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Conserved domains on  [gi|2024457330|ref|XP_040539121|]
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inactive rhomboid protein 1 isoform X1 [Gallus gallus]

Protein Classification

inactive rhomboid protein( domain architecture ID 10576411)

inactive rhomboid protein regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation; does not exhibit any protease activity on its own

CATH:  1.20.1540.10
MEROPS:  S54
SCOP:  4000471

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rhomboid_SP pfam12595
Rhomboid serine protease; This domain family is found in eukaryotes, and is approximately 210 ...
125-318 4.66e-129

Rhomboid serine protease; This domain family is found in eukaryotes, and is approximately 210 amino acids in length. The family is found in association with pfam01694. Rhomboid is a seven-transmembrane spanning protein that resides in the Golgi and acts as a serine protease to cleave Spitz.


:

Pssm-ID: 463639  Cd Length: 193  Bit Score: 385.38  E-value: 4.66e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 125 VSKDSDATQKWQRKSLRHCSLRYGKLKPQVIREMDLPSQDNISLTSTETPPPLYVGPCQLGMQKIIDPLARGRAFRMADD 204
Cdd:pfam12595   1 VSKDSDSTQRWQRKSLRHCSMRYGKLKPQVIREMELPSQDNPSLTSTETPPPLYLPKSHHGMQRIVDPLARGRAFRMVEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 205 NDGYSIPHTPITPGATSLCSFTSSRSGFNRLPRRRKRESVAKMSFRAAAALVKGRSVKDSTLRRAQRRSFTPASFMEEDT 284
Cdd:pfam12595  81 VDGYSVPQTPITPGVASLCSFTSSRSGLNRLPRRRKRESVAKMSFRAAAALMKGRSLRESTLRRRRRRSFTPPSFLEEDT 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2024457330 285 VDFPDELDTSFFAREGvLHEELSTYPDEVFESPS 318
Cdd:pfam12595 161 VDFADELDTSFFSKDD-LHEELSSMADEVFESPS 193
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
680-823 4.17e-36

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


:

Pssm-ID: 426384  Cd Length: 147  Bit Score: 133.50  E-value: 4.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 680 PEVPDQFYRLWLSLFLHAGILHCLVSVCFQMTILRDLEKLAGWHRISIIYLLSGITGNLASAIFLPY-RAEVGPAGSQFG 758
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLsTPSVGASGAIFG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024457330 759 ILACLFVELFQSWQILARPWRAFFKLLAVVLFLFAFGLLPW--IDNFAHISGFISGFFLSFAFLPYI 823
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLLPGngVSNLAHLGGLLVGLLLGFILLRRP 147
 
Name Accession Description Interval E-value
Rhomboid_SP pfam12595
Rhomboid serine protease; This domain family is found in eukaryotes, and is approximately 210 ...
125-318 4.66e-129

Rhomboid serine protease; This domain family is found in eukaryotes, and is approximately 210 amino acids in length. The family is found in association with pfam01694. Rhomboid is a seven-transmembrane spanning protein that resides in the Golgi and acts as a serine protease to cleave Spitz.


Pssm-ID: 463639  Cd Length: 193  Bit Score: 385.38  E-value: 4.66e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 125 VSKDSDATQKWQRKSLRHCSLRYGKLKPQVIREMDLPSQDNISLTSTETPPPLYVGPCQLGMQKIIDPLARGRAFRMADD 204
Cdd:pfam12595   1 VSKDSDSTQRWQRKSLRHCSMRYGKLKPQVIREMELPSQDNPSLTSTETPPPLYLPKSHHGMQRIVDPLARGRAFRMVEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 205 NDGYSIPHTPITPGATSLCSFTSSRSGFNRLPRRRKRESVAKMSFRAAAALVKGRSVKDSTLRRAQRRSFTPASFMEEDT 284
Cdd:pfam12595  81 VDGYSVPQTPITPGVASLCSFTSSRSGLNRLPRRRKRESVAKMSFRAAAALMKGRSLRESTLRRRRRRSFTPPSFLEEDT 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2024457330 285 VDFPDELDTSFFAREGvLHEELSTYPDEVFESPS 318
Cdd:pfam12595 161 VDFADELDTSFFSKDD-LHEELSSMADEVFESPS 193
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
680-823 4.17e-36

