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Conserved domains on  [gi|564373783|ref|XP_006247187|]
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phosphatidylcholine transfer protein isoform X1 [Rattus norvegicus]

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 ...
 4-170 1.55e-103

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: 296.71  E-value: 1.55e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783   4 PAAHFSDEQFREACAELQKPALTGADWQLLVEASGITIYRLLDQSTGLYEYKVFGVLESCIPSLLADVYMDLDYRKKWDQ 83
Cdd:cd08910    1 AAGTFSEEQFREACAELQQPALDGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783  84 YVKELYEKSFDGQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGRKIYVVLAQNISVPQFPEKSGVIRVKQYKQSLAIES 163
Cdd:cd08910   81 YVKELYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRVKQYKQSLAIES 160


                 ....*..
gi 564373783 164 DGKKGSR 170
Cdd:cd08910  161 DGKKGSK 167
 
Name Accession Description Interval E-value
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 4-170 1.55e-103

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: 296.71  E-value: 1.55e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783   4 PAAHFSDEQFREACAELQKPALTGADWQLLVEASGITIYRLLDQSTGLYEYKVFGVLESCIPSLLADVYMDLDYRKKWDQ 83
Cdd:cd08910    1 AAGTFSEEQFREACAELQQPALDGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783  84 YVKELYEKSFDGQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGRKIYVVLAQNISVPQFPEKSGVIRVKQYKQSLAIES 163
Cdd:cd08910   81 YVKELYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRVKQYKQSLAIES 160


                 ....*..
gi 564373783 164 DGKKGSR 170
Cdd:cd08910  161 DGKKGSK 167
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 12-170 3.83e-30

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 109.83  E-value: 3.83e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783    12 QFREACAELQKPALTGADWQLLVEA--SGITIYRLLDQSTGLYEYKVFGVLESCIPSLLADVYMDLDYRKKWDQYVK--E 87
Cdd:smart00234   2 AEEAAAELLKMAAASEEGWVLSSENenGDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAkaE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783    88 LYEKSFDGQMVAYWEVKYPF-PLSNRDYVYTRQRRdldVDGRKIYVVLAQNISVPQFPEKSGVIRVKQYKQSLAIESDGK 166
Cdd:smart00234  82 TLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWR---EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158


                   ....
gi 564373783   167 KGSR 170
Cdd:smart00234 159 GPSK 162
START pfam01852
START domain;
10-170 1.29e-25

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 98.24  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783   10 DEQFREACAELQKPALTGADWQLLV--EASGITIYRLLDQSTglYEYKVFGVLESCIPSLLADVYMDLDYRKKWDQYVK- 86
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSsnENGDVVLQIVEPDHG--EASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRs 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783   87 -ELYEKSFDGQMVAYWEVKYPF--PLSNRDYVYTRQRRdldVDGRKIYVVLAQNISVPQFPEKSGVIRVKQYKQSLAIES 163
Cdd:pfam01852  79 aETLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWR---RLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQP 155


                  ....*..
gi 564373783  164 DGKKGSR 170
Cdd:pfam01852 156 CGNGPSK 162
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
2-34 9.05e-03

NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 36.13  E-value: 9.05e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 564373783   2 AGPAAHFSDEQFREACAELQKPALTGADWQLLV 34
Cdd:COG3288   39 AGLAAGFPDAAYEAAGAEIVDAELLGADIVLKV 71
 
Name Accession Description Interval E-value
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 4-170 1.55e-103

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: 296.71  E-value: 1.55e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783   4 PAAHFSDEQFREACAELQKPALTGADWQLLVEASGITIYRLLDQSTGLYEYKVFGVLESCIPSLLADVYMDLDYRKKWDQ 83
Cdd:cd08910    1 AAGTFSEEQFREACAELQQPALDGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783  84 YVKELYEKSFDGQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGRKIYVVLAQNISVPQFPEKSGVIRVKQYKQSLAIES 163
Cdd:cd08910   81 YVKELYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRVKQYKQSLAIES 160


                 ....*..
gi 564373783 164 DGKKGSR 170
Cdd:cd08910  161 DGKKGSK 167
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 7-170 4.91e-50

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: 161.01  E-value: 4.91e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783   7 HFSDEQFREACAELQKPALtGADWQLLVEASG----ITIYRLLDQSTGLYEYKVFGVLESCIPSLLADVYMDLDYRKKWD 82
Cdd:cd08870    2 HVSEEDLRDLVQELQEGAE-GQAWQQVMDKSTpdmsYQAWRRKPKGTGLYEYLVRGVFEDCTPELLRDFYWDDEYRKKWD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783  83 QYVKELYEKSFD---GQMVAYWEVKYPFPLSNRDYVYTRQRRDLDvdgRKIYVVLAQNISVPQFPEkSGVIRVKQYKQSL 159
Cdd:cd08870   81 ETVIEHETLEEDeksGTEIVRWVKKFPFPLSDREYVIARRLWESD---DRSYVCVTKGVPYPSVPR-SGRKRVDDYESSL 156

                        170
                 ....*....|...
gi 564373783 160 AIES--DGKKGSR 170
Cdd:cd08870  157 VIRAvkGDGQGSA 169
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 12-170 3.83e-30

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 109.83  E-value: 3.83e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783    12 QFREACAELQKPALTGADWQLLVEA--SGITIYRLLDQSTGLYEYKVFGVLESCIPSLLADVYMDLDYRKKWDQYVK--E 87
Cdd:smart00234   2 AEEAAAELLKMAAASEEGWVLSSENenGDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAkaE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783    88 LYEKSFDGQMVAYWEVKYPF-PLSNRDYVYTRQRRdldVDGRKIYVVLAQNISVPQFPEKSGVIRVKQYKQSLAIESDGK 166
Cdd:smart00234  82 TLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWR---EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158


