|
Name |
Accession |
Description |
Interval |
E-value |
| Sterol-sensing |
pfam12349 |
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ... |
308-452 |
7.30e-57 |
|
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins (SREBPs) are membrane-bound transcription factors that promote lipid synthesis in animal cells. They are embedded in the membranes of the endoplasmic reticulum (ER) in a helical hairpin orientation and are released from the ER by a two-step proteolytic process. Proteolysis begins when the SREBPs are cleaved at Site-1, which is located at a leucine residue in the middle of the hydrophobic loop in the lumen of the ER. Upon proteolytic processing SREBP can activate the expression of genes involved in cholesterol biosynthesis and uptake. SCAP stimulates cleavage of SREBPs via fusion of the their two C-termini. This domain is the transmembrane region that traverses the membrane eight times and is the sterol-sensing domain of the cleavage protein. WD40 domains are found towards the C-terminus. :
Pssm-ID: 463544 [Multi-domain] Cd Length: 153 Bit Score: 193.57 E-value: 7.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 308 MVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSS 387
Cdd:pfam12349 1 MVKSKFGLGLAGVIIVLASVASSLGLCAYFGLPLTLIISEVIPFLVLAIGVDNIFLLVKAVVRTPRSLDVSERIAEALGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932902 388 ESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRMELADL 452
Cdd:pfam12349 81 VGPSITLTSLTEILAFLLGALTDMPAVQEFCLFAAVAVLFDFLLQMTFFVAVLSLDIRRLESNRL 145
|
|
| WD40 super family |
cl29593 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1078-1235 |
2.22e-25 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. The actual alignment was detected with superfamily member cd00200:
Pssm-ID: 475233 [Multi-domain] Cd Length: 289 Bit Score: 107.81 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1078 HQKPITALKAAA--GRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTV-YIDQTMVLASGGQDGAICLWDVLTGSRVS 1154
Cdd:cd00200 8 HTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVaASADGTYLASGSSDKTIRLWDLETGECVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1155 HVFAHRGDVTSLTCTTSC--VISSGLDDLISIWDRSTGIKFYSIQQDLGCGASLGVISDNLLVTGGQ--GCVSFWDLNYG 1230
Cdd:cd00200 88 TLTGHTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSqdGTIKLWDLRTG 167
|
....*
gi 66932902 1231 DLLQT 1235
Cdd:cd00200 168 KCVAT 172
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
893-1235 |
1.64e-23 |
|
WD40 repeat [General function prediction only]; :
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.61 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 893 PEPRHRAVCGRSRDSPGYDFSCLVQRVYQEEGLAAVCTPALRPPSPGPVLSQAPEDEGGSPEKGSPSLAWAPSAEGSIWS 972
Cdd:COG2319 4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 973 LELQ--GNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFLD--KRIVAARLNGSLDFFSLETHTALSPLqfRGT 1048
Cdd:COG2319 84 VAFSpdGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTL--TGH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1049 PGRGSSPA-SP----VYSSS--------DTVACHLTHTVPcAHQKPITALK-AAAGR-LVTGSQDHTLRVFRLEDSCCLF 1113
Cdd:COG2319 162 SGAVTSVAfSPdgklLASGSddgtvrlwDLATGKLLRTLT-GHTGAVRSVAfSPDGKlLASGSADGTVRLWDLATGKLLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1114 TLQGHSGAITTVYI--DQTMvLASGGQDGAICLWDVLTGSRVSHVFAHRGDVTSLTCTT--SCVISSGLDDLISIWDRST 1189
Cdd:COG2319 241 TLTGHSGSVRSVAFspDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPdgKLLASGSDDGTVRLWDLAT 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 66932902 1190 GIKFYSIQQDLGCGASLGVISD-NLLVTGGQ-GCVSFWDLNYGDLLQT 1235
Cdd:COG2319 320 GKLLRTLTGHTGAVRSVAFSPDgKTLASGSDdGTVRLWDLATGELLRT 367
