NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|755509632|ref|XP_011248556|]
View 

protein dispatched homolog 3 isoform X1 [Mus musculus]

Protein Classification

RND transporter family protein( domain architecture ID 1001856)

resistance-nodulation-cell division (RND) transporter family protein

Gene Ontology:  GO:0016020|GO:0055085
PubMed:  10941792
TCDB:  2.A.6

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MMPL super family cl34072
Predicted exporter protein, RND superfamily [General function prediction only];
386-571 7.18e-28

Predicted exporter protein, RND superfamily [General function prediction only];


The actual alignment was detected with superfamily member COG1033:

Pssm-ID: 440656 [Multi-domain]  Cd Length: 767  Bit Score: 120.35  E-value: 7.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 386 AMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSCLVAL-FLYhvV 464
Cdd:COG1033  188 AIIAKYEDPGVEVYLTGFPVLRGDIAEAIQSDLAIFFPLALLLILLLLFLFFRSLRGVLLPLLVVLLAVIWTLgLMG--L 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 465 FGIQyLGILNGVAAFVIVGIGVDDVFVFINTYRQAT-HLEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVH 543
Cdd:COG1033  266 LGIP-LSPLTILVPPLLLAIGIDYGIHLLNRYREERrKGLDKREALREALRKLGPPVLLTSLTTAIGFLSLLFSDIPPIR 344
                        170       180
                 ....*....|....*....|....*...
gi 755509632 544 DFGLFMSLIVTCCWLAVLFTMPAALGLW 571
Cdd:COG1033  345 DFGIVAAIGVLLAFLTSLTLLPALLSLL 372
 
Name Accession Description Interval E-value
MMPL COG1033
Predicted exporter protein, RND superfamily [General function prediction only];
386-571 7.18e-28

Predicted exporter protein, RND superfamily [General function prediction only];


Pssm-ID: 440656 [Multi-domain]  Cd Length: 767  Bit Score: 120.35  E-value: 7.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 386 AMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSCLVAL-FLYhvV 464
Cdd:COG1033  188 AIIAKYEDPGVEVYLTGFPVLRGDIAEAIQSDLAIFFPLALLLILLLLFLFFRSLRGVLLPLLVVLLAVIWTLgLMG--L 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 465 FGIQyLGILNGVAAFVIVGIGVDDVFVFINTYRQAT-HLEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVH 543
Cdd:COG1033  266 LGIP-LSPLTILVPPLLLAIGIDYGIHLLNRYREERrKGLDKREALREALRKLGPPVLLTSLTTAIGFLSLLFSDIPPIR 344
                        170       180
                 ....*....|....*....|....*...
gi 755509632 544 DFGLFMSLIVTCCWLAVLFTMPAALGLW 571
Cdd:COG1033  345 DFGIVAAIGVLLAFLTSLTLLPALLSLL 372
Sterol-sensing pfam12349
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ...
440-570 1.36e-14

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: 71.85  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  440 VFLSFFGIASIGLS--CLVALFLYhvvFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATHLEDPQLRMIHTIQTAG 517
Cdd:pfam12349   6 FGLGLAGVIIVLASvaSSLGLCAY---FGLPLTLIISEVIPFLVLAIGVDNIFLLVKAVVRTPRSLDVSERIAEALGEVG 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755509632  518 KATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVTCCWLAVLFTMPAALGL 570
Cdd:pfam12349  83 PSITLTSLTEILAFLLGALTDMPAVQEFCLFAAVAVLFDFLLQMTFFVAVLSL 135
2A067 TIGR00921
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized ...
396-570 1.10e-10

The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. They fall into seven phylogenetic families, this family (2.A.6.7) consists of uncharacterised putative transporters, largely in the Archaea. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273340 [Multi-domain]  Cd Length: 719  Bit Score: 65.24  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  396 VQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSCLVALfLYHVVFGIQYLGILNG 475
Cdd:TIGR00921 547 VKVGVTGLPVAFAEMHELVNEGMRRMTIAGAILVLMILLAVFRNPIKAVFPLIAIGSGILWAI-GLMGLRGIPSFLAMAT 625
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  476 VAAfVIVGIGVDDVFVFINTYRQATHLEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVTC 555
Cdd:TIGR00921 626 TIS-IILGLGMDYSIHLAERYFEERKEHGPKEAITHTMERTGPGILFSGLTTAGGFLSLLLSHFPIMRNFGLVQGIGVLS 704
                         170
                  ....*....|....*
gi 755509632  556 CWLAVLFTMPAALGL 570
Cdd:TIGR00921 705 SLTAALVVFPALLVL 719
 
