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Conserved domains on  [gi|1786622127|gb|QGZ14903|]
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plastidic ATP/ADP-transporter-like protein, partial [Lens orientalis]

Protein Classification

MFS transporter( domain architecture ID 999995)

major facilitator superfamily (MFS) transporter facilitates the transport across cytoplasmic or internal membranes of one or more from a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides

CATH:  1.20.1250.20
Gene Ontology:  GO:0022857|GO:0055085
PubMed:  26758938|26098515
SCOP:  3000310
TCDB:  2.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MFS super family cl28910
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
 1-110 1.63e-58

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.


The actual alignment was detected with superfamily member TIGR00769:

Pssm-ID: 475125  Cd Length: 472  Bit Score: 186.50  E-value: 1.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786622127   1 MLLSQYIFDKYGWGVAAKITPTVLLLTGVGFFSLILFGGPIAPGLASLGMTPLLAAVYVGALQNIFSKSAKYSLFDPCKE 80
Cdd:TIGR00769 320 MLLSGNVIRKYGWLTAALITPLVMLLTGVAFFSLIFFGGPAAPLVAKLGMTPLLLAVYVGAIQNILSKSTKYSLFDATKE 399

                          90       100       110
                  ....*....|....*....|....*....|
gi 1786622127  81 MAYIPLDEDTKVKGKAAIDVVCNPLGKSGG 110
Cdd:TIGR00769 400 MAYIPLDEEQKVKGKAAIDVVAARLGKSGG 429
 
Name Accession Description Interval E-value
AAA TIGR00769
ADP/ATP carrier protein family; These proteins are members of the ATP:ADP Antiporter (AAA) ...
 1-110 1.63e-58

ADP/ATP carrier protein family; These proteins are members of the ATP:ADP Antiporter (AAA) Family (TC 2.A.12), which consists of nucleotide transporters that have 12 GES predicted transmembrane regions. One protein from Rickettsia prowazekii functions to take up ATP from the eukaryotic cell cytoplasm into the bacterium in exchange for ADP. Five AAA family paralogues are encoded within the genome of R. prowazekii. This organism transports UMP and GMP but not CMP, and it seems likely that one or more of the AAA family paralogues are responsible. The genome of Chlamydia trachomatis encodes two AAA family members, Npt1 and Npt2, which catalyse ATP/ADP exchange and GTP, CTP, ATP and UTP uptake probably employing a proton symport mechanism. Two homologous adenylate translocators of Arabidopsis thaliana are postulated to be localized to the intracellular plastid membrane where they function as ATP importers. [Transport and binding proteins, Nucleosides, purines and pyrimidines]


Pssm-ID: 273262  Cd Length: 472  Bit Score: 186.50  E-value: 1.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786622127   1 MLLSQYIFDKYGWGVAAKITPTVLLLTGVGFFSLILFGGPIAPGLASLGMTPLLAAVYVGALQNIFSKSAKYSLFDPCKE 80
Cdd:TIGR00769 320 MLLSGNVIRKYGWLTAALITPLVMLLTGVAFFSLIFFGGPAAPLVAKLGMTPLLLAVYVGAIQNILSKSTKYSLFDATKE 399

                          90       100       110
                  ....*....|....*....|....*....|
gi 1786622127  81 MAYIPLDEDTKVKGKAAIDVVCNPLGKSGG 110
Cdd:TIGR00769 400 MAYIPLDEEQKVKGKAAIDVVAARLGKSGG 429
TLC pfam03219
TLC ATP/ADP transporter;
1-110 3.47e-54

TLC ATP/ADP transporter;


Pssm-ID: 397363  Cd Length: 491  Bit Score: 175.61  E-value: 3.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786622127   1 MLLSQYIFDKYGWGVAAKITPTVLLLTGVGFFSLILFGGPIAPGLASL-GMTPLLAAVYVGALQNIFSKSAKYSLFDPCK 79
Cdd:pfam03219 338 MFIGGNIIRRFGWTTAALITPIILLVTGVLFFGLIIFRDHAAGIFAGLiGTTPLLLAVVVGAIQNILSKSTKYSLFDATK 417

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1786622127  80 EMAYIPLDEDTKVKGKAAIDVVCNPLGKSGG 110
Cdd:pfam03219 418 EMAYIPLDDESKVKGKAAIDVVGARLGKSGG 448
TlcC COG3202
ATP/ADP translocase [Energy production and conversion];
1-110 1.75e-24

ATP/ADP translocase [Energy production and conversion];


Pssm-ID: 442435  Cd Length: 430  Bit Score: 95.32  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786622127   1 MLLSQYIFDKYGWGVAAKITPTVLLLTGVGFFSLIlfggpiapglaslgmtpllaAVYVGALQNIFSKSAKYSLFDPCKE 80
Cdd:COG3202   293 LFVTSRLLRRLGVGVALLITPVIILVGGLLFFLFP--------------------ALAVGAIQNVLSRALKYSLFDPTRE 352

                          90       100       110
                  ....*....|....*....|....*....|
gi 1786622127  81 MAYIPLDEDTKVKGKAAIDVVCNPLGKSGG 110
Cdd:COG3202   353 MLYIPLDRELKYKGKAFIDTVVYRLGKSLG 382
 
Name Accession Description Interval E-value
AAA TIGR00769
ADP/ATP carrier protein family; These proteins are members of the ATP:ADP Antiporter (AAA) ...
 1-110 1.63e-58

ADP/ATP carrier protein family; These proteins are members of the ATP:ADP Antiporter (AAA) Family (TC 2.A.12), which consists of nucleotide transporters that have 12 GES predicted transmembrane regions. One protein from Rickettsia prowazekii functions to take up ATP from the eukaryotic cell cytoplasm into the bacterium in exchange for ADP. Five AAA family paralogues are encoded within the genome of R. prowazekii. This organism transports UMP and GMP but not CMP, and it seems likely that one or more of the AAA family paralogues are responsible. The genome of Chlamydia trachomatis encodes two AAA family members, Npt1 and Npt2, which catalyse ATP/ADP exchange and GTP, CTP, ATP and UTP uptake probably employing a proton symport mechanism. Two homologous adenylate translocators of Arabidopsis thaliana are postulated to be localized to the intracellular plastid membrane where they function as ATP importers. [Transport and binding proteins, Nucleosides, purines and pyrimidines]


Pssm-ID: 273262  Cd Length: 472  Bit Score: 186.50  E-value: 1.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786622127   1 MLLSQYIFDKYGWGVAAKITPTVLLLTGVGFFSLILFGGPIAPGLASLGMTPLLAAVYVGALQNIFSKSAKYSLFDPCKE 80
Cdd:TIGR00769 320 MLLSGNVIRKYGWLTAALITPLVMLLTGVAFFSLIFFGGPAAPLVAKLGMTPLLLAVYVGAIQNILSKSTKYSLFDATKE 399

                          90       100       110
                  ....*....|....*....|....*....|
gi 1786622127  81 MAYIPLDEDTKVKGKAAIDVVCNPLGKSGG 110
Cdd:TIGR00769 400 MAYIPLDEEQKVKGKAAIDVVAARLGKSGG 429
TLC pfam03219
TLC ATP/ADP transporter;
1-110 3.47e-54

TLC ATP/ADP transporter;


Pssm-ID: 397363  Cd Length: 491  Bit Score: 175.61  E-value: 3.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786622127   1 MLLSQYIFDKYGWGVAAKITPTVLLLTGVGFFSLILFGGPIAPGLASL-GMTPLLAAVYVGALQNIFSKSAKYSLFDPCK 79
Cdd:pfam03219 338 MFIGGNIIRRFGWTTAALITPIILLVTGVLFFGLIIFRDHAAGIFAGLiGTTPLLLAVVVGAIQNILSKSTKYSLFDATK 417

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1786622127  80 EMAYIPLDEDTKVKGKAAIDVVCNPLGKSGG 110
Cdd:pfam03219 418 EMAYIPLDDESKVKGKAAIDVVGARLGKSGG 448
TlcC COG3202
ATP/ADP translocase [Energy production and conversion];
1-110 1.75e-24

ATP/ADP translocase [Energy production and conversion];


Pssm-ID: 442435  Cd Length: 430  Bit Score: 95.32  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786622127   1 MLLSQYIFDKYGWGVAAKITPTVLLLTGVGFFSLIlfggpiapglaslgmtpllaAVYVGALQNIFSKSAKYSLFDPCKE 80
Cdd:COG3202   293 LFVTSRLLRRLGVGVALLITPVIILVGGLLFFLFP--------------------ALAVGAIQNVLSRALKYSLFDPTRE 352

                          90       100       110
                  ....*....|....*....|....*....|
gi 1786622127  81 MAYIPLDEDTKVKGKAAIDVVCNPLGKSGG 110
Cdd:COG3202   353 MLYIPLDRELKYKGKAFIDTVVYRLGKSLG 382
 
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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