|
|
| 2A060601 super family |
cl36767 |
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ... |
11-466 |
5.56e-22 |
|
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in eukaryotes. The defective protein has been associated with Niemann-Pick disease which is described in humans as autosomal recessive lipidosis. It is characterized by the lysosomal accumulation of unestrified cholesterol. It is an integral membrane protein, which indicates that this protein is most likely involved in cholesterol transport or acts as some component of cholesterol homeostasis. [Transport and binding proteins, Other] The actual alignment was detected with superfamily member TIGR00917:
Pssm-ID: 273337 [Multi-domain] Cd Length: 1205 Bit Score: 103.45 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 11 ISRAFYNHGLLCASYPIPIILFTGFCILACCYPLLKLPLPgtgpvefTTPVKDYSPPpvdsDRKQGEPTEQPEWYVGaPV 90
Cdd:TIGR00917 309 LARFFGKYGIWVARHPTLVICLSVSVVLLLCVGLIRFKVE-------TRPVKLWVAP----GSRAALEKQYFDTHFG-PF 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 91 AYVQQIFVKSSVFPWHK---NLLAVDVfrspLSRAFQLVEEIRNHVLRDSSGIRSLEELCLQVTDllPGlrklrnllpeh 167
Cdd:TIGR00917 377 YRIEQLIIATVQTSSHEkapEILTDDN----LKLLFDIQKKVSQLFANYEGELITLDSPCFKPNH--PY----------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 168 GCLLLSPGNFWQNDWERF---HADPDIIGTIHQH-EPKTLQTSATLKDllFGVP-------GKYSGVSLYTRKRMVsytI 236
Cdd:TIGR00917 440 NCFIYSTCKKLQNMYSKLkpeNYDDYGGVDYVKYcFEHFTSPESCLSA--FGGPvdpttvlGGFSGNNFSEASAFV---V 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 237 TLVFQHYHAK-------------FLGSLRARLmLLHPSPNCSLRAESLVHVHFKEEiGVAELIPLVTTYIILFAYIY--- 300
Cdd:TIGR00917 515 TFPVNNFVNKtnktekavawekaFIQLAKDEL-LPMVQATISFSAERSIEDELKRE-STADVITIAISYLVMFAYISltl 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 301 -FSTR-KIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSV---------- 368
Cdd:TIGR00917 593 gDSPRlKSLYVTSKVLLGLSGILIVMLSVLGSVGVFSAVGLKSTLIIMEVIPFLVLAVGVDNIFILVFFYfyleyfyrqv 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 369 -VSTPVDLEVKLRIAQGLSSESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRM 447
Cdd:TIGR00917 673 gVDNEQELTLERRLSRALMEVGPSITLASLSEILAFALGALIKMPAVRVFSMFAVLAVFLDFLLQITAFVALLVLDFKRT 752
|
490
....*....|....*....
gi 66932902 448 EladlNKRLPPEACLPSAK 466
Cdd:TIGR00917 753 E----DKRVDCFPCIKTSK 767
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
771-802 |
1.98e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. :
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 37.29 E-value: 1.98e-03
10 20 30
....*....|....*....|....*....|....
gi 66932902 771 VLRGHLMDIECLA--SDGMLLVSCCLAGHVCVWD 802
Cdd:smart00320 7 TLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Sterol-sensing |
pfam12349 |
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ... |
308-452 |
7.30e-57 |
|
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins (SREBPs) are membrane-bound transcription factors that promote lipid synthesis in animal cells. They are embedded in the membranes of the endoplasmic reticulum (ER) in a helical hairpin orientation and are released from the ER by a two-step proteolytic process. Proteolysis begins when the SREBPs are cleaved at Site-1, which is located at a leucine residue in the middle of the hydrophobic loop in the lumen of the ER. Upon proteolytic processing SREBP can activate the expression of genes involved in cholesterol biosynthesis and uptake. SCAP stimulates cleavage of SREBPs via fusion of the their two C-termini. This domain is the transmembrane region that traverses the membrane eight times and is the sterol-sensing domain of the cleavage protein. WD40 domains are found towards the C-terminus.