Name Accession Description Interval E-value
MMPL COG1033
Predicted exporter protein, RND superfamily [General function prediction only];
386-571 7.18e-28

Predicted exporter protein, RND superfamily [General function prediction only];


Pssm-ID: 440656 [Multi-domain]  Cd Length: 767  Bit Score: 120.35  E-value: 7.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 386 AMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSCLVAL-FLYhvV 464
Cdd:COG1033  188 AIIAKYEDPGVEVYLTGFPVLRGDIAEAIQSDLAIFFPLALLLILLLLFLFFRSLRGVLLPLLVVLLAVIWTLgLMG--L 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 465 FGIQyLGILNGVAAFVIVGIGVDDVFVFINTYRQAT-HLEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVH 543
Cdd:COG1033  266 LGIP-LSPLTILVPPLLLAIGIDYGIHLLNRYREERrKGLDKREALREALRKLGPPVLLTSLTTAIGFLSLLFSDIPPIR 344
                        170       180
                 ....*....|....*....|....*...
gi 755509632 544 DFGLFMSLIVTCCWLAVLFTMPAALGLW 571
Cdd:COG1033  345 DFGIVAAIGVLLAFLTSLTLLPALLSLL 372
MMPL COG1033
Predicted exporter protein, RND superfamily [General function prediction only];
393-571 2.74e-19

Predicted exporter protein, RND superfamily [General function prediction only];


Pssm-ID: 440656 [Multi-domain]  Cd Length: 767  Bit Score: 93.00  E-value: 2.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 393 TSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLScLVALFLYHVVFGIQyLGI 472
Cdd:COG1033  582 PDGVEVTLTGSAVLFAAINESVIESQIRSLLLALLLIFLLLLLAFRSLRLGLISLIPNLLP-ILLTFGLMGLLGIP-LNI 659
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 473 LNGVAAFVIVGIGVDDVFVFINTYRQA-THLEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSL 551
Cdd:COG1033  660 ATAVVASIALGIGVDYTIHFLSRYREErRKGGDLEEAIRRALRTTGKAILFTSLTLAAGFGVLLFSSFPPLADFGLLLAL 739
                        170       180
                 ....*....|....*....|
gi 755509632 552 IVTCCWLAVLFTMPAALGLW 571
Cdd:COG1033  740 GLLVALLAALLLLPALLLLL 759
Sterol-sensing pfam12349
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ...
440-570 1.36e-14

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: 71.85  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  440 VFLSFFGIASIGLS--CLVALFLYhvvFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATHLEDPQLRMIHTIQTAG 517
Cdd:pfam12349   6 FGLGLAGVIIVLASvaSSLGLCAY---FGLPLTLIISEVIPFLVLAIGVDNIFLLVKAVVRTPRSLDVSERIAEALGEVG 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755509632  518 KATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVTCCWLAVLFTMPAALGL 570
Cdd:pfam12349  83 PSITLTSLTEILAFLLGALTDMPAVQEFCLFAAVAVLFDFLLQMTFFVAVLSL 135
Patched pfam02460
Patched family; The transmembrane protein Patched is a receptor for the morphogene Sonic ...
367-586 3.19e-13

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: 73.54  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  367 DDRWEEQRAKFqsFVVTYVAMLAKQSTSK-VQVLYGGTDLFDYEVRRtfNNDMLLAFISSSCIAALVYILTSCSVFLSFF 445
Cdd:pfam02460 166 DEEEVEEDSKE--WEDELSQLLHNKYASEhIQFTIFHDQILNDELVR--NALTLTPFFVIGFFLLLTFSIIVSVTLSSYT 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  446 -------------GIASIGLSCLVAL-FLYhvVFGIQYLGILNgVAAFVIVGIGVDDVFVFINTYRQATHLEDPQLRMIH 511
Cdd:pfam02460 242 idwvrskpilaalGLLSPVMAIVSSFgLLF--WMGFPFNSIVC-VTPFLVLAIGVDDMFLMVAAWQRTTATLSVKKRMGE 318
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755509632  512 TIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVTCCWLAVLfTMPAALglwSLYMAPLESSCQNSC 586
Cdd:pfam02460 319 ALSEAGVSITITSLTDVLSFGIGTYTPTPAIQLFCAYTAVAIFFDFIYQI-TFFAAI---MAICAKPEAEGRHCL 389
2A067 TIGR00921
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized ...
396-570 1.10e-10

