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Conserved domains on  [gi|19921100|ref|NP_609417|]
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uncharacterized protein Dmel_CG7384 [Drosophila melanogaster]

Protein Classification

DUF389 domain-containing protein( domain architecture ID 10513626)

DUF389 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF389 pfam04087
Domain of unknown function (DUF389); Family of hypothetical bacterial proteins with an ...
 245-419 3.74e-39

Domain of unknown function (DUF389); Family of hypothetical bacterial proteins with an undetermined function.


:

Pssm-ID: 461166  Cd Length: 137  Bit Score: 140.26  E-value: 3.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   245 MLISPLMGPIIAAIFGTVIQDRSLRRLGMLNELIGILTATLVGFLFGLVVcttdrkyGIGEGLTEEMLSRCDLHslVVGV 324
Cdd:pfam04087   1 MLIAPLMGPILALAFGLVLGDRRLLKRSLRALLIGLLLAILVAALFGLLL-------PLGEATTSEILARTSPN--LLDL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   325 FTAIPSGAAAAIGILGGNIGSLVGVAISASLLPPAVNSGLLWAVAciykifenddslyvdviksrRYSdnqatelavLGG 404
Cdd:pfam04087  72 LVALAAGAAGALALTRGKSSSLVGVAIAVALVPPLATAGLGLAWG--------------------NWA---------LAL 122

                         170
                  ....*....|....*
gi 19921100   405 ISMCLTLSNVLCVYL 419
Cdd:pfam04087 123 GALLLFLVNLVGINL 137
 
Name Accession Description Interval E-value
DUF389 pfam04087
Domain of unknown function (DUF389); Family of hypothetical bacterial proteins with an ...
 245-419 3.74e-39

Domain of unknown function (DUF389); Family of hypothetical bacterial proteins with an undetermined function.


Pssm-ID: 461166  Cd Length: 137  Bit Score: 140.26  E-value: 3.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   245 MLISPLMGPIIAAIFGTVIQDRSLRRLGMLNELIGILTATLVGFLFGLVVcttdrkyGIGEGLTEEMLSRCDLHslVVGV 324
Cdd:pfam04087   1 MLIAPLMGPILALAFGLVLGDRRLLKRSLRALLIGLLLAILVAALFGLLL-------PLGEATTSEILARTSPN--LLDL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   325 FTAIPSGAAAAIGILGGNIGSLVGVAISASLLPPAVNSGLLWAVAciykifenddslyvdviksrRYSdnqatelavLGG 404
Cdd:pfam04087  72 LVALAAGAAGALALTRGKSSSLVGVAIAVALVPPLATAGLGLAWG--------------------NWA---------LAL 122

                         170
                  ....*....|....*
gi 19921100   405 ISMCLTLSNVLCVYL 419
Cdd:pfam04087 123 GALLLFLVNLVGINL 137
AF0785 COG1808
Uncharacterized membrane protein AF0785, contains DUF389 domain [Function unknown];
197-432 1.21e-37

Uncharacterized membrane protein AF0785, contains DUF389 domain [Function unknown];


Pssm-ID: 441413  Cd Length: 211  Bit Score: 138.79  E-value: 1.21e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 197 SRLNVAQIVRDVRQDAAITFDFCILLVSAAVLASFGLVENSTIFLASSMLISPLMGPIIAAIFGTVIQDRSLRRLGMLNE 276
Cdd:COG1808   5 DRISREELYERAEEESRLSGTYLVLLVLSTIIATIGLLLNSPAVIIGAMVIAPLMGPILALALGLVLGDRELLRRSLKTL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 277 LIGILTATLVGFLFGLVVCTTDrkygigegLTEEMLSRC--DLHSLVVGVFtaipSGAAAAIGILGGNIGSLVGVAISAS 354
Cdd:COG1808  85 LVGLLLAIAVAALLALLLPLTE--------ATSEILARTspTLLDLLVALA----AGAAGALALTRGKSSALVGVAIAVA 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921100 355 LLPPAVNSGLLWAVAciykifenddslyvdviksrrysdnqatELAVLGGiSMCLTLSNVLCVYLMGILVLKVKEIAP 432
Cdd:COG1808 153 LVPPLATAGIGLAWG----------------------------NWDLALG-ALLLFLVNLVGINLAALLVFLLLGYRP 201
TIGR00271 TIGR00271
uncharacterized hydrophobic domain; This domain is in a family of archaeal proteins that ...
 212-375 3.44e-19