Pssm-ID: 463544 [Multi-domain] Cd Length: 153 Bit Score: 193.57 E-value: 7.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 308 MVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSS 387
Cdd:pfam12349 1 MVKSKFGLGLAGVIIVLASVASSLGLCAYFGLPLTLIISEVIPFLVLAIGVDNIFLLVKAVVRTPRSLDVSERIAEALGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932902 388 ESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRMELADL 452
Cdd:pfam12349 81 VGPSITLTSLTEILAFLLGALTDMPAVQEFCLFAAVAVLFDFLLQMTFFVAVLSLDIRRLESNRL 145
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1078-1235 |
2.22e-25 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 107.81 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1078 HQKPITALKAAA--GRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTV-YIDQTMVLASGGQDGAICLWDVLTGSRVS 1154
Cdd:cd00200 8 HTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVaASADGTYLASGSSDKTIRLWDLETGECVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1155 HVFAHRGDVTSLTCTTSC--VISSGLDDLISIWDRSTGIKFYSIQQDLGCGASLGVISDNLLVTGGQ--GCVSFWDLNYG 1230
Cdd:cd00200 88 TLTGHTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSqdGTIKLWDLRTG 167
|
....*
gi 66932902 1231 DLLQT 1235
Cdd:cd00200 168 KCVAT 172
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
893-1235 |
1.64e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.61 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 893 PEPRHRAVCGRSRDSPGYDFSCLVQRVYQEEGLAAVCTPALRPPSPGPVLSQAPEDEGGSPEKGSPSLAWAPSAEGSIWS 972
Cdd:COG2319 4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 973 LELQ--GNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFLD--KRIVAARLNGSLDFFSLETHTALSPLqfRGT 1048
Cdd:COG2319 84 VAFSpdGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTL--TGH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1049 PGRGSSPA-SP----VYSSS--------DTVACHLTHTVPcAHQKPITALK-AAAGR-LVTGSQDHTLRVFRLEDSCCLF 1113
Cdd:COG2319 162 SGAVTSVAfSPdgklLASGSddgtvrlwDLATGKLLRTLT-GHTGAVRSVAfSPDGKlLASGSADGTVRLWDLATGKLLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1114 TLQGHSGAITTVYI--DQTMvLASGGQDGAICLWDVLTGSRVSHVFAHRGDVTSLTCTT--SCVISSGLDDLISIWDRST 1189
Cdd:COG2319 241 TLTGHSGSVRSVAFspDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPdgKLLASGSDDGTVRLWDLAT 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 66932902 1190 GIKFYSIQQDLGCGASLGVISD-NLLVTGGQ-GCVSFWDLNYGDLLQT 1235
Cdd:COG2319 320 GKLLRTLTGHTGAVRSVAFSPDgKTLASGSDdGTVRLWDLATGELLRT 367
|
|
| 2A060601 |
TIGR00917 |
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ... |
11-466 |
5.56e-22 |
|
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in eukaryotes. The defective protein has been associated with Niemann-Pick disease which is described in humans as autosomal recessive lipidosis. It is characterized by the lysosomal accumulation of unestrified cholesterol. It is an integral membrane protein, which indicates that this protein is most likely involved in cholesterol transport or acts as some component of cholesterol homeostasis. [Transport and binding proteins, Other]
Pssm-ID: 273337 [Multi-domain] Cd Length: 1205 Bit Score: 103.45 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 11 ISRAFYNHGLLCASYPIPIILFTGFCILACCYPLLKLPLPgtgpvefTTPVKDYSPPpvdsDRKQGEPTEQPEWYVGaPV 90
Cdd:TIGR00917 309 LARFFGKYGIWVARHPTLVICLSVSVVLLLCVGLIRFKVE-------TRPVKLWVAP----GSRAALEKQYFDTHFG-PF 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 91 AYVQQIFVKSSVFPWHK---NLLAVDVfrspLSRAFQLVEEIRNHVLRDSSGIRSLEELCLQVTDllPGlrklrnllpeh 167
Cdd:TIGR00917 377 YRIEQLIIATVQTSSHEkapEILTDDN----LKLLFDIQKKVSQLFANYEGELITLDSPCFKPNH--PY----------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 168 GCLLLSPGNFWQNDWERF---HADPDIIGTIHQH-EPKTLQTSATLKDllFGVP-------GKYSGVSLYTRKRMVsytI 236
Cdd:TIGR00917 440 NCFIYSTCKKLQNMYSKLkpeNYDDYGGVDYVKYcFEHFTSPESCLSA--FGGPvdpttvlGGFSGNNFSEASAFV---V 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 237 TLVFQHYHAK-------------FLGSLRARLmLLHPSPNCSLRAESLVHVHFKEEiGVAELIPLVTTYIILFAYIY--- 300
Cdd:TIGR00917 515 TFPVNNFVNKtnktekavawekaFIQLAKDEL-LPMVQATISFSAERSIEDELKRE-STADVITIAISYLVMFAYISltl 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 301 -FSTR-KIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSV---------- 368
Cdd:TIGR00917 593 gDSPRlKSLYVTSKVLLGLSGILIVMLSVLGSVGVFSAVGLKSTLIIMEVIPFLVLAVGVDNIFILVFFYfyleyfyrqv 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 369 -VSTPVDLEVKLRIAQGLSSESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRM 447
Cdd:TIGR00917 673 gVDNEQELTLERRLSRALMEVGPSITLASLSEILAFALGALIKMPAVRVFSMFAVLAVFLDFLLQITAFVALLVLDFKRT 752
|
490
....*....|....*....