The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. They fall into seven phylogenetic families, this family (2.A.6.7) consists of uncharacterised putative transporters, largely in the Archaea. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273340 [Multi-domain]  Cd Length: 719  Bit Score: 65.24  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  396 VQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSCLVALfLYHVVFGIQYLGILNG 475
Cdd:TIGR00921 547 VKVGVTGLPVAFAEMHELVNEGMRRMTIAGAILVLMILLAVFRNPIKAVFPLIAIGSGILWAI-GLMGLRGIPSFLAMAT 625
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  476 VAAfVIVGIGVDDVFVFINTYRQATHLEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVTC 555
Cdd:TIGR00921 626 TIS-IILGLGMDYSIHLAERYFEERKEHGPKEAITHTMERTGPGILFSGLTTAGGFLSLLLSHFPIMRNFGLVQGIGVLS 704
                         170
                  ....*....|....*
gi 755509632  556 CWLAVLFTMPAALGL 570
Cdd:TIGR00921 705 SLTAALVVFPALLVL 719
2A060602 TIGR00918
The Eukaryotic (Putative) Sterol Transporter (EST) Family;
362-570 2.00e-10

The Eukaryotic (Putative) Sterol Transporter (EST) Family;


Pssm-ID: 273338 [Multi-domain]  Cd Length: 1145  Bit Score: 64.90  E-value: 2.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632   362 NYYSVDDRWEEQRAKF------QSFVVTYVAMLAKQSTSKVQVlYGGTDLfdyevrrtfnNDMLLAFISSSCI----AAL 431
Cdd:TIGR00918  339 YYKVHHIGWNEEKAAAvleawqRNFSEEVQQSLPKNSSQKILV-FSSTTL----------DDILKKFSDVSAIrivsGYL 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632   432 VYILTSCSVFL--------SFFGIASIGLSCL-VALFL-YHVVFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATH 501
Cdd:TIGR00918  408 LMLAYACLTMLrwdcaksqGSVGLAGVLLVALsVAAGLgLCALLGISFNAATTQVLPFLALGVGVDDVFLLAHAFSETGQ 487
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755509632   502 LEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVTCCWLAVLFTMPAALGL 570
Cdd:TIGR00918  488 NIPFEERTGECLKRTGASVVLTSISNVTAFFMAALIPIPALRAFSLQAAIVVVFNFAAVLLVFPAILSL 556
2A067 TIGR00921
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized ...
395-568 3.28e-10

The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. They fall into seven phylogenetic families, this family (2.A.6.7) consists of uncharacterised putative transporters, largely in the Archaea. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273340 [Multi-domain]  Cd Length: 719  Bit Score: 63.70  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  395 KVQVLYGGTDLfDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIAsiglsclVALFLYHVVFGIQ-YLGI- 472
Cdd:TIGR00921 173 KFLDVTGSPAI-NYDIEREFGKDMGTTMAISGILVVLVLLLDFKRWWRPLLPLV-------IILFGVAWVLGIMgWLGIp 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  473 ----LNGVAAfVIVGIGVDDVFVFINTYRQATHL-EDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGL 547
Cdd:TIGR00921 245 lyatTLLAVP-MLIGVGIDYGIQTLNRYEEERDIgRAKGEAIVTAVRRTGRAVLIALLTTSAGFAALALSEFPMVSEFGL 323
                         170       180
                  ....*....|....*....|.
gi 755509632  548 FMSLIVTCCWLAVLFTMPAAL 568
Cdd:TIGR00921 324 GLVAGLITAYLLTLLVLPALL 344
MMPL pfam03176
MMPL family; Members of this family are putative integral membrane proteins from bacteria. ...
381-570 1.33e-09

MMPL family; Members of this family are putative integral membrane proteins from bacteria. Several of the members are mycobacterial proteins. Many of the proteins contain two copies of this aligned region. The function of these proteins is not known, although it has been suggested that they may be involved in lipid transport.


Pssm-ID: 308676 [Multi-domain]  Cd Length: 332  Bit Score: 60.38  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  381 VVTYVAMLAKQSTSKVQVlyGGT-----DLFDYevrrtFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSC- 454
Cdd:pfam03176 109 VRDAVEQAPPPEGLKAYL--TGPaatvaDLRDA-----GDRDLGLIEAVTLVVIFIILLIVYRSVVAALLPLLTVGLSLg 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  455 ----LVALFLYHVVFGIQYLGIlnGVAAFVIVGIGVDDVFVFINTYRQATHL-EDPQLRMIHTIQTAGKATFFTSLTTAA 529
Cdd:pfam03176 182 aaqgLVAILAHILGIGLSTFAL--NLLVVLLIAVGTDYALFLVSRYREELRAgEDREEAVIRAVRGTGKVVTAAGLTVAI 259
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 755509632  530 AYAANVFSQIPAVHDFGLFMSLIVTCCWLAVLFTMPAALGL 570
Cdd:pfam03176 260 AMLALSFARLPVFAQVGPTIAIGVLVDVLAALTLLPALLAL 300
YdfJ COG2409
Predicted lipid transporter YdfJ, MMPL/SSD domain, RND superfamily [General function ...
388-570 1.28e-08