                   ....
gi 564373783   167 KGSR 170
Cdd:smart00234 159 GPSK 162
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 29-161 1.95e-27

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: 103.14  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783  29 DWQLLVEASGITIYRLLDQSTGLYEYKVFGVLESCIPSLLADVYMDLDYRKKWDQYVKELyeKSFD-----GQMVAYWEV 103
Cdd:cd08911   22 GWEPFIEKKDMLVWRREHPGTGLYEYKVYGSFDDVTARDFLNVQLDLEYRKKWDATAVEL--EVVDedpetGSEIIYWEM 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564373783 104 KYPFPLSNRDYVYTRqRRDLDVDgRKIYVVLAQNISVPQFPEKSGVIRVKQYKQSLAI 161
Cdd:cd08911  100 QWPKPFANRDYVYVR-RYIIDEE-NKLIVIVSKAVQHPSYPESPKKVRVEDYWSYMVI 155
START pfam01852
START domain;
10-170 1.29e-25

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 98.24  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783   10 DEQFREACAELQKPALTGADWQLLV--EASGITIYRLLDQSTglYEYKVFGVLESCIPSLLADVYMDLDYRKKWDQYVK- 86
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSsnENGDVVLQIVEPDHG--EASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRs 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783   87 -ELYEKSFDGQMVAYWEVKYPF--PLSNRDYVYTRQRRdldVDGRKIYVVLAQNISVPQFPEKSGVIRVKQYKQSLAIES 163
Cdd:pfam01852  79 aETLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWR---RLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQP 155


                  ....*..
gi 564373783  164 DGKKGSR 170
Cdd:pfam01852 156 CGNGPSK 162
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 11-170 7.39e-24

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: 93.17  E-value: 7.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783  11 EQFREACAElqkpaltGADWQLLVEASGITIYRLLDQSTGLYEYKVFGVLEsCIPSLLADVYMDLDYRKKWDQYVKELYE 90
Cdd:cd00177    5 EELLELLEE-------PEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIP-ASPEQVFELLMDIDLRKKWDKNFEEFEV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783  91 -KSFDG-QMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGrkiYVVLAQNISVPQFPEKSGVIRVKQYKQSLAIESDGKKG 168
Cdd:cd00177   77 iEEIDEhTDIIYYKTKPPWPVSPRDFVYLRRRRKLDDGT---YVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGK 153


                 ..
gi 564373783 169 SR 170
Cdd:cd00177  154 TK 155
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 5-169 2.38e-15

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: 71.52  E-value: 2.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783   5 AAHFsdEQFREACaelqkpaLTGADWQLLVEASGITIYRLLDQSTGLYEYKVFGVLESCIPSLLADVYMDLDYRKKWDQY 84
Cdd:cd08871    9 DADF--EEFKKLC-------DSTDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783  85 VKElyekSFD-GQM-----VAYWEVKYPFPLSNRDYVYTRQRRDLDVDgrkiYVVLaqNISV--PQFPEKSGVIRVKQYK 156
Cdd:cd08871   80 MIE----SFDiCQLnpnndIGYYSAKCPKPLKNRDFVNLRSWLEFGGE----YIIF--NHSVkhKKYPPRKGFVRAISLL 149

                        170
                 ....*....|...
gi 564373783 157 QSLAIESDGKKGS 169
Cdd:cd08871  150 TGYLIRPTGPKGC 162
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 28-156 1.33e-11

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: 60.75  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783  28 ADWQLLVEASGITIYRLLDQSTGLYEYKVFGVLESCIPSLLAdVYMDLDYRKKWDQYVKE--LYEKSFDGQMVAYWEVKY 105
Cdd:cd08876   17 GDWQLVKDKDGIKVYTRDVEGSPLKEFKAVAEVDASIEAFLA-LLRDTESYPQWMPNCKEsrVLKRTDDNERSVYTVIDL 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564373783 106 PFPLSNRDYV-YTRQRRDLDVDGRKIyvvlaQNISVPQ-FPEKSGVIRVKQYK 156
Cdd:cd08876   96 PWPVKDRDMVlRSTTEQDADDGSVTI-----TLEAAPEaLPEQKGYVRIKTVE 143
START_2 cd08877
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 19-150 4.69e-04

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: 39.59  E-value: 4.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373783  19 ELQKPALTGADWQLLVEASGITIYRLLDQSTGLYEYKVFGVLESCIPSLLAdVYMDLDYRKKWDQYVKELYEKSFDG--Q 96
Cdd:cd08877   13 ENLKDLDESDGWTLQKESEGIRVYYKFEPDGSLLSLRMEGEIDGPLFNLLA-LLNEVELYKTWVPFCIRSKKVKQLGraD 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564373783  97 MVAYWEVKYPFPLSNRD-YVYTRQRRDLDVDGRkiYVVLAQNIS-VPQFPEKSGVI 150
Cdd:cd08877   92 KVCYLRVDLPWPLSNREaVFRGFGVDRLEENGQ--IVILLKSIDdDPEFLKLTDLD 145
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
2-34 9.05e-03

NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 36.13  E-value: 9.05e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 564373783   2 AGPAAHFSDEQFREACAELQKPALTGADWQLLV 34
Cdd:COG3288   39 AGLAAGFPDAAYEAAGAEIVDAELLGADIVLKV 71
 
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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