gi 66932902 448 EladlNKRLPPEACLPSAK 466
Cdd:TIGR00917 753 E----DKRVDCFPCIKTSK 767
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
972-1235 |
1.31e-19 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 92.67 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 972 SLELQGNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFLDKRIVAARLNGSLDFFSLETHTALSPLQFRGTPGR 1051
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1052 G-----SSPASPVYSSSD-------TVACHLTHTVPCAHQKPITALKAAA--GRLVTGSQDHTLRVFRLEDSCCLFTLQG 1117
Cdd:COG2319 81 VlsvafSPDGRLLASASAdgtvrlwDLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTLTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1118 HSGAITTVYI--DQTMvLASGGQDGAICLWDVLTGSRVSHVFAHRGDVTSLTCTT--SCVISSGLDDLISIWDRSTGIKF 1193
Cdd:COG2319 161 HSGAVTSVAFspDGKL-LASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPdgKLLASGSADGTVRLWDLATGKLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 66932902 1194 YSIQQDLGCGASLGVISDN-LLVTGGQ-GCVSFWDLNYGDLLQT 1235
Cdd:COG2319 240 RTLTGHSGSVRSVAFSPDGrLLASGSAdGTVRLWDLATGELLRT 283
|
|
| 2A060605 |
TIGR00920 |
3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, ... |
276-442 |
8.26e-14 |
|
3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273339 [Multi-domain] Cd Length: 886 Bit Score: 76.43 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 276 FKEEIGVAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPT-LNggEIFPYLVV 354
Cdd:TIGR00920 53 FEEEYLSSDVIVMTITRCIAVLYIYYQFCNLRQLGSKYILGIAGLFTIFSSFVFSTAVIHFLGSELTgLN--EALPFFLL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 355 VIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQML 434
Cdd:TIGR00920 131 LIDLSKASALAKFALSSNSQDEVRDNIARGMAILGPTITLDTVVETLVIGVGTMSGVRRLEVLCCFGCMSVLANYFVFMT 210
|
....*...
gi 66932902 435 FFTTVLSI 442
Cdd:TIGR00920 211 FFPACLSL 218
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1108-1146 |
1.57e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 43.07 E-value: 1.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 66932902 1108 DSCCLFTLQGHSGAITTVYIDQT-MVLASGGQDGAICLWD 1146
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDgKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1111-1146 |
7.13e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 41.18 E-value: 7.13e-05
10 20 30
....*....|....*....|....*....|....*..
gi 66932902 1111 CLFTLQGHSGAITTVYIDQT-MVLASGGQDGAICLWD 1146
Cdd:pfam00400 3 LLKTLEGHTGSVTSLAFSPDgKLLASGSDDGTVKVWD 39
|
|
| MMPL |
COG1033 |
Predicted exporter protein, RND superfamily [General function prediction only]; |
285-442 |
9.57e-04 |
|
Predicted exporter protein, RND superfamily [General function prediction only];
Pssm-ID: 440656 [Multi-domain] Cd Length: 767 Bit Score: 43.70 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 285 LIPLVTTYIILFAYIYFstrkidmvKSKWGLALAaVVTVLSSLLMSVGLCTLFG--LTPTLNggeIFPYLVVVIGLENVL 362
Cdd:COG1033 223 FFPLALLLILLLLFLFF--------RSLRGVLLP-LLVVLLAVIWTLGLMGLLGipLSPLTI---LVPPLLLAIGIDYGI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 363 -VLTKsvvstpvdleVKLRIAQGLSSESwsIMKNMATELGI-IL-------IGYFTL----VPAIQEFCLFAVVGLVSDF 429
Cdd:COG1033 291 hLLNR----------YREERRKGLDKRE--ALREALRKLGPpVLltslttaIGFLSLlfsdIPPIRDFGIVAAIGVLLAF 358
|
170
....*....|...
gi 66932902 430 FLQMLFFTTVLSI 442
Cdd:COG1033 359 LTSLTLLPALLSL 371
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
771-802 |
1.98e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 37.29 E-value: 1.98e-03
10 20 30
....*....|....*....|....*....|....
gi 66932902 771 VLRGHLMDIECLA--SDGMLLVSCCLAGHVCVWD 802
Cdd:smart00320 7 TLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
771-813 |
3.62e-03 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 40.78 E-value: 3.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66932902 771 VLRGHLMDIECLA--SDGMLLVSCCLAGHVCVWDAQTGDCLTRIP 813
Cdd:cd00200 214 TLRGHENGVNSVAfsPDGYLLASGSEDGTIRVWDLRTGECVQTLS 258
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Sterol-sensing |
pfam12349 |
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ... |
308-452 |
7.30e-57 |
|
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins (SREBPs) are membrane-bound transcription factors that promote lipid synthesis in animal cells. They are embedded in the membranes of the endoplasmic reticulum (ER) in a helical hairpin orientation and are released from the ER by a two-step proteolytic process. Proteolysis begins when the SREBPs are cleaved at Site-1, which is located at a leucine residue in the middle of the hydrophobic loop in the lumen of the ER. Upon proteolytic processing SREBP can activate the expression of genes involved in cholesterol biosynthesis and uptake. SCAP stimulates cleavage of SREBPs via fusion of the their two C-termini. This domain is the transmembrane region that traverses the membrane eight times and is the sterol-sensing domain of the cleavage protein. WD40 domains are found towards the C-terminus.
