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Conserved domains on  [gi|1622878909|ref|XP_028692166|]
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phosphatidylcholine transfer protein isoform X6 [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 ...
 4-194 1.40e-135

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 cd08910:

Pssm-ID: 472699  Cd Length: 207  Bit Score: 378.76  E-value: 1.40e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909   4 AAGSFSGEQFREACAELQQPALAGADWQLLVETSGISIYRLLDQKTGLYEYKVFGVLEDCSPTLLADIYMDLDYRKQWDQ 83
Cdd:cd08910     1 AAGTFSEEQFREACAELQQPALDGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  84 YVKELYEQECNGQTVVYWEVKYPFPMSNRDYVYLRQRRDLDMEGRKIHVVLAQSTSVPQLVERSGVIRVKQYKQSLAIES 163
Cdd:cd08910    81 YVKELYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRVKQYKQSLAIES 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622878909 164 DGKKGSKVFMYYFDNPGGQIPSWLINWAAKN 194
Cdd:cd08910   161 DGKKGSKVFMYYFDNPGGMIPSWLINWAAKN 191
 
Name Accession Description Interval E-value
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 4-194 1.40e-135

Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP) 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. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may have a mitochondrial function.


Pssm-ID: 176919  Cd Length: 207  Bit Score: 378.76  E-value: 1.40e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909   4 AAGSFSGEQFREACAELQQPALAGADWQLLVETSGISIYRLLDQKTGLYEYKVFGVLEDCSPTLLADIYMDLDYRKQWDQ 83
Cdd:cd08910     1 AAGTFSEEQFREACAELQQPALDGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  84 YVKELYEQECNGQTVVYWEVKYPFPMSNRDYVYLRQRRDLDMEGRKIHVVLAQSTSVPQLVERSGVIRVKQYKQSLAIES 163
Cdd:cd08910    81 YVKELYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRVKQYKQSLAIES 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622878909 164 DGKKGSKVFMYYFDNPGGQIPSWLINWAAKN 194
Cdd:cd08910   161 DGKKGSKVFMYYFDNPGGMIPSWLINWAAKN 191
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 12-194 1.79e-47

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 155.28  E-value: 1.79e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909   12 QFREACAELQQPALAGADWQLLVE--TSGISIYRLLDQKTGLYEYKVFGVLEDCSPTLLADIYMDLDYRKQWDQYVK--E 87
Cdd:smart00234   2 AEEAAAELLKMAAASEEGWVLSSEneNGDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAkaE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909   88 LYEQECNGQTVVYWEVKYPF-PMSNRDYVYLRQRRDLdmeGRKIHVVLAQSTSVPQLVERSGVIRVKQYKQSLAIESDGK 166
Cdd:smart00234  82 TLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWRED---EDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170       180
                   ....*....|....*....|....*...
gi 1622878909  167 KGSKVFMYYFDNPGGQIPSWLINWAAKN 194
Cdd:smart00234 159 GPSKVTWVSHADLKGWLPHWLVRSLIKS 186
START pfam01852
START domain;
11-194 4.41e-42

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 141.39  E-value: 4.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  11 EQFREACAELQQPALAGADWQLLV--ETSGISIYRLLDQktGLYEYKVFGVLEDCSPTLLADIYMDLDYRKQWDQYVK-- 86
Cdd:pfam01852   2 LAEEAAQELLKLALSDEPGWVLLSsnENGDVVLQIVEPD--HGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  87 ELYEQECNGQTVVYWEVKYPF--PMSNRDYVYLRQRRDLdmeGRKIHVVLAQSTSVPQLVERSGVIRVKQYKQSLAIESD 164
Cdd:pfam01852  80 ETLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWRRL---GGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPC 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622878909 165 GKKGSKVFMYYFDNPGGQIPSWLINWAAKN 194
Cdd:pfam01852 157 GNGPSKVTWVSHADLKGWLPSWLLRSLYKS 186
 
Name Accession Description Interval E-value
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 4-194 1.40e-135

Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP) 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. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may have a mitochondrial function.


