPRDFIDLVYIKRyEGNMNIISSKSVDFPEYPPSSNYIR 156
Cdd:cd08905   73 EQMGE---WNPNVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKR-RGSTCVLAGMATHFGLMPEQKGFIR 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 967489507 157 GYNHPCGFVCSPMKENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFI 207
Cdd:cd08905  149 AENGPTCIVLRPLAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFA 199
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 61-209 1.65e-10

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: 59.15  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  61 VEGIIPESAAKLSDFLYQTGERVTWDKSLQVYDMVHRIDSDTFICHTITQSfaMGSISPRDFIDLVYIKR--YEGNMNII 138
Cdd:cd08873   81 VELKVQTCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPS--LTSEKPNDFVLLVSRRKpaTDGDPYKV 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967489507 139 SSKSVDFPEYPPSSNYIRGYNHPCGFV----CSPMKE----NPAYSKLVMFVQTEMRGkLSpSIIEKTMPSnLVNFILN 209
Cdd:cd08873  159 AFRSVTLPRVPQTPGYSRTEVACAGFVirqdCGTCTEvsyyNETNPKLLSYVTCNLAG-LS-ALYCRTFHC-CEQFLVT 234
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 19-193 1.21e-08

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: 53.38  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  19 QDTSGWKVVKIsliicgflfpfEKKITVSSKA-SRKFHGnlYRVEGIIPESAAKLSDFLYQTGERVTWDKSLQVYDMVHR 97
Cdd:cd08874   19 QATAGWSYQCL-----------EKDVVIYYKVfNGTYHG--FLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTARIHKT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  98 IDSDTFICHTITQSFAMGSISPRDFIdLVYIKRYEGNMNIISSKSVDFPEYP-PSSNYIRGYNHPCGFVCSPMKEN-PAY 175
Cdd:cd08874   86 FTEDICLVYLVHETPLCLLKQPRDFC-CLQVEAKEGELSVVACQSVYDKSMPePGRSLVRGEILPSAWILEPVTVEgNQY 164

                        170
                 ....*....|....*...
gi 967489507 176 SKLVMFVQTEMRGKLSPS 193
Cdd:cd08874  165 TRVIYIAQVALCGPDVPA 182
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 59-164 2.80e-08

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: 52.56  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  59 YRVEGIIPESAAKLSDFLYQTGERVTWDKSLQVYDMVHRIDSDTFICHTITQSFAMGSiSPRDFIDLVYIKR--YEGNMN 136
Cdd:cd08913   83 FKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHG-KPQDFVILASRRKpcDNGDPY 161

                         90       100
                 ....*....|....*....|....*...
gi 967489507 137 IISSKSVDFPEYPPSSNYIRGYNHPCGF 164
Cdd:cd08913  162 VIALRSVTLPTHPPTPEYTRGETLCSGF 189
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 42-207 8.49e-08

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: 51.10  E-value: 8.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  42 KKITVSSKASRKFHGNLYRVEGIIPE-SAAKLSDFLYQTGERVTWDKSLQVYDMVHRIDSDTFICHtitQSFAMGS-ISP 119
Cdd:cd08871   32 NNVKVWTKNPENSSIKMIKVSAIFPDvPAETLYDVLHDPEYRKTWDSNMIESFDICQLNPNNDIGY---YSAKCPKpLKN 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507 120 RDFIDLVYIKRYEGNMnIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMKENPaySKLVMFVQTEMRGKLspsiiektm 199
Cdd:cd08871  109 RDFVNLRSWLEFGGEY-IIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKG--CTLTYVTQNDPKGSL--------- 176


                 ....*...
gi 967489507 200 PSNLVNFI 207
Cdd:cd08871  177 PKWVVNKA 184
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 72-165 2.00e-04

Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114) 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. STARD15/ACOT12 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. Human STARD15/ACOT12 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176922  Cd Length: 236  Bit Score: 41.42  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  72 LSDFlyqtGERVTWDK---SLQVYDMVHRIDSDTFI-CHTITQSfamgsiSPRDFIDLVYiKRY---EGNMNIISSKSVD 144
Cdd:cd08914   97 LSDF----TKRPLWDPhflSCEVIDWVSEDDQIYHItCPIVNND------KPKDLVVLVS-RRKplkDGNTYVVAVKSVI 165

                         90       100
                 ....*....|....*....|.
gi 967489507 145 FPEYPPSSNYIRGYNHPCGFV 165
Cdd:cd08914  166 LPSVPPSPQYIRSEIICAGFL 186
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 19-171 1.59e-03

Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD7 (also known as gestational trophoblastic tumor 1/GTT1). 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. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of phosphatidycholine (PtdCho) to mitochondria. STARD7 was shown to be surface active and to interact differentially with phospholipid monolayers, it showed a preference for phosphatidylserine, cholesterol, and phosphatidylglycerol.


Pssm-ID: 176920  Cd Length: 207  Bit Score: 38.42  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  19 QDTSGWKVVkisliicgflfpFEKKitvSSKASRKFH--GNL--YRVEGIIPESAAKlsDFLY-QTG--ERVTWDKSLQV 91
Cdd:cd08911   18 QEPDGWEPF------------IEKK---DMLVWRREHpgTGLyeYKVYGSFDDVTAR--DFLNvQLDleYRKKWDATAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967489507  92 YDMVHR-IDSDTFICHTITQ---SFAmgsisPRDFidlVYIKRY----EGNMNIISSKSVDFPEYPPSSNYIRGYNHPCG 163
Cdd:cd08911   81 LEVVDEdPETGSEIIYWEMQwpkPFA-----NRDY---VYVRRYiideENKLIVIVSKAVQHPSYPESPKKVRVEDYWSY 152


                 ....*...
gi 967489507 164 FVCSPMKE 171
Cdd:cd08911  153 MVIRPHKS 160
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 81-147 1.86e-03

C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). 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. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear.


Pssm-ID: 176878  Cd Length: 197  Bit Score: 38.06  E-value: 1.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967489507  81 ERVTWDKSLQVYDMVHRIDSDTFICHTITQSfaMGSISPRDFidlVYIKRYEGNMN----IISSKSVDFPE 147
Cdd:cd08869   66 ERHLWDDDLLQWKVVETLDEDTEVYQYVTNS--MAPHPTRDY---VVLRTWRTDLPkgacVLVETSVEHTE 131
 
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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