uncharacterized hydrophobic domain; This domain is in a family of archaeal proteins that includes AF0785 of Archaeoglobus fulgidus and in several eubacterial proteins, including the much longer protein sll1151 from Synechocystis PCC6803.


Pssm-ID: 129372  Cd Length: 175  Bit Score: 85.13  E-value: 3.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   212 AAITFDFCILLVSAAVLASFGLVENSTIFLASSMLISPLMGPIIAAIFGTVIQDRSLRRLGMLNELIGILTATLVGFLFG 291
Cdd:TIGR00271   1 STLSKTYIIFVILATIIAACGLVLDNAVLIIGAMIIAPLLGPIAGSAVGLVVGDVKLALRSAKNLLLAMAFVIVFAMIMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   292 LVVcttdrkygIGEGLTEEMLSRC--DLHSLVVGVFtaipSGAAAAIGILGGNIGSLVGVAISASLLPPAVNSGLLWAVA 369
Cdd:TIGR00271  81 LFH--------PSKLTVPQILSRTspDFLSLIVAVL----AGIAGSLSLTSGKSGSLVGVAISVSLLPPAAVAGVALGIG 148


                  ....*.
gi 19921100   370 CIYKIF 375
Cdd:TIGR00271 149 DLLQSY 154
MFS cd06174
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
 212-371 5.86e-05

Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.


Pssm-ID: 349949 [Multi-domain]  Cd Length: 378  Bit Score: 45.50  E-value: 5.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 212 AAITFDFCILLVSAaVLASFGLVENSTIFLASSMLISPLMGPIIAAIFGTVIQDRSLRRLGMlneLIGILTATLVGFLFG 291
Cdd:cd06174   4 GFFLTGLARGLISP-LLPALLQSFGLSASQLGLLFALFSLGYALLQPLAGLLADRFGRRPVL---LLGLLLFALGALLFA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 292 L-----VVCTTDRKYGIGEGLTeeMLSrcdLHSLVVGVFTAIPSGAAAAIGILGGNIGSLVGVAISASLLPPAVNS--GL 364
Cdd:cd06174  80 FapsfwLLLLGRFLLGLGSGLI--DPA---VLALIADLFPERERGRALGLLQAFGSVGGILGPLLGGILASSLGFGwrAV 154


                ....*..
gi 19921100 365 LWAVACI 371
Cdd:cd06174 155 FLIAAAL 161
 
Name Accession Description Interval E-value
DUF389 pfam04087
Domain of unknown function (DUF389); Family of hypothetical bacterial proteins with an ...
 245-419 3.74e-39

Domain of unknown function (DUF389); Family of hypothetical bacterial proteins with an undetermined function.


Pssm-ID: 461166  Cd Length: 137  Bit Score: 140.26  E-value: 3.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   245 MLISPLMGPIIAAIFGTVIQDRSLRRLGMLNELIGILTATLVGFLFGLVVcttdrkyGIGEGLTEEMLSRCDLHslVVGV 324
Cdd:pfam04087   1 MLIAPLMGPILALAFGLVLGDRRLLKRSLRALLIGLLLAILVAALFGLLL-------PLGEATTSEILARTSPN--LLDL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   325 FTAIPSGAAAAIGILGGNIGSLVGVAISASLLPPAVNSGLLWAVAciykifenddslyvdviksrRYSdnqatelavLGG 404
Cdd:pfam04087  72 LVALAAGAAGALALTRGKSSSLVGVAIAVALVPPLATAGLGLAWG--------------------NWA---------LAL 122