Pssm-ID: 176919  Cd Length: 207  Bit Score: 378.76  E-value: 1.40e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909   4 AAGSFSGEQFREACAELQQPALAGADWQLLVETSGISIYRLLDQKTGLYEYKVFGVLEDCSPTLLADIYMDLDYRKQWDQ 83
Cdd:cd08910     1 AAGTFSEEQFREACAELQQPALDGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  84 YVKELYEQECNGQTVVYWEVKYPFPMSNRDYVYLRQRRDLDMEGRKIHVVLAQSTSVPQLVERSGVIRVKQYKQSLAIES 163
Cdd:cd08910    81 YVKELYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRVKQYKQSLAIES 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622878909 164 DGKKGSKVFMYYFDNPGGQIPSWLINWAAKN 194
Cdd:cd08910   161 DGKKGSKVFMYYFDNPGGMIPSWLINWAAKN 191
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 6-194 1.80e-73

Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP), and STARD7 (also known as gestational trophoblastic tumor 1/GTT1). 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. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may also have a mitochondrial function. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of 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: 176879  Cd Length: 209  Bit Score: 221.48  E-value: 1.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909   6 GSFSGEQFREACAELQQPAlAGADWQLLVETSG----ISIYRLLDQKTGLYEYKVFGVLEDCSPTLLADIYMDLDYRKQW 81
Cdd:cd08870     1 GHVSEEDLRDLVQELQEGA-EGQAWQQVMDKSTpdmsYQAWRRKPKGTGLYEYLVRGVFEDCTPELLRDFYWDDEYRKKW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  82 DQYVKELYEQECN---GQTVVYWEVKYPFPMSNRDYVYLRQRRDLDmegRKIHVVLAQSTSVPqLVERSGVIRVKQYKQS 158
Cdd:cd08870    80 DETVIEHETLEEDeksGTEIVRWVKKFPFPLSDREYVIARRLWESD---DRSYVCVTKGVPYP-SVPRSGRKRVDDYESS 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622878909 159 LAIES--DGKKGSKVFMYYFDNPGGQIPSWLINWAAKN 194
Cdd:cd08870   156 LVIRAvkGDGQGSACEVTYFHNPDGGIPRELAKLAVKR 193
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 12-194 1.79e-47

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 155.28  E-value: 1.79e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909   12 QFREACAELQQPALAGADWQLLVE--TSGISIYRLLDQKTGLYEYKVFGVLEDCSPTLLADIYMDLDYRKQWDQYVK--E 87
Cdd:smart00234   2 AEEAAAELLKMAAASEEGWVLSSEneNGDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAkaE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909   88 LYEQECNGQTVVYWEVKYPF-PMSNRDYVYLRQRRDLdmeGRKIHVVLAQSTSVPQLVERSGVIRVKQYKQSLAIESDGK 166
Cdd:smart00234  82 TLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWRED---EDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170       180
                   ....*....|....*....|....*...
gi 1622878909  167 KGSKVFMYYFDNPGGQIPSWLINWAAKN 194
Cdd:smart00234 159 GPSKVTWVSHADLKGWLPHWLVRSLIKS 186
START pfam01852
START domain;
11-194 4.41e-42

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 141.39  E-value: 4.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  11 EQFREACAELQQPALAGADWQLLV--ETSGISIYRLLDQktGLYEYKVFGVLEDCSPTLLADIYMDLDYRKQWDQYVK-- 86
Cdd:pfam01852   2 LAEEAAQELLKLALSDEPGWVLLSsnENGDVVLQIVEPD--HGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  87 ELYEQECNGQTVVYWEVKYPF--PMSNRDYVYLRQRRDLdmeGRKIHVVLAQSTSVPQLVERSGVIRVKQYKQSLAIESD 164
Cdd:pfam01852  80 ETLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWRRL---GGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPC 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622878909 165 GKKGSKVFMYYFDNPGGQIPSWLINWAAKN 194
Cdd:pfam01852 157 GNGPSKVTWVSHADLKGWLPSWLLRSLYKS 186
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 11-195 4.35e-38

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: 130.54  E-value: 4.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  11 EQFREACAElqqpalaGADWQLLVETSGISIYRLLDQKTGLYEYKVFGVLeDCSPTLLADIYMDLDYRKQWDQYVKELY- 89
Cdd:cd00177     5 EELLELLEE-------PEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVI-PASPEQVFELLMDIDLRKKWDKNFEEFEv 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  90 -EQECNGQTVVYWEVKYPFPMSNRDYVYLRQRRDLDMEGrkiHVVLAQSTSVPQLVERSGVIRVKQYKQSLAIESDGKKG 168
Cdd:cd00177    77 iEEIDEHTDIIYYKTKPPWPVSPRDFVYLRRRRKLDDGT---YVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGK 153