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 133.50  E-value: 4.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 680 PEVPDQFYRLWLSLFLHAGILHCLVSVCFQMTILRDLEKLAGWHRISIIYLLSGITGNLASAIFLPY-RAEVGPAGSQFG 758
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLsTPSVGASGAIFG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024457330 759 ILACLFVELFQSWQILARPWRAFFKLLAVVLFLFAFGLLPW--IDNFAHISGFISGFFLSFAFLPYI 823
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLLPGngVSNLAHLGGLLVGLLLGFILLRRP 147
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
685-821 1.03e-21

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 93.39  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 685 QFYRLWLSLFLHAGILHCLvsvcFQMTIL----RDLEKLAGWHRISIIYLLSGITGNLASAIFLPYRAE--VGPAGSQFG 758
Cdd:COG0705    42 ELWRLLTSMFLHGGFLHLL----FNMLALwvfgPLLERRLGSKRFLLLYLLSGLGGGLLQLLFSPGSGYplVGASGAIFG 117
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024457330 759 ILACLFV-ELFQSWQILARPWRAFFKLLAVVLFLFAFGLLPW--IDNFAHISGFISGFFLSFAFLP 821
Cdd:COG0705   118 LLGALLVlGPRRRVLLLFIPIPALLFLLVWLLLGLLFGLLGGggIAWEAHLGGLLAGLLLALLLRK 183
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
685-813 2.30e-14

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 74.50  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 685 QFYRLWLSLFLHAGILHCLVSVCFQMTILRDLEKLAGWHRISIIYLLSGITGNL--ASAIFLPYRaeVGPAGSQFGILAC 762
Cdd:PTZ00101  101 EIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVKIIILYFLTGIYGNIlsSSVTYCPIK--VGASTSGMGLLGI 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024457330 763 LFVELFQSWQILARPWRAFFKLLAVVL--FLFAFGLL-PWIDNFAHISGFISGF 813
Cdd:PTZ00101  179 VTSELILLWHVIRHRERVVFNIIFFSLisFFYYFTFNgSNIDHVGHLGGLLSGI 232
MFS cd06174
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
725-860 5.36e-03

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: 40.10  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 725 ISIIYLLSGITGNLASAIFLPYRAEVGPAGSQFGIL--ACLFVELFqsWQILARPW------RAFFKLLAVVLFLFAFgL 796
Cdd:cd06174     1 LLLGFFLTGLARGLISPLLPALLQSFGLSASQLGLLfaLFSLGYAL--LQPLAGLLadrfgrRPVLLLGLLLFALGAL-L 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024457330 797 LPWIDNFAH--ISGFISGFFLSFAFLPYISFGkFDLYRKRCQIIVFQLIFIALFSGLVILFYFYPI 860
Cdd:cd06174    78 FAFAPSFWLllLGRFLLGLGSGLIDPAVLALI-ADLFPERERGRALGLLQAFGSVGGILGPLLGGI 142
 
Name Accession Description Interval E-value
Rhomboid_SP pfam12595
Rhomboid serine protease; This domain family is found in eukaryotes, and is approximately 210 ...
125-318 4.66e-129

Rhomboid serine protease; This domain family is found in eukaryotes, and is approximately 210 amino acids in length. The family is found in association with pfam01694. Rhomboid is a seven-transmembrane spanning protein that resides in the Golgi and acts as a serine protease to cleave Spitz.


Pssm-ID: 463639  Cd Length: 193  Bit Score: 385.38  E-value: 4.66e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 125 VSKDSDATQKWQRKSLRHCSLRYGKLKPQVIREMDLPSQDNISLTSTETPPPLYVGPCQLGMQKIIDPLARGRAFRMADD 204
Cdd:pfam12595   1 VSKDSDSTQRWQRKSLRHCSMRYGKLKPQVIREMELPSQDNPSLTSTETPPPLYLPKSHHGMQRIVDPLARGRAFRMVEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 205 NDGYSIPHTPITPGATSLCSFTSSRSGFNRLPRRRKRESVAKMSFRAAAALVKGRSVKDSTLRRAQRRSFTPASFMEEDT 284
Cdd:pfam12595  81 VDGYSVPQTPITPGVASLCSFTSSRSGLNRLPRRRKRESVAKMSFRAAAALMKGRSLRESTLRRRRRRSFTPPSFLEEDT 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2024457330 285 VDFPDELDTSFFAREGvLHEELSTYPDEVFESPS 318
Cdd:pfam12595 161 VDFADELDTSFFSKDD-LHEELSSMADEVFESPS 193
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
680-823 4.17e-36