                         170
                  ....*....|....*
gi 19921100   405 ISMCLTLSNVLCVYL 419
Cdd:pfam04087 123 GALLLFLVNLVGINL 137
AF0785 COG1808
Uncharacterized membrane protein AF0785, contains DUF389 domain [Function unknown];
197-432 1.21e-37

Uncharacterized membrane protein AF0785, contains DUF389 domain [Function unknown];


Pssm-ID: 441413  Cd Length: 211  Bit Score: 138.79  E-value: 1.21e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 197 SRLNVAQIVRDVRQDAAITFDFCILLVSAAVLASFGLVENSTIFLASSMLISPLMGPIIAAIFGTVIQDRSLRRLGMLNE 276
Cdd:COG1808   5 DRISREELYERAEEESRLSGTYLVLLVLSTIIATIGLLLNSPAVIIGAMVIAPLMGPILALALGLVLGDRELLRRSLKTL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 277 LIGILTATLVGFLFGLVVCTTDrkygigegLTEEMLSRC--DLHSLVVGVFtaipSGAAAAIGILGGNIGSLVGVAISAS 354
Cdd:COG1808  85 LVGLLLAIAVAALLALLLPLTE--------ATSEILARTspTLLDLLVALA----AGAAGALALTRGKSSALVGVAIAVA 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921100 355 LLPPAVNSGLLWAVAciykifenddslyvdviksrrysdnqatELAVLGGiSMCLTLSNVLCVYLMGILVLKVKEIAP 432
Cdd:COG1808 153 LVPPLATAGIGLAWG----------------------------NWDLALG-ALLLFLVNLVGINLAALLVFLLLGYRP 201
TIGR00271 TIGR00271
uncharacterized hydrophobic domain; This domain is in a family of archaeal proteins that ...
 212-375 3.44e-19

uncharacterized hydrophobic domain; This domain is in a family of archaeal proteins that includes AF0785 of Archaeoglobus fulgidus and in several eubacterial proteins, including the much longer protein sll1151 from Synechocystis PCC6803.


Pssm-ID: 129372  Cd Length: 175  Bit Score: 85.13  E-value: 3.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   212 AAITFDFCILLVSAAVLASFGLVENSTIFLASSMLISPLMGPIIAAIFGTVIQDRSLRRLGMLNELIGILTATLVGFLFG 291
Cdd:TIGR00271   1 STLSKTYIIFVILATIIAACGLVLDNAVLIIGAMIIAPLLGPIAGSAVGLVVGDVKLALRSAKNLLLAMAFVIVFAMIMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   292 LVVcttdrkygIGEGLTEEMLSRC--DLHSLVVGVFtaipSGAAAAIGILGGNIGSLVGVAISASLLPPAVNSGLLWAVA 369
Cdd:TIGR00271  81 LFH--------PSKLTVPQILSRTspDFLSLIVAVL----AGIAGSLSLTSGKSGSLVGVAISVSLLPPAAVAGVALGIG 148


                  ....*.
gi 19921100   370 CIYKIF 375
Cdd:TIGR00271 149 DLLQSY 154
TIGR00341 TIGR00341
TIGR00341 family protein; This conserved hypothetical protein is found so far only in three ...
 197-375 6.89e-17

TIGR00341 family protein; This conserved hypothetical protein is found so far only in three archaeal genomes and in Streptomyces coelicolor. It shares a hydrophobic uncharacterized domain (see TIGR00271) of about 180 residues with several eubacterial proteins, including the much longer protein sll1151 of Synechocystis PCC6803. [Hypothetical proteins, Conserved]


Pssm-ID: 273024  Cd Length: 325  Bit Score: 82.24  E-value: 6.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   197 SRLNVAQIVRDVRQDAAITFDFCILLVSAAVLASFGLVENSTIFLASSMLISPLMGPIIAAIFGTVIQDRSLRRLGMLNE 276
Cdd:TIGR00341  95 TSLPVEELYEMAKSYASLNKGRSVVTILAGIIALSGLIMNNAVILIGAMIIAPLLGPIHGFAVNLSVGDVKLAFRSAKNL 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   277 LIGILTATLVGFLFGLVVcttdrkyGIGEgLTEEMLSRCDLHslVVGVFTAIPSGAAAAIGILGGNIGSLVGVAISASLL 356
Cdd:TIGR00341 175 LFDLFLVIVFSTIFAMMI-------GLVQ-LTPQILSRTEVS--PVSEILAVLAGIAGILSLSSGILESLAGVAISASLL 244

                         170
                  ....*....|....*....
gi 19921100   357 PPAVNSGLLWAVACIYKIF 375
Cdd:TIGR00341 245 PPAVATGILLVISPLPLAV 263
MFS cd06174
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
 212-371 5.86e-05

Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.


Pssm-ID: 349949 [Multi-domain]  Cd Length: 378  Bit Score: 45.50  E-value: 5.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 212 AAITFDFCILLVSAaVLASFGLVENSTIFLASSMLISPLMGPIIAAIFGTVIQDRSLRRLGMlneLIGILTATLVGFLFG 291
Cdd:cd06174   4 GFFLTGLARGLISP-LLPALLQSFGLSASQLGLLFALFSLGYALLQPLAGLLADRFGRRPVL---LLGLLLFALGALLFA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 292 L-----VVCTTDRKYGIGEGLTeeMLSrcdLHSLVVGVFTAIPSGAAAAIGILGGNIGSLVGVAISASLLPPAVNS--GL 364
Cdd:cd06174  80 FapsfwLLLLGRFLLGLGSGLI--DPA---VLALIADLFPERERGRALGLLQAFGSVGGILGPLLGGILASSLGFGwrAV 154


                ....*..
gi 19921100 365 LWAVACI 371
Cdd:cd06174 155 FLIAAAL 161
Nramp pfam01566
Natural resistance-associated macrophage protein; The natural resistance-associated macrophage ...
 218-360 3.65e-04

Natural resistance-associated macrophage protein; The natural resistance-associated macrophage protein (NRAMP) family consists of Nramp1, Nramp2, and yeast proteins Smf1 and Smf2. The NRAMP family is a novel family of functional related proteins defined by a conserved hydrophobic core of ten transmembrane domains. This family of membrane proteins are divalent cation transporters. Nramp1 is an integral membrane protein expressed exclusively in cells of the immune system and is recruited to the membrane of a phagosome upon phagocytosis. By controlling divalent cation concentrations Nramp1 may regulate the interphagosomal replication of bacteria. Mutations in Nramp1 may genetically predispose an individual to susceptibility to diseases including leprosy and tuberculosis conversely this might however provide protection form rheumatoid arthritis. Nramp2 is a multiple divalent cation transporter for Fe2+, Mn2+ and Zn2+ amongst others it is expressed at high levels in the intestine; and is major transferrin-independent iron uptake system in mammals. The yeast proteins Smf1 and Smf2 may also transport divalent cations.


Pssm-ID: 426327 [Multi-domain]  Cd Length: 356  Bit Score: 42.94  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   218 FCILLVSAAVLASFGLVENSTIFLASSMLiSPLMGPIIAAIFGtviqdrslrrlgmlnelIGILTATlvgfLFGLVVCTT 297
Cdd:pfam01566 217 AAILIVAAAAFHGSGGIDVATLADAAAAL-EPLLGKAAAVLFA-----------------LGLLAAG----LSSTITGTL 274

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921100   298 DRKYGIGEGLTEEMlsRCDLHSLVVGVFTAIPSGAAAAIGILGGNIGSLVGVAISASL-LPPAV 360
Cdd:pfam01566 275 AGQYVMEGFLGWRI--PLWLRRLITRAIAFYPALAVILLGGAPGVVQLLVLSQVVLSLqLPFAL 336
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 223-365 1.28e-03

Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.


Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 41.38  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   223 VSAAVLASFGLVENSTIFLASSMLISP---LMGPIIAAIFG------TVIQDRSLRRLGMLNELIGILTATLVGFLFGLV 293
Cdd:pfam00654 133 VVAALVSRLIFGNSPLFSVGEPGSLSLlelPLFILLGILCGllgalfNRLLLKVQRLFRKLLKIPPVLRPALGGLLVGLL 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100   294 VCTTDRKYGIGEGLTEEMLSRCDLHSLVVG------VFTAIPSGAAAAIGI------LGGNIGSLVGVAISASLLPPAVN 361
Cdd:pfam00654 213 GLLFPEVLGGGYELIQLLFNGNTSLSLLLLllllkfLATALSLGSGAPGGIfapslaIGAALGRAFGLLLALLFPIGGLP 292


                  ....
gi 19921100   362 SGLL 365
Cdd:pfam00654 293 PGAF 296
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 220-368 8.39e-03

ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, are putative halogen ion (Cl-, Br- and I-) transport proteins found in eubacteria. They belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. This superfamily lacks any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge.


Pssm-ID: 238506 [Multi-domain]  Cd Length: 390  Bit Score: 38.75  E-value: 8.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 220 ILLVSAAVLASFGLVENSTIF--------LASSMLISPLMGPI---IAAIFGTVIQDRSLRRLGMLNELIG---ILTATL 285
Cdd:cd01034 169 LLAVIAAGLVSLAVLGNYPYFgvaavalpLGEAWLLVLVCGVVgglAGGLFARLLVALSSGLPGWVRRFRRrrpVLFAAL 248

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 286 VGFLF---GLVvcTTDRKYGIGEGLTEEMLSRCDLHSLVVGVFTAIPSGAAAAIGILGG------NIGSLVGVAISAslL 356
Cdd:cd01034 249 CGLALaliGLV--SGGLTFGTGYLQARAALEGGGGLPLWFGLLKFLATLLSYWSGIPGGlfapslAVGAGLGSLLAA--L 324

                       170
                ....*....|..
gi 19921100 357 PPAVNSGLLWAV 368
Cdd:cd01034 325 LGSVSQGALVLL 336
MFS_MMR_MDR_like cd17321
Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance ...
 226-356 9.54e-03

Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily; This family is composed of bacterial, fungal, and archaeal multidrug resistance (MDR) transporters including several proteins from Bacilli such as methylenomycin A resistance protein (also called MMR peptide), tetracycline resistance protein (TetB), and lincomycin resistance protein LmrB, as well as fungal proteins such as vacuolar basic amino acid transporters, which are involved in the transport into vacuoles of the basic amino acids histidine, lysine, and arginine in Saccharomyces cerevisiae, and aminotriazole/azole resistance proteins. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. For example, MMR confers resistance to the epoxide antibiotic methylenomycin while TetB resistance to tetracycline by an active tetracycline efflux. MMR-like MDR transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340879 [Multi-domain]  Cd Length: 370  Bit Score: 38.69  E-value: 9.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921100 226 AVLASFGLVENSTIFLASSMLISPL---MGPIIAAIFGTVIQdrslrRLGMLNELIGILTATLVGFLFGLVVCttdrkyG 302
Cdd:cd17321 203 PLQAGLALLPLALAMLVAAPLAGRLadrFGPRLVLVAGLLLT-----AVGLLLLALLGADSSVWLLLPGLVLL------G 271

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19921100 303 IGEGLTEEMLSrcdlhSLVVGVFTAIPSGAAAAIGILGGNIGSLVGVAISASLL 356
Cdd:cd17321 272 LGLGLFATPLT-----NAALSSVPKEKAGAASGILNTARQLGGALGVALLGALL 320
 
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.
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