                         170       180
                  ....*....|....*....|....*..
gi 1622878909 169 SKVFMYYFDNPGGQIPSWLINWAAKNQ 195
Cdd:cd00177   154 TKVTYVLQVDPKGSIPKSLVNSAAKKQ 180
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 29-195 5.70e-38

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: 130.87  E-value: 5.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  29 DWQLLVETSGISIYRLLDQKTGLYEYKVFGVLEDCSPTLLADIYMDLDYRKQWDQYVKEL----YEQECNGQtVVYWEVK 104
Cdd:cd08911    22 GWEPFIEKKDMLVWRREHPGTGLYEYKVYGSFDDVTARDFLNVQLDLEYRKKWDATAVELevvdEDPETGSE-IIYWEMQ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909 105 YPFPMSNRDYVYLRqRRDLDMEgRKIHVVLAQSTSVPQLVERSGVIRVKQYKQSLAIE---SDGKKGSKVFMYYFDNPGG 181
Cdd:cd08911   101 WPKPFANRDYVYVR-RYIIDEE-NKLIVIVSKAVQHPSYPESPKKVRVEDYWSYMVIRphkSFDEPGFEFVLTYFDNPGV 178

                         170
                  ....*....|....
gi 1622878909 182 QIPSWLINWAAKNQ 195
Cdd:cd08911   179 NIPSYITSWVAMSG 192
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 11-194 5.54e-24

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: 95.02  E-value: 5.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  11 EQFREACaelqqpaLAGADWQLLVETSGISIYRLLDQKTGLYEYKVFGVLEDCSPTLLADIYMDLDYRKQWDQYVKELYE 90
Cdd:cd08871    13 EEFKKLC-------DSTDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSNMIESFD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  91 ----QECNgqTVVYWEVKYPFPMSNRDYVYLRQRRDLDMEgrkiHVVLAQSTSVPQLVERSGVIRVKQYKQSLAIESDGK 166
Cdd:cd08871    86 icqlNPNN--DIGYYSAKCPKPLKNRDFVNLRSWLEFGGE----YIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622878909 167 KGSKvfMYYF--DNPGGQIPSWLINWAAKN 194
Cdd:cd08871   160 KGCT--LTYVtqNDPKGSLPKWVVNKATTK 187
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 20-195 1.62e-18

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: 79.62  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  20 LQQPALAG-ADWQLLVETSGISIYRLLDQKTGLYEYKvfGVLE-DCSPTLLADIYMDLDYRKQWDQYVKE--LYEQECNG 95
Cdd:cd08876     8 LAGAALAPdGDWQLVKDKDGIKVYTRDVEGSPLKEFK--AVAEvDASIEAFLALLRDTESYPQWMPNCKEsrVLKRTDDN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  96 QTVVYWEVKYPFPMSNRDYVyLRQR--RDLDMEGRKIHVVlAQSTSVPqlvERSGVIRVKQYKQSLAIESDGKKGSKV-F 172
Cdd:cd08876    86 ERSVYTVIDLPWPVKDRDMV-LRSTteQDADDGSVTITLE-AAPEALP---EQKGYVRIKTVEGQWTFTPLGNGKTRVtY 160

                         170       180
                  ....*....|....*....|...
gi 1622878909 173 MYYFDnPGGQIPSWLINWAAKNQ 195
Cdd:cd08876   161 QAYAD-PGGSIPGWLANAFAKDA 182
START_2 cd08877
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 29-198 1.41e-03

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176886  Cd Length: 215  Bit Score: 38.44  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909  29 DWQLLVETSGISIYRLLDQKTGLYEYKVFGVLEDCSPTLLADIYmDLDYRKQWDQYVKELY--EQECNGQTVVYWEVKYP 106
Cdd:cd08877    23 GWTLQKESEGIRVYYKFEPDGSLLSLRMEGEIDGPLFNLLALLN-EVELYKTWVPFCIRSKkvKQLGRADKVCYLRVDLP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878909 107 FPMSNRDYVYLRQRRDLDMEGRKIhVVLAQSTS------------VPQLVERSGVIRVKQYkqSLAIESDGKKGSKV-FM 173
Cdd:cd08877   102 WPLSNREAVFRGFGVDRLEENGQI-VILLKSIDddpeflkltdldIPSTSAKGVRRIIKYY--GFVITPISPTKCYLrFV 178

                         170       180
                  ....*....|....*....|....*
gi 1622878909 174 YYFDNPGGQIPSWLINWAAKNQSRT 198
Cdd:cd08877   179 ANVDPKMSLVPKSLLNFVARKFAGL 203
 
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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