Pssm-ID: 463544 [Multi-domain] Cd Length: 153 Bit Score: 193.57 E-value: 7.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 308 MVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSS 387
Cdd:pfam12349 1 MVKSKFGLGLAGVIIVLASVASSLGLCAYFGLPLTLIISEVIPFLVLAIGVDNIFLLVKAVVRTPRSLDVSERIAEALGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66932902 388 ESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRMELADL 452
Cdd:pfam12349 81 VGPSITLTSLTEILAFLLGALTDMPAVQEFCLFAAVAVLFDFLLQMTFFVAVLSLDIRRLESNRL 145
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1078-1235 |
2.22e-25 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 107.81 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1078 HQKPITALKAAA--GRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTV-YIDQTMVLASGGQDGAICLWDVLTGSRVS 1154
Cdd:cd00200 8 HTGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVaASADGTYLASGSSDKTIRLWDLETGECVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1155 HVFAHRGDVTSLTCTTSC--VISSGLDDLISIWDRSTGIKFYSIQQDLGCGASLGVISDNLLVTGGQ--GCVSFWDLNYG 1230
Cdd:cd00200 88 TLTGHTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSqdGTIKLWDLRTG 167
|
....*
gi 66932902 1231 DLLQT 1235
Cdd:cd00200 168 KCVAT 172
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
893-1235 |
1.64e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.61 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 893 PEPRHRAVCGRSRDSPGYDFSCLVQRVYQEEGLAAVCTPALRPPSPGPVLSQAPEDEGGSPEKGSPSLAWAPSAEGSIWS 972
Cdd:COG2319 4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 973 LELQ--GNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFLD--KRIVAARLNGSLDFFSLETHTALSPLqfRGT 1048
Cdd:COG2319 84 VAFSpdGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTL--TGH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1049 PGRGSSPA-SP----VYSSS--------DTVACHLTHTVPcAHQKPITALK-AAAGR-LVTGSQDHTLRVFRLEDSCCLF 1113
Cdd:COG2319 162 SGAVTSVAfSPdgklLASGSddgtvrlwDLATGKLLRTLT-GHTGAVRSVAfSPDGKlLASGSADGTVRLWDLATGKLLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1114 TLQGHSGAITTVYI--DQTMvLASGGQDGAICLWDVLTGSRVSHVFAHRGDVTSLTCTT--SCVISSGLDDLISIWDRST 1189
Cdd:COG2319 241 TLTGHSGSVRSVAFspDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPdgKLLASGSDDGTVRLWDLAT 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 66932902 1190 GIKFYSIQQDLGCGASLGVISD-NLLVTGGQ-GCVSFWDLNYGDLLQT 1235
Cdd:COG2319 320 GKLLRTLTGHTGAVRSVAFSPDgKTLASGSDdGTVRLWDLATGELLRT 367
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
967-1235 |
3.64e-23 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 101.26 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 967 EGSIWSLEL--QGNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFL--DKRIVAARLNGSLDFFSLEThtalsp 1042
Cdd:cd00200 9 TGGVTCVAFspDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASadGTYLASGSSDKTIRLWDLET------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1043 lqfrgtpgrgsspaspvysssdtvaCHLTHTVPCaHQKPITALKAAAGR--LVTGSQDHTLRVFRLEDSCCLFTLQGHSG 1120
Cdd:cd00200 83 -------------------------GECVRTLTG-HTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLTTLRGHTD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1121 AITTVYIDQT-MVLASGGQDGAICLWDVLTGSRVsHVF-AHRGDVTSLTC--TTSCVISSGLDDLISIWDRSTGIKFYSI 1196
Cdd:cd00200 137 WVNSVAFSPDgTFVASSSQDGTIKLWDLRTGKCV-ATLtGHTGEVNSVAFspDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 66932902 1197 QQDLGCGASLGVISDNLLVTGG--QGCVSFWDLNYGDLLQT 1235
Cdd:cd00200 216 RGHENGVNSVAFSPDGYLLASGseDGTIRVWDLRTGECVQT 256
|
|
| 2A060601 |
TIGR00917 |
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ... |
11-466 |
5.56e-22 |
|
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in eukaryotes. The defective protein has been associated with Niemann-Pick disease which is described in humans as autosomal recessive lipidosis. It is characterized by the lysosomal accumulation of unestrified cholesterol. It is an integral membrane protein, which indicates that this protein is most likely involved in cholesterol transport or acts as some component of cholesterol homeostasis. [Transport and binding proteins, Other]
Pssm-ID: 273337 [Multi-domain] Cd Length: 1205 Bit Score: 103.45 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 11 ISRAFYNHGLLCASYPIPIILFTGFCILACCYPLLKLPLPgtgpvefTTPVKDYSPPpvdsDRKQGEPTEQPEWYVGaPV 90