Predicted lipid transporter YdfJ, MMPL/SSD domain, RND superfamily [General function prediction only];


Pssm-ID: 441964 [Multi-domain]  Cd Length: 697  Bit Score: 58.62  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 388 LAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFF----GIASIGLSCLVALFLYHV 463
Cdd:COG2409  141 VAAAPAPGLTVYVTGPAALAADLNEAFEEDLGRAELITLPVALVVLLLVFRSLVAALLplltAGLAVGVALGLLALLAAF 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 464 V-FGIQYLGIlngvaAFVIV-GIGVDDVFVFINTYRQA-THLEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIP 540
Cdd:COG2409  221 TdVSSFAPNL-----LTMLGlGVGIDYALFLVSRYREElRAGEDREEAVARAVATAGRAVLFSGLTVAIALLGLLLAGLP 295
                        170       180       190
                 ....*....|....*....|....*....|
gi 755509632 541 AVHDFGLFMSLIVTCCWLAVLFTMPAALGL 570
Cdd:COG2409  296 FLRSMGPAAAIGVAVAVLAALTLLPALLAL 325
COG4258 COG4258
Predicted exporter [General function prediction only];
389-566 1.08e-07

Predicted exporter [General function prediction only];


Pssm-ID: 443400 [Multi-domain]  Cd Length: 783  Bit Score: 55.63  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 389 AKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSCLVALFLYHVVFGiq 468
Cdd:COG4258  222 LNAAFPGAQLLLTGAGLFAVAAAQQIKHDISTIGLISLLGILLLLLLVFRSLRPLLLGLLPVAVGALAGLAAVSLVFG-- 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 469 YLGILNGVAAFVIVGIGVDDVFVFInTYRQATHLEDPQlrmiHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGLF 548
Cdd:COG4258  300 SVHGITLGFGSSLIGVAVDYSLHYL-THRRAAGEWDPR----AALRRIWPTLLLGLLTTVLGYLALLFSPFPGLRQLGVF 374
                        170
                 ....*....|....*...
gi 755509632 549 MSLIVTCCWLAVLFTMPA 566
Cdd:COG4258  375 AAAGLLAAALTTLLWLPL 392
2A060601 TIGR00917
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ...
330-553 4.44e-07

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: 53.76  E-value: 4.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632   330 PEFYWYVDEGLSVDNLKSSllrSEILFGAPLPNYYSVDDRWEEQRAKFQSFVVTYVAMLAKQSTSKVQvlYGGTDLFDYE 409
Cdd:TIGR00917  491 PVDPTTVLGGFSGNNFSEA---SAFVVTFPVNNFVNKTNKTEKAVAWEKAFIQLAKDELLPMVQATIS--FSAERSIEDE 565
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632   410 VRRTFNNDM---------LLAFISSSC--IAALVYILTSCSVFLSFFGIASIGLSCLVALFLYHVVfGIQYLGILNGVAA 478
Cdd:TIGR00917  566 LKRESTADVitiaisylvMFAYISLTLgdSPRLKSLYVTSKVLLGLSGILIVMLSVLGSVGVFSAV-GLKSTLIIMEVIP 644
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632   479 FVIVGIGVDDVFVFINTY------RQATHLEDPQL-----RMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGL 547
Cdd:TIGR00917  645 FLVLAVGVDNIFILVFFYfyleyfYRQVGVDNEQEltlerRLSRALMEVGPSITLASLSEILAFALGALIKMPAVRVFSM 724

                   ....*.
gi 755509632   548 FMSLIV 553
Cdd:TIGR00917  725 FAVLAV 730
HpnN TIGR03480
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
404-569 1.21e-06

hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins appear to be related to the RND family of export proteins, particularly the hydrophobe/amphiphile efflux-3 (HAE3) family represented by TIGR00921.