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 133.50  E-value: 4.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 680 PEVPDQFYRLWLSLFLHAGILHCLVSVCFQMTILRDLEKLAGWHRISIIYLLSGITGNLASAIFLPY-RAEVGPAGSQFG 758
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLsTPSVGASGAIFG 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024457330 759 ILACLFVELFQSWQILARPWRAFFKLLAVVLFLFAFGLLPW--IDNFAHISGFISGFFLSFAFLPYI 823
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLLPGngVSNLAHLGGLLVGLLLGFILLRRP 147
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
685-821 1.03e-21

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 93.39  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 685 QFYRLWLSLFLHAGILHCLvsvcFQMTIL----RDLEKLAGWHRISIIYLLSGITGNLASAIFLPYRAE--VGPAGSQFG 758
Cdd:COG0705    42 ELWRLLTSMFLHGGFLHLL----FNMLALwvfgPLLERRLGSKRFLLLYLLSGLGGGLLQLLFSPGSGYplVGASGAIFG 117
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024457330 759 ILACLFV-ELFQSWQILARPWRAFFKLLAVVLFLFAFGLLPW--IDNFAHISGFISGFFLSFAFLP 821
Cdd:COG0705   118 LLGALLVlGPRRRVLLLFIPIPALLFLLVWLLLGLLFGLLGGggIAWEAHLGGLLAGLLLALLLRK 183
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
685-813 2.30e-14

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 74.50  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 685 QFYRLWLSLFLHAGILHCLVSVCFQMTILRDLEKLAGWHRISIIYLLSGITGNL--ASAIFLPYRaeVGPAGSQFGILAC 762
Cdd:PTZ00101  101 EIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVKIIILYFLTGIYGNIlsSSVTYCPIK--VGASTSGMGLLGI 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024457330 763 LFVELFQSWQILARPWRAFFKLLAVVL--FLFAFGLL-PWIDNFAHISGFISGF 813
Cdd:PTZ00101  179 VTSELILLWHVIRHRERVVFNIIFFSLisFFYYFTFNgSNIDHVGHLGGLLSGI 232
7TMR-DISM_7TM pfam07695
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ...
674-818 4.77e-04

7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).


Pssm-ID: 429600 [Multi-domain]  Cd Length: 207  Bit Score: 42.26  E-value: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 674 LLPFLNPEVPDQF--YRLWLSLFLHAGILHCLvsvcFQMTILrDLEKLAGWHRISIIYLLSGITGNLASAIFLPYRAEVg 751
Cdd:pfam07695  52 GFQYLWPNAPPWLnnKLLYLSLLLLLPFFALL----FARSFL-ELKKYLPRLLRLLLGLALLLALLLLLLPLFPYTLSL- 125
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024457330 752 PAGSQFGILACLFVELFQSWQILARPWRAFFKLLAVVLFLFA--------FGLLP---WIDNFAHISGFISGFFLSFA 818
Cdd:pfam07695 126 PLAQLLALLFILFLLLLGIIAWRKGYKPARYFLLAWLLLLIGalidilslLGLLPsnfFTNYLLQIGSALEVLLLSLA 203
MFS cd06174
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
725-860 5.36e-03

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: 40.10  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 725 ISIIYLLSGITGNLASAIFLPYRAEVGPAGSQFGIL--ACLFVELFqsWQILARPW------RAFFKLLAVVLFLFAFgL 796
Cdd:cd06174     1 LLLGFFLTGLARGLISPLLPALLQSFGLSASQLGLLfaLFSLGYAL--LQPLAGLLadrfgrRPVLLLGLLLFALGAL-L 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024457330 797 LPWIDNFAH--ISGFISGFFLSFAFLPYISFGkFDLYRKRCQIIVFQLIFIALFSGLVILFYFYPI 860
Cdd:cd06174    78 FAFAPSFWLllLGRFLLGLGSGLIDPAVLALI-ADLFPERERGRALGLLQAFGSVGGILGPLLGGI 142
MFS_MdtG_SLC18_like cd17325
bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator ...
719-855 6.38e-03

bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily of transporters; This family is composed of eukaryotic solute carrier 18 (SLC18) family transporters and related bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as multidrug resistance protein MdtG, from Bacillus subtilis such as multidrug resistance proteins 1 (Bmr1) and 2 (Bmr2), and from Staphylococcus aureus such as quinolone resistance protein NorA. The family also includes Escherichia coli arabinose efflux transporters YfcJ and YhhS. 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. The SLC18 transporter family includes vesicular monoamine transporters (VAT1 and VAT2), vesicular acetylcholine transporter (VAChT), and SLC18B1, which is proposed to be a vesicular polyamine transporter (VPAT). The MdtG/SLC18 family belongs 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: 340883 [Multi-domain]  Cd Length: 375  Bit Score: 39.87  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 719 LAGWHRISIIYLLSGITGNLASAI---FLPYRAEVGPAGSQfgilacLFVELFQSWQILARPWRAFFKLLAVVLFLFAFG 795
Cdd:cd17325   143 LADALGYRAPFLVCAALALLALVLallLLPEPRPPPNKRAV------SAARLRSGLRLLLRDRRLLALFLAIFVLAFAFG 216
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 796 ----LLP-WIDNFAHISGFISGFFLSFAFLPY----ISFGKF-DLYRKRcQIIVFQLIFIALFSGLVILF 855
Cdd:cd17325   217 alepFLPlYAAELGGLSPAQIGLLFGAQGLASalsqPPAGKLsDRIGRK-PLILIGLLLSAVALLLLPLA 285
LNT_N pfam20154
Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal ...
736-874 6.90e-03

Apolipoprotein N-acyltransferase N-terminal domain; This domain represents the N-terminal transmembrane region of the apolipoprotein N-acyltransferase enzyme. The enzyme catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. This entry does not represent the enzymatic domain found at the C-terminus of the protein.


Pssm-ID: 466311 [Multi-domain]  Cd Length: 159  Bit Score: 38.38  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 736 GNLASAIFLPYraEVGPAGsqFGILACLFVELFQSwqilaRPWRAFFKLLAVVLFLFAFGLLPWIDNFAHISG---FISG 812
Cdd:pfam20154   1 GLLLSLAFPPF--GLWPLA--WVALAPLLLALEAR-----SSPRRAFLLGFLFGLGFFGLGLYWLGVSLHTFGgapLPLA 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024457330 813 FFLSFAFLPYIS-FGKFDLYRKRCQIIVFQLIFIALFSGLvilfyfypikcewcEFLTCIPFT 874
Cdd:pfam20154  72 LLLLLLLALYLAlFALAAWLLKRLWGLFRALLFAALWVGL--------------EYLRGWPFG 120
COG4984 COG4984
Uncharacterized membrane protein [Function unknown];
720-857 7.12e-03

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 444008  Cd Length: 319  Bit Score: 39.41  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 720 AGWHRISIIYLLSGITgnLASAIFLPYRAEVGPAGSQFGILACLFV------------------ELFQSWQILARPW--- 778
Cdd:COG4984    62 ASLHRFAKFALLQALL--VASALAAWRLGLERLAGQAALLLAAVLVgallalfgqtyqtgadpwQLFALWALLILPWvll 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024457330 779 -RAFFKLLAVVLFLFAFGLLPWIDNFAHISGFISGFFL------SFAFLPYISFGKFDLYRKRCQIIVFQLIFIALFSGL 851
Cdd:COG4984   140 aAFLGLLLLYLLLLNLLLILYFLQVRSDFELNWLTLVLallaalLLALLLVLALDKLSLLSAAYLGILLLLARLILVLAI 219

                  ....*.
gi 2024457330 852 VILFYF 857
Cdd:COG4984   220 AALAAF 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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