Cdd:TIGR00917 309 LARFFGKYGIWVARHPTLVICLSVSVVLLLCVGLIRFKVE-------TRPVKLWVAP----GSRAALEKQYFDTHFG-PF 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 91 AYVQQIFVKSSVFPWHK---NLLAVDVfrspLSRAFQLVEEIRNHVLRDSSGIRSLEELCLQVTDllPGlrklrnllpeh 167
Cdd:TIGR00917 377 YRIEQLIIATVQTSSHEkapEILTDDN----LKLLFDIQKKVSQLFANYEGELITLDSPCFKPNH--PY----------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 168 GCLLLSPGNFWQNDWERF---HADPDIIGTIHQH-EPKTLQTSATLKDllFGVP-------GKYSGVSLYTRKRMVsytI 236
Cdd:TIGR00917 440 NCFIYSTCKKLQNMYSKLkpeNYDDYGGVDYVKYcFEHFTSPESCLSA--FGGPvdpttvlGGFSGNNFSEASAFV---V 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 237 TLVFQHYHAK-------------FLGSLRARLmLLHPSPNCSLRAESLVHVHFKEEiGVAELIPLVTTYIILFAYIY--- 300
Cdd:TIGR00917 515 TFPVNNFVNKtnktekavawekaFIQLAKDEL-LPMVQATISFSAERSIEDELKRE-STADVITIAISYLVMFAYISltl 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 301 -FSTR-KIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSV---------- 368
Cdd:TIGR00917 593 gDSPRlKSLYVTSKVLLGLSGILIVMLSVLGSVGVFSAVGLKSTLIIMEVIPFLVLAVGVDNIFILVFFYfyleyfyrqv 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 369 -VSTPVDLEVKLRIAQGLSSESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRM 447
Cdd:TIGR00917 673 gVDNEQELTLERRLSRALMEVGPSITLASLSEILAFALGALIKMPAVRVFSMFAVLAVFLDFLLQITAFVALLVLDFKRT 752
|
490
....*....|....*....
gi 66932902 448 EladlNKRLPPEACLPSAK 466
Cdd:TIGR00917 753 E----DKRVDCFPCIKTSK 767
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
976-1186 |
1.89e-20 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 93.17 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 976 QGNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFLDKR--IVAARLNGSLDFFSLETHTALSPLQFRGTPGRG- 1052
Cdd:cd00200 62 DGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSv 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1053 -SSPASPVYSSS---------DTVACHLTHTVPcAHQKPITALKAAA--GRLVTGSQDHTLRVFRLEDSCCLFTLQGHSG 1120
Cdd:cd00200 142 aFSPDGTFVASSsqdgtiklwDLRTGKCVATLT-GHTGEVNSVAFSPdgEKLLSSSSDGTIKLWDLSTGKCLGTLRGHEN 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66932902 1121 AITTV-YIDQTMVLASGGQDGAICLWDVLTGSRVSHVFAHRGDVTSLTC--TTSCVISSGLDDLISIWD 1186
Cdd:cd00200 221 GVNSVaFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWspDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
972-1235 |
1.31e-19 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 92.67 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 972 SLELQGNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFLDKRIVAARLNGSLDFFSLETHTALSPLQFRGTPGR 1051
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1052 G-----SSPASPVYSSSD-------TVACHLTHTVPCAHQKPITALKAAA--GRLVTGSQDHTLRVFRLEDSCCLFTLQG 1117
Cdd:COG2319 81 VlsvafSPDGRLLASASAdgtvrlwDLATGLLLRTLTGHTGAVRSVAFSPdgKTLASGSADGTVRLWDLATGKLLRTLTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1118 HSGAITTVYI--DQTMvLASGGQDGAICLWDVLTGSRVSHVFAHRGDVTSLTCTT--SCVISSGLDDLISIWDRSTGIKF 1193
Cdd:COG2319 161 HSGAVTSVAFspDGKL-LASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPdgKLLASGSADGTVRLWDLATGKLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 66932902 1194 YSIQQDLGCGASLGVISDN-LLVTGGQ-GCVSFWDLNYGDLLQT 1235
Cdd:COG2319 240 RTLTGHSGSVRSVAFSPDGrLLASGSAdGTVRLWDLATGELLRT 283
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
967-1189 |
8.08e-19 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 90.36 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 967 EGSIWSLEL--QGNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFL--DKRIVAARLNGSLDFFSLETHTALSP 1042
Cdd:COG2319 162 SGAVTSVAFspDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSpdGKLLASGSADGTVRLWDLATGKLLRT 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1043 LqfRGTPGRGSSPA-SP-----VYSSSDTVAC-------HLTHTVPcAHQKPITALKAAA-GR-LVTGSQDHTLRVFRLE 1107
Cdd:COG2319 242 L--TGHSGSVRSVAfSPdgrllASGSADGTVRlwdlatgELLRTLT-GHSGGVNSVAFSPdGKlLASGSDDGTVRLWDLA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1108 DSCCLFTLQGHSGAITTVYI---DQTmvLASGGQDGAICLWDVLTGSRVSHVFAHRGDVTSLTCTT--SCVISSGLDDLI 1182
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFspdGKT--LASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPdgRTLASGSADGTV 396
|
....*..
gi 66932902 1183 SIWDRST 1189
Cdd:COG2319 397 RLWDLAT 403
|
|
| Patched |
pfam02460 |
Patched family; The transmembrane protein Patched is a receptor for the morphogene Sonic ... |
284-533 |
1.27e-17 |
|
Patched family; The transmembrane protein Patched is a receptor for the morphogene Sonic Hedgehog. This protein associates with the smoothened protein to transduce hedgehog signals.
Pssm-ID: 308203 [Multi-domain] Cd Length: 793 Bit Score: 88.57 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 284 ELIP-LVTTYIILFAY-----IYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLtPTLNGGEIFPYLVVVIG 357
Cdd:pfam02460 214 TLTPfFVIGFFLLLTFsiivsVTLSSYTIDWVRSKPILAALGLLSPVMAIVSSFGLLFWMGF-PFNSIVCVTPFLVLAIG 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 358 LENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFT 437
Cdd:pfam02460 293 VDDMFLMVAAWQRTTATLSVKKRMGEALSEAGVSITITSLTDVLSFGIGTYTPTPAIQLFCAYTAVAIFFDFIYQITFFA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 438 TVLSIdirrMELADLNKRLPPEACLPSakpvgQPTRYERQLAVRPSTPHTITLQPSSFRNLRLPkrlrvvyFLARTRLaq 517
Cdd:pfam02460 373 AIMAI----CAKPEAEGRHCLFVWATS-----SPQRIDSEGSEPDKSHNIEQLKSRFFLDIYCP-------FLLNPSV-- 434
|
250
....*....|....*..
gi 66932902 518 RLIMAGT-VVWIGILVY 533
Cdd:pfam02460 435 RVCMLVLfVVYIAIAIY 451
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
959-1147 |
5.53e-16 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 81.88 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 959 SLAWAPsaegsiwslelQGNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFL--DKRIVAARLNGSLDFFSLET 1036
Cdd:COG2319 209 SVAFSP-----------DGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSpdGRLLASGSADGTVRLWDLAT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1037 HTALSPLqfRGTPGRGSSPA-SP-----VYSSSDTVAC-------HLTHTVPcAHQKPITALKAAA--GRLVTGSQDHTL 1101
Cdd:COG2319 278 GELLRTL--TGHSGGVNSVAfSPdgkllASGSDDGTVRlwdlatgKLLRTLT-GHTGAVRSVAFSPdgKTLASGSDDGTV 354
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 66932902 1102 RVFRLEDSCCLFTLQGHSGAITTVYI--DQTMvLASGGQDGAICLWDV 1147
Cdd:COG2319 355 RLWDLATGELLRTLTGHTGAVTSVAFspDGRT-LASGSADGTVRLWDL 401
|
|
| 2A060605 |
TIGR00920 |
3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, ... |
276-442 |
8.26e-14 |
|
3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273339 [Multi-domain] Cd Length: 886 Bit Score: 76.43 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 276 FKEEIGVAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPT-LNggEIFPYLVV 354
Cdd:TIGR00920 53 FEEEYLSSDVIVMTITRCIAVLYIYYQFCNLRQLGSKYILGIAGLFTIFSSFVFSTAVIHFLGSELTgLN--EALPFFLL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 355 VIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQML 434
Cdd:TIGR00920 131 LIDLSKASALAKFALSSNSQDEVRDNIARGMAILGPTITLDTVVETLVIGVGTMSGVRRLEVLCCFGCMSVLANYFVFMT 210
|
....*...
gi 66932902 435 FFTTVLSI 442
Cdd:TIGR00920 211 FFPACLSL 218
|
|
| 2A060602 |
TIGR00918 |
The Eukaryotic (Putative) Sterol Transporter (EST) Family; |
286-491 |
1.27e-13 |
|
The Eukaryotic (Putative) Sterol Transporter (EST) Family;
Pssm-ID: 273338 [Multi-domain] Cd Length: 1145 Bit Score: 76.07 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 286 IPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLT 365
Cdd:TIGR00918 400 IRIVSGYLLMLAYACLTMLRWDCAKSQGSVGLAGVLLVALSVAAGLGLCALLGISFNAATTQVLPFLALGVGVDDVFLLA 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 366 KSVVSTPVDLEVKLRIAQGLSSESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIR 445
Cdd:TIGR00918 480 HAFSETGQNIPFEERTGECLKRTGASVVLTSISNVTAFFMAALIPIPALRAFSLQAAIVVVFNFAAVLLVFPAILSLDLR 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 66932902 446 RMEladlNKRLPPEACL--PSAKPVGQ--PTRYERQLAVRPSTPH-TITLQ 491
Cdd:TIGR00918 560 RRE----DRRLDIFCCFfsPCSARVIQiePQAYADGSAPPVYSSHmQSTVQ 606
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1111-1235 |
5.62e-13 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 70.83 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1111 CLFTLQGHSGAITTV-YIDQTMVLASGGQDGAICLWDVLTGSRVSHVFAHRGDVTSLTCT--TSCVISSGLDDLISIWDR 1187
Cdd:cd00200 1 LRRTLKGHTGGVTCVaFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASadGTYLASGSSDKTIRLWDL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 66932902 1188 STGIKFYSIQQDLGCGASLGVISDNLLVTGG--QGCVSFWDLNYGDLLQT 1235
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSsrDKTIKVWDVETGKCLTT 130
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1069-1236 |
1.48e-11 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 68.01 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1069 HLTHTVPCAHQKPITALKAAAGRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTV-YIDQTMVLASGGQDGAICLWDV 1147
Cdd:COG2319 28 LLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVaFSPDGRLLASASADGTVRLWDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 1148 LTGSRVSHVFAHRGDVTSLTCT--TSCVISSGLDDLISIWDRSTGIKFYSIQQDLGCGASLGVISD-NLLVTGGQ-GCVS 1223
Cdd:COG2319 108 ATGLLLRTLTGHTGAVRSVAFSpdGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDgKLLASGSDdGTVR 187
|
170
....*....|...
gi 66932902 1224 FWDLNYGDLLQTV 1236
Cdd:COG2319 188 LWDLATGKLLRTL 200
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1108-1146 |
1.57e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 43.07 E-value: 1.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 66932902 1108 DSCCLFTLQGHSGAITTVYIDQT-MVLASGGQDGAICLWD 1146
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDgKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1111-1146 |
7.13e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 41.18 E-value: 7.13e-05
10 20 30
....*....|....*....|....*....|....*..
gi 66932902 1111 CLFTLQGHSGAITTVYIDQT-MVLASGGQDGAICLWD 1146
Cdd:pfam00400 3 LLKTLEGHTGSVTSLAFSPDgKLLASGSDDGTVKVWD 39
|
|
| MMPL |
COG1033 |
Predicted exporter protein, RND superfamily [General function prediction only]; |
285-442 |
9.57e-04 |
|
Predicted exporter protein, RND superfamily [General function prediction only];
Pssm-ID: 440656 [Multi-domain] Cd Length: 767 Bit Score: 43.70 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 285 LIPLVTTYIILFAYIYFstrkidmvKSKWGLALAaVVTVLSSLLMSVGLCTLFG--LTPTLNggeIFPYLVVVIGLENVL 362
Cdd:COG1033 223 FFPLALLLILLLLFLFF--------RSLRGVLLP-LLVVLLAVIWTLGLMGLLGipLSPLTI---LVPPLLLAIGIDYGI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932902 363 -VLTKsvvstpvdleVKLRIAQGLSSESwsIMKNMATELGI-IL-------IGYFTL----VPAIQEFCLFAVVGLVSDF 429
Cdd:COG1033 291 hLLNR----------YREERRKGLDKRE--ALREALRKLGPpVLltslttaIGFLSLlfsdIPPIRDFGIVAAIGVLLAF 358
|
170
....*....|...
gi 66932902 430 FLQMLFFTTVLSI 442
Cdd:COG1033 359 LTSLTLLPALLSL 371
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
771-802 |
1.98e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 37.29 E-value: 1.98e-03
10 20 30
....*....|....*....|....*....|....
gi 66932902 771 VLRGHLMDIECLA--SDGMLLVSCCLAGHVCVWD 802
Cdd:smart00320 7 TLKGHTGPVTSVAfsPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
771-813 |
3.62e-03 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 40.78 E-value: 3.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66932902 771 VLRGHLMDIECLA--SDGMLLVSCCLAGHVCVWDAQTGDCLTRIP 813
Cdd:cd00200 214 TLRGHENGVNSVAfsPDGYLLASGSEDGTIRVWDLRTGECVQTLS 258
|
|
|