Pssm-ID: 274598 [Multi-domain]  Cd Length: 862  Bit Score: 52.31  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  404 DLFDYEVRRTFNNDMLLafISSSCIAALVYILTSCSV----FLSFFGIASIGLSCL----------VALFLYHVVFGIQY 469
Cdd:TIGR03480 675 DLNDNEALRRFVRAVRK--VAPDATGAPVSILESGDTvvgaFLQAFIYALVAITVLllltlrrvrdVLLVLAPLLLAGLL 752
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  470 LGIL-----------NGVAAFVIVGIGVDDVFVFINTYRQATHLEDPqlrmIHTiqTAGKATFFTSLTTAAAYAANVFSQ 538
Cdd:TIGR03480 753 TVAAmvllgipfnfaNIIALPLLLGLGVDFGIYMVHRWRNGVDSGNL----LQS--STARAVFFSALTTATAFGSLAVSS 826
                         170       180       190
                  ....*....|....*....|....*....|.
gi 755509632  539 IPAVHDFGLFMSLIVTCCWLAVLFTMPAALG 569
Cdd:TIGR03480 827 HPGTASMGILLSLGLGLTLLCTLIFLPALLG 857
COG4258 COG4258
Predicted exporter [General function prediction only];
429-558 4.59e-04

Predicted exporter [General function prediction only];


Pssm-ID: 443400 [Multi-domain]  Cd Length: 783  Bit Score: 43.69  E-value: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632 429 AALVYILTSCSVFLSFFGI-------ASIGLSCLVALFLYhVVFGIQyLGILNGVAAFVIVGIGVD-DVFVfintyRQAT 500
Cdd:COG4258  645 LLLALLLILLLLLLRLRSLrralrvlLPPLLAVLLTLAIL-GLLGIP-LNLFHLIALLLVLGIGIDyALFF-----TEGL 717
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755509632 501 HLEDPQLRMIHTIqtagkatFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVTCCWL 558
Cdd:COG4258  718 LDKGELARTLLSI-------LLAALTTLLGFGLLAFSSTPALRSFGLTVLLGILLALL 768
actII TIGR00833
Transport protein; The Resistance-Nodulation-Cell Division (RND) Superfamily- MmpL sub family ...
414-572 1.33e-03

Transport protein; The Resistance-Nodulation-Cell Division (RND) Superfamily- MmpL sub family (TC 2.A.6.5)Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. This sub-family includes the S. coelicolor ActII3 protein, which may play a role in drug resistance, and the M. tuberculosis MmpL7 protein, which catalyzes export of an outer membrane lipid, phthiocerol dimycocerosate. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 129913 [Multi-domain]  Cd Length: 910  Bit Score: 42.26  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  414 FNNDMLLAFISSSCIAALVYILTSCSVFLSFFGIASIGLSCLVALflyHVVFGIQYLGILnGVAAF-------VIVGIGV 486
Cdd:TIGR00833 171 GDKDMNRITATTGIIVLIILLLVYRSPITMLVPLVSVGFSVVVAQ---GIVSLLGIPGLI-GVNAQttvlltaLVIGAGT 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  487 DDVFVFINTYRQAT-HLEDPQLRMIHTIQTAGKATFFTSLTTAAAYAANVFSQIPAVHDFGLFMSLIVTCCWLAVLFTMP 565
Cdd:TIGR00833 247 DYAVFLTGRYHEERrKGESLEEAAAEALRGTGKAILGSALTVAVAFLALSLARLPSFKTLGVSCAVGVLVALLNAVTLTP 326

                  ....*..
gi 755509632  566 AALGLWS 572
Cdd:TIGR00833 327 ALLTLEG 333
HpnN TIGR03480
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
392-571 1.41e-03

hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins appear to be related to the RND family of export proteins, particularly the hydrophobe/amphiphile efflux-3 (HAE3) family represented by TIGR00921.


Pssm-ID: 274598 [Multi-domain]  Cd Length: 862  Bit Score: 42.29  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  392 STSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAALVYILTscsvFLSFFGIASIgLSCLVALFLYHVVFGIQYLG 471
Cdd:TIGR03480 245 EDHGVTVRLTGEVALSDEELATVSEGATVAGLLSFVLVLVLLWLA----LRSPRLVFAV-LVTLIVGLILTAAFATLAVG 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755509632  472 ILNGVA-AFVI--VGIGVDDVFVFINTYRQATHLEDPQLRMIH-TIQTAGKATFFTSLTTAAAYAANVF------SQIPA 541
Cdd:TIGR03480 320 HLNLISvAFAVlfIGLGVDFAIQFSLRYREERFRGGNHREALSvAARRMGAALLLAALATAAGFFAFLPtdykgvSELGI 399
                         170       180       190
                  ....*....|....*....|....*....|
gi 755509632  542 VHDFGLFMSLIVTccwLAVLftmPAALGLW 571
Cdd:TIGR03480 400 IAGTGMFIALFVT---LTVL---PALLRLL 423
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH