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Searching for up to 100 curated homologs for Pf6N2E2_1812 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1812 (338 a.a.)

Found high-coverage hits (≥70%) to 89 curated proteins.

You can add additional sequences or change the %identity threshold for inclusion. Once you have selected sequences, you can build an alignment and a tree.

Hits with ≥ 30% identity

TC 3.A.1.5.2 / P26905 DppD aka DCIAD, component of Dipeptide porter. Also transports δ-aminolevulinic acid (ALA) and heme from Bacillus subtilis (see 2 papers)
    49% identity, 95% coverage of query (305 bits)

OPPD_BACSU / P24136 Oligopeptide transport ATP-binding protein OppD; Stage 0 sporulation protein KD from Bacillus subtilis (strain 168) (see paper)
    49% identity, 89% coverage of query (298 bits)

TC 3.A.1.5.20 / P42064 AppD, component of 5-6 amino acyl oligopeptide transporter AppA-F from Bacillus subtilis (see 2 papers)
    46% identity, 95% coverage of query (290 bits)

TC 3.A.1.5.36 / Q93IU0 BldKD, putative ABC transporter intracellular ATPase subunit, component of Peptide transporter encoded adjacent to the putative transport system with TC#3.A.1.5.35 (Akanuma et al. 2011). Induced by exogenous S-adenosylmethionine (SAM) at a concentration of 2muM which also enhanced antibiotic production and inhibited morphological development (Park et al. 2005). SAM can be imported into cells. Mutants in the bldK genes confer resistance to the toxic tripeptide, bialaphos from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    50% identity, 88% coverage of query (290 bits)

TC 3.A.1.5.37 / B1W1L9 Putative peptide ABC transporter ATP-binding protein, component of The ABC BldKA-E (SGR_2418-2414) oligopeptide transport system. It controls aerial mycelium formation on glucose media. Probably involved in extracellular peptide signalling (Akanuma et al. 2011).  Probably orthologous to 3.A.1.5.35 from Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
    47% identity, 93% coverage of query (282 bits)

TC 3.A.1.5.19 / Q2FZR5 OppD, component of The major oligopeptide uptake porter, Opp-3 (of four paralogues, this is the only one that mediates nitrogen nutrition from Staphylococcus aureus (strain NCTC 8325)
    48% identity, 88% coverage of query (276 bits)

TC 3.A.1.5.1 / P04285 OppD aka STM1743, component of Oligopeptide porter (also takes up amino glycoside antibiotics such as kanamycin, streptomycin and neomycin as well as cell wall-derived peptides such as murein tripeptide). It transports substrate peptides of 2-5 amino acids with highest affinity for tripeptides. Also transports δ-aminolevulinic acid (ALA). [May be regulated by PTS Enzyme INtr-aspartokinase.] ATP-binding to OppDF may result in donation of peptide to OppBC and simultaneous release of OppA from Salmonella typhimurium (see 3 papers)
    46% identity, 94% coverage of query (275 bits)

OppD / b1246 murein tripeptide ABC transporter / oligopeptide ABC transporter ATP binding subunit OppD (EC 7.4.2.6) from Escherichia coli K-12 substr. MG1655 (see 4 papers)
oppD / P76027 murein tripeptide ABC transporter / oligopeptide ABC transporter ATP binding subunit OppD (EC 7.4.2.6) from Escherichia coli (strain K12) (see 2 papers)
TC 3.A.1.5.41 / P76027 Oligopeptide transport ATP-binding protein OppD, component of Oligopeptide transporter, OppABCDF/MppA/YgiS from Escherichia coli (strain K12)
oppD oligopeptide ABC transporter, ATP-binding protein OppD from Escherichia coli K12 (see paper)
    47% identity, 91% coverage of query (275 bits)

DPPD_LACLM / A2RI77 Dipeptide transport ATP-binding protein DppD; EC 7.4.2.9 from Lactococcus lactis subsp. cremoris (strain MG1363) (see paper)
    45% identity, 96% coverage of query (275 bits)

TC 3.A.1.5.29 / Q9WXR4 Oligopeptide ABC transporter, ATP-binding protein, component of Probable xylan oligosaccharide porter (Conners et al. 2005). Induced by cylan and xylose. Regulated by xylose-responsive regulator XylR from Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    46% identity, 88% coverage of query (273 bits)

Q5V9R9 ABC-type oligopeptide transporter (EC 7.4.2.6) from Vibrio fluvialis (see paper)
TC 3.A.1.5.22 / Q5V9R9 OppD, component of The peptide transporter OppA,B,C,D,F (influences biofilm formation; Lee et al., 2004). Similar to 3.A.1.5.1, OppA is similar to the Vibrio furnissii OppA that provides several functions: hemolysis, antibiotic resistance, and virulence from Vibrio fluvialis (see paper)
    45% identity, 91% coverage of query (272 bits)

TC 3.A.1.5.25 / Q9CIK9 Oligopeptide ABC trasporter ATP binding protein, component of The ABC peptide/signalling peptide transporter. OptA binds peptides of 3-6 aas; OptS binds dipeptides. OptB,C,D are most similar to 3.A.1.5.19 from Lactococcus lactis subsp. lactis (see paper)
    45% identity, 96% coverage of query (272 bits)

DppD / b3541 dipeptide ABC transporter ATP binding subunit DppD (EC 7.4.2.9) from Escherichia coli K-12 substr. MG1655 (see 5 papers)
dppD / P0AAG0 dipeptide ABC transporter ATP binding subunit DppD (EC 7.4.2.9) from Escherichia coli (strain K12) (see 4 papers)
DPPD_ECOLI / P0AAG0 Dipeptide transport ATP-binding protein DppD; EC 7.4.2.9 from Escherichia coli (strain K12) (see 3 papers)
dppD / RF|NP_417998 dipeptide transport ATP-binding protein dppD from Escherichia coli K12 (see paper)
    45% identity, 95% coverage of query (271 bits)

GsiA / b0829 glutathione ABC transporter ATP binding subunit GsiA (EC 7.4.2.10) from Escherichia coli K-12 substr. MG1655 (see 3 papers)
gsiA / P75796 glutathione ABC transporter ATP binding subunit GsiA (EC 7.4.2.10) from Escherichia coli (strain K12) (see 3 papers)
GSIA_ECOLI / P75796 Glutathione import ATP-binding protein GsiA; EC 7.4.2.10 from Escherichia coli (strain K12) (see paper)
P75796 ABC-type glutathione transporter (EC 7.4.2.10) from Escherichia coli (see paper)
TC 3.A.1.5.11 / P75796 Hypothetical ABC transporter ATP-binding protein yliA, component of Glutathione porter, YliABCD or GsiABCD from Escherichia coli (see 4 papers)
    52% identity, 79% coverage of query (270 bits)

TC 3.A.1.5.15 / Q9X271 TM1749, component of Probable mannose/mannoside porter. Induced by beta-mannan (Conners et al., 2005). Regulated by mannose-responsive regulator manR (see paper)
    43% identity, 95% coverage of query (268 bits)

DPPD_PSEAB / A0A0H2ZGN6 Di/tripeptide transport ATP-binding protein DppD; EC 7.4.2.9 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
TC 3.A.1.5.39 / W0WJ90 Dipeptide transport ATP-binding protein DppD, component of Di- and tri-peptide transporter, DppBCDF with periplasmic substrate binding receptors, A1, A3, A5, A7 and A9, each with differing specificities for peptides from Pseudomonas aeruginosa MH38
    47% identity, 95% coverage of query (266 bits)

TC 3.A.1.5.12 / Q9X0F4 TM1064, component of Probable rhamnose oligosaccharide porter. Induced by rhamnose (see paper)
    46% identity, 88% coverage of query (266 bits)

TC 3.A.1.5.27 / P45095 Dipeptide transport ATP-binding protein DppD, component of The glutathione uptake porter, DppBCDF with the glutathione binding protein, DppA (GbpA; HbpA). Takes up reduced (GSH) and oxidized (GSSG) but not bulky glutathione S conjugates or glutathione derivatives with C-terminal modifications from Haemophilus influenzae (see 2 papers)
    46% identity, 93% coverage of query (265 bits)

DdpD / b1484 putative D,D-dipeptide ABC transporter ATP-binding subunit DdpD from Escherichia coli K-12 substr. MG1655 (see paper)
DDPD_ECOLI / P77268 Probable D,D-dipeptide transport ATP-binding protein DdpD from Escherichia coli (strain K12) (see paper)
    43% identity, 96% coverage of query (263 bits)

TC 3.A.1.5.18 / O31309 OppD, component of The oligopeptide transporter OppA1-5, B1, C1, DF (functions with five binding proteins of differing induction properties and peptide specificities; OppA1-3 are chromosomally encoded; OppA4 and 5 are plasmid encoded.) from Borrelia burgdorferi (Lyme disease spirochete) (see 2 papers)
    49% identity, 77% coverage of query (261 bits)

TC 3.A.1.5.32 / F0TFT0 Oligopeptide ABC transporter, component of ABC α-galactoside uptake porter from Lactobacillus acidophilus (strain 30SC)
    45% identity, 87% coverage of query (259 bits)

SM_b21644 ABC transporter for D-Raffinose, ATPase component from Sinorhizobium meliloti 1021
    55% identity, 71% coverage of query (257 bits)

TC 3.A.1.5.10 / Q07733 OppD, component of Oligopeptide porter (transports peptides of 4-35) amino acyl residues; di- and tripeptides are not transported; hydrophobic basic peptides are preferred). OppA determines the specificity of the system (Doeven et al., 2004). A large cavity in OppA binds proline-rich peptides preferentially (Berntsson et al., 2009). Two crystal structures of OppA with different nonapeptides show binding in different registers from Lactococcus lactis subsp. lactis (Streptococcus lactis) (see 2 papers)
    53% identity, 76% coverage of query (256 bits)

Q8ZQM4 ABC-type glutathione transporter (EC 7.4.2.10) from Salmonella enterica subsp. enterica serovar Typhimurium (see paper)
    54% identity, 70% coverage of query (255 bits)

A0A150QXP6 5-(carboxyamino)imidazole ribonucleotide mutase (EC 5.4.99.18) from Bacillus anthracis (see paper)
    42% identity, 92% coverage of query (253 bits)

TC 3.A.1.5.26 / P63395 Uncharacterized ABC transporter ATP-binding protein Rv1281c/MT1318, component of The glutathione transporter, OppA (Dasgupta et al., 2010). OppA binds glutathione and the nanopeptide, bradykinin. Also regulates cytokine release, apoptosis and the innate immune response of macrophages infected with M. tuberculosis from Mycobacterium tuberculosis (see 2 papers)
    45% identity, 89% coverage of query (252 bits)

TC 3.A.1.5.23 / Q9F9T4 EppD, component of The Ethylene diamine tetraacetate (EDTA) uptake porter, EppABCD (see 2 papers)
    52% identity, 71% coverage of query (244 bits)

TC 3.A.1.5.24 / Q8ZNJ8 YejF, component of The antimicrobial peptide (protamine, melittin, polymyxin B, human defensin (HBD)-1 and HBD-2 exporter, YejABEF (Eswarappa et al., 2008). Prefers N-formyl methionine peptides, such as Microcin C (of prokaryotic origin) to non formylated peptides (of eukaryotic origin) from Salmonella typhimurium (see paper)
    48% identity, 79% coverage of query (242 bits)

TC 3.A.1.5.4 / O30541 AccB, component of Agrocinopine (an opine)/Agrocin 84 (an antibiotic) porter from Agrobacterium radiobacter (see 3 papers)
    44% identity, 91% coverage of query (239 bits)

Q5V9R8 ABC-type oligopeptide transporter (EC 7.4.2.6) from Vibrio fluvialis (see paper)
TC 3.A.1.5.22 / Q5V9R8 OppF, component of The peptide transporter OppA,B,C,D,F (influences biofilm formation; Lee et al., 2004). Similar to 3.A.1.5.1, OppA is similar to the Vibrio furnissii OppA that provides several functions: hemolysis, antibiotic resistance, and virulence from Vibrio fluvialis (see paper)
    40% identity, 95% coverage of query (239 bits)

YejF / b2180 putative oligopeptide ABC transporter ATP binding subunit YejF (EC 7.4.2.6) from Escherichia coli K-12 substr. MG1655 (see 6 papers)
YejF / P33916 putative oligopeptide ABC transporter ATP binding subunit YejF (EC 7.4.2.6) from Escherichia coli (strain K12) (see 3 papers)
TC 3.A.1.5.21 / P33916 YejF, component of The Microcin C/peptide uptake porter, YejABEF from Escherichia coli (strain K12) (see 3 papers)
yejF / RF|NP_416685 uncharacterized ABC transporter ATP-binding protein yejF from Escherichia coli K12 (see paper)
    48% identity, 78% coverage of query (234 bits)

TC 3.A.1.5.27 / P45094 Dipeptide transport ATP-binding protein DppF, component of The glutathione uptake porter, DppBCDF with the glutathione binding protein, DppA (GbpA; HbpA). Takes up reduced (GSH) and oxidized (GSSG) but not bulky glutathione S conjugates or glutathione derivatives with C-terminal modifications from Haemophilus influenzae (see 2 papers)
    42% identity, 88% coverage of query (232 bits)

TC 3.A.1.5.1 / P08007 OppF aka STM1742, component of Oligopeptide porter (also takes up amino glycoside antibiotics such as kanamycin, streptomycin and neomycin as well as cell wall-derived peptides such as murein tripeptide). It transports substrate peptides of 2-5 amino acids with highest affinity for tripeptides. Also transports δ-aminolevulinic acid (ALA). [May be regulated by PTS Enzyme INtr-aspartokinase.] ATP-binding to OppDF may result in donation of peptide to OppBC and simultaneous release of OppA from Salmonella typhimurium (see 2 papers)
    41% identity, 96% coverage of query (229 bits)

SapD / b1291 putrescine ABC exporter ATP binding protein SapD (EC 7.6.2.16) from Escherichia coli K-12 substr. MG1655 (see 5 papers)
SapD / P0AAH4 putrescine ABC exporter ATP binding protein SapD (EC 7.6.2.16) from Escherichia coli (strain K12) (see 5 papers)
SAPD_ECOLI / P0AAH4 Putrescine export system ATP-binding protein SapD from Escherichia coli (strain K12) (see 2 papers)
    35% identity, 95% coverage of query (200 bits)

4fwiB / Q8RDH4 Crystal structure of the nucleotide-binding domain of a dipeptide abc transporter (see paper)
    37% identity, 88% coverage of query (187 bits)

DPPD_CALS4 / Q8RDH4 Dipeptide transport ATP-binding protein DppD; EC 7.4.2.9 from Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis) (see paper)
    37% identity, 88% coverage of query (187 bits)

4u00A / Q5SJ55 Crystal structure of ttha1159 in complex with adp (see paper)
    34% identity, 70% coverage of query (134 bits)

3c4jA Abc protein artp in complex with atp-gamma-s
    32% identity, 70% coverage of query (128 bits)

3c41J / D0VWX4 Abc protein artp in complex with amp-pnp/mg2+
    32% identity, 70% coverage of query (128 bits)

2olkA Abc protein artp in complex with adp-beta-s
    32% identity, 70% coverage of query (128 bits)

2oljA Abc protein artp in complex with adp/mg2+
    32% identity, 70% coverage of query (128 bits)

4ymuJ / Q8RCC2 Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
    31% identity, 70% coverage of query (117 bits)

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Build an alignment for Pf6N2E2_1812 and 42 homologs with ≥ 30% identity

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Additional hits (identity < 30%)

7ahhC Opua inhibited inward-facing, sbd docked
    29% identity, 84% coverage of query (116 bits)

7aheC / Q9KIF7 Opua inhibited inward facing (see paper)
    29% identity, 84% coverage of query (116 bits)

MetN / b0199 L-methionine/D-methionine ABC transporter ATP binding subunit (EC 7.4.2.11) from Escherichia coli K-12 substr. MG1655 (see 4 papers)
MetN / P30750 L-methionine/D-methionine ABC transporter ATP binding subunit (EC 7.4.2.11) from Escherichia coli (strain K12) (see 3 papers)
METN_ECOLI / P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 7 papers)
P30750 ABC-type methionine transporter (subunit 2/2) (EC 7.4.2.11) from Escherichia coli (see 3 papers)
TC 3.A.1.24.1 / P30750 MetN, D-methionine transport ATP-binding protein, component of The L- and D-methionine porter (also transports formyl-L-methionine and other methionine derivatives) (Zhang et al., 2003). The 3.7A structure of MetNI has been solved. An allosteric regulatory mechanism operates at the level of transport activity, so increased intracellular levels of the transported ligand stabilize an inward-facing, ATPase-inactive state of MetNI to inhibit further ligand translocation into the cell from Escherichia coli (see 5 papers)
    32% identity, 70% coverage of query (111 bits)

3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form
    32% identity, 70% coverage of query (110 bits)

3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form
    32% identity, 70% coverage of query (110 bits)

6cvlD / P30750 Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
    32% identity, 70% coverage of query (110 bits)

7w78A / Q6NEF2 Heme exporter hrtba in complex with mg-amppnp (see paper)
    37% identity, 70% coverage of query (108 bits)

5ws4A / A0A0D8G707 Crystal structure of tripartite-type abc transporter macb from acinetobacter baumannii (see paper)
    33% identity, 71% coverage of query (107 bits)

7w79A Heme exporter hrtba in complex with mn-amppnp
    36% identity, 72% coverage of query (107 bits)

MacB / b0879 ABC-type tripartite efflux pump ATP binding/membrane subunit from Escherichia coli K-12 substr. MG1655 (see 14 papers)
MacB / P75831 ABC-type tripartite efflux pump ATP binding/membrane subunit from Escherichia coli (strain K12) (see 16 papers)
MACB_ECOLI / P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see 5 papers)
TC 3.A.1.122.1 / P75831 MacB aka B0879, component of Macrolide (14- and 15- but not 16-membered lactone macrolides including erythromycin) exporter, MacAB (formerly YbjYZ). Both MacA and MacB are required for activity (Tikhonova et al., 2007). MacAB functions with TolC to export multiple drugs and heat-stable enterotoxin II (enterotoxin STII) (Yamanaka et al., 2008). The crystal structure of MacA is available (Yum et al., 2009). MacB is a dimer whose ATPase activity and macrolide-binding capacity are regulated by the membrane fusion protein MacA (Lin et al., 2009). Xu et al. (2009) have reported the crystal structure of the periplasmic region of MacB which they claim resembles the periplasmic domain of RND-type transporters such as AcrB (TC# 2.A.6.2.2). Also exports L-cysteine (Yamada et al., 2006). The periplasmic membrane proximal domain of MacA acts as a switch in stimulation of ATP hydrolysis by the MacB transporter from Escherichia coli (see 5 papers)
macB / BAB64542.1 macrolide-specific ABC-type efflux carrier from Escherichia coli (see paper)
    33% identity, 71% coverage of query (106 bits)

2d62A / O57933 Crystal structure of multiple sugar binding transport atp- binding protein
    29% identity, 70% coverage of query (105 bits)

1g291 / Q9YGA6 Malk (see paper)
    29% identity, 70% coverage of query (103 bits)

8bmpA Cryo-em structure of the folate-specific ecf transporter complex in msp2n2 lipid nanodiscs bound to atp and adp
    33% identity, 75% coverage of query (103 bits)

5d3mA / Q1GBJ0 Folate ecf transporter: amppnp bound state (see paper)
    33% identity, 75% coverage of query (103 bits)

ECFA1_STRT2 / Q5M243 Energy-coupling factor transporter ATP-binding protein EcfA1; ECF transporter A component EcfA1; EC 7.-.-.- from Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) (see paper)
TC 3.A.1.25.6 / Q5M243 Energy-coupling factor transporter ATP-binding protein EcfA 2, component of Riboflavin ECF transport system, EcfAA'T/RibU from Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
    29% identity, 72% coverage of query (103 bits)

8bmsA Cryo-em structure of the mutant solitary ecf module 2eq in msp2n2 lipid nanodiscs in the atpase closed and atp-bound conformation
    32% identity, 76% coverage of query (102 bits)

PotA / b1126 spermidine preferential ABC transporter ATP binding subunit (EC 7.6.2.11; EC 7.6.2.16) from Escherichia coli K-12 substr. MG1655 (see 5 papers)
PotA / P69874 spermidine preferential ABC transporter ATP binding subunit (EC 7.6.2.11) from Escherichia coli (strain K12) (see 5 papers)
POTA_ECOLI / P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 6 papers)
TC 3.A.1.11.1 / P69874 Spermidine/putrescine import ATP-binding protein PotA aka B1126, component of Polyamine (putrescine/spermidine) uptake porter from Escherichia coli (see 9 papers)
potA / MB|P69874 spermidine/putrescine ABC transporter, ATP-binding protein PotA; EC 3.6.3.31 from Escherichia coli K12 (see 10 papers)
    29% identity, 70% coverage of query (102 bits)

sugC / P9WQI3 ABC-type trehalose transporter ATP-binding protein from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
SUGC_MYCTU / P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
TC 3.A.1.1.31 / O50454 PROBABLE SUGAR-TRANSPORT ATP-BINDING PROTEIN ABC TRANSPORTER SUGC, component of The trehalose-recycling ABC transporter, LpqY-SugA-SugB-SugC (essential for virulence) from Mycobacterium tuberculosis (see 2 papers)
    29% identity, 72% coverage of query (101 bits)

8hprD Lpqy-sugabc in state 4
    29% identity, 71% coverage of query (97.1 bits)

8hprC Lpqy-sugabc in state 4
    29% identity, 71% coverage of query (97.1 bits)

1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus
    27% identity, 74% coverage of query (94.7 bits)

1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus
    27% identity, 74% coverage of query (94.7 bits)

GLCV_SACS2 / Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see 3 papers)
TC 3.A.1.1.13 / Q97UY8 GlcV, component of Glucose, mannose, galactose porter from Sulfolobus solfataricus (see 3 papers)
1oxuA / Q97UY8 Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
    27% identity, 74% coverage of query (94.7 bits)

3fvqB / Q5FA19 Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
    31% identity, 74% coverage of query (92.0 bits)

6xgyA Crystal structure of e. Coli mlafb abc transport subunits in the dimeric state
    29% identity, 72% coverage of query (88.6 bits)

7ch6C / P63386 Cryo-em structure of e.Coli mlafeb with amppnp (see paper)
    29% identity, 72% coverage of query (88.6 bits)

7cgnB The overall structure of the mlafedb complex in atp-bound eqtall conformation (mutation of e170q on mlaf)
    29% identity, 72% coverage of query (87.4 bits)

Q8TTZ3 ABC-type molybdate transporter (EC 7.3.2.5) from Methanosarcina acetivorans (see paper)
3d31A / Q8TTZ3 Modbc from methanosarcina acetivorans (see paper)
    29% identity, 76% coverage of query (84.3 bits)

4f4cA / P34712 The crystal structure of the multi-drug transporter (see paper)
    28% identity, 71% coverage of query (78.6 bits)

1jj7A / Q03518 Crystal structure of thE C-terminal atpase domain of human tap1 (see paper)
    31% identity, 73% coverage of query (77.0 bits)

TAP1_HUMAN / Q03518 Antigen peptide transporter 1; APT1; ATP-binding cassette sub-family B member 2; Peptide supply factor 1; Peptide transporter PSF1; PSF-1; Peptide transporter TAP1; Peptide transporter involved in antigen processing 1; Really interesting new gene 4 protein; RING4; EC 7.4.2.14 from Homo sapiens (Human) (see 30 papers)
Q03518 ABC-type antigen peptide transporter (EC 7.4.2.14); bacterial ABC-type protein transporter (EC 7.4.2.5) from Homo sapiens (see 2 papers)
    31% identity, 73% coverage of query (75.9 bits)

2onjA Structure of the multidrug abc transporter sav1866 from s. Aureus in complex with amp-pnp
    27% identity, 70% coverage of query (75.1 bits)

Y1866_STAAM / Q99T13 Putative multidrug export ATP-binding/permease protein SAV1866; EC 7.6.2.- from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see paper)
Q99T13 ABC-type xenobiotic transporter (EC 7.6.2.2) from Staphylococcus aureus (see paper)
TC 3.A.1.106.2 / Q2G2M9 The homodimeric Sav1866 multidrug exporter (transports doxorubicin, verapamil, ethidium, tetraphenylphosphonium, vinblastine and the fluorescent dye, Hoechst 33342; 3-D structure known at 3 Å resolution; Dawson and Locher, 2006; Velamakanni et al., 2008) The empty site opens by rotation of the nucleotide-binding domain whereas the ATP-bound site remains occluded (Jones and George, 2011). Conformational changes induced by ATP-binding and hydrolysis have been proposed (Becker et al. 2010; Oliveira et al., 2011). The alternating access mechanism and the flippase activity of this ABC exporter has been shown to be lipid-dependent (Becker et al. 2010; Oliveira et al., 2011). The alternating access mechanism and the flippase activity of this ABC exporter has been shown to be lipid-dependent from Staphylococcus aureus (strain NCTC 8325)
2hydA / Q99T13 Multidrug abc transporter sav1866 (see paper)
    27% identity, 70% coverage of query (75.1 bits)

8ipsA / P23886 Cryo-em structure of heme transporter cyddc from escherichia coli in the inward facing heme loading state (see paper)
    28% identity, 70% coverage of query (73.9 bits)

7zdkC If(apo/asym) conformation of cyddc in amp-pnp(cydc)/amp-pnp(cydd) bound state (dataset-8)
    28% identity, 70% coverage of query (71.2 bits)

7zdfC If(heme/confined) conformation of cyddc in amp-pnp(cydd) bound state (dataset-4)
    28% identity, 70% coverage of query (71.2 bits)

ABCBB_RAT / O70127 Bile salt export pump; ATP-binding cassette sub-family B member 11; Sister of P-glycoprotein; EC 7.6.2.- from Rattus norvegicus (Rat) (see 12 papers)
    28% identity, 72% coverage of query (70.1 bits)

8pm6A / O95342 Human bile salt export pump (bsep) in complex with inhibitor gbm in nanodiscs (see paper)
    28% identity, 72% coverage of query (65.5 bits)

ABCG8_MOUSE / Q9DBM0 ATP-binding cassette sub-family G member 8; Sterolin-2; EC 7.6.2.- from Mus musculus (Mouse) (see 13 papers)
    26% identity, 72% coverage of query (63.5 bits)

TAP1_RAT / P36370 Antigen peptide transporter 1; APT1; ATP-binding cassette sub-family B member 2; Peptide transporter TAP1; EC 7.4.2.14 from Rattus norvegicus (Rat) (see 2 papers)
P36370 ABC-type antigen peptide transporter (subunit 2/2) (EC 7.4.2.14) from Rattus norvegicus (see 6 papers)
    27% identity, 70% coverage of query (62.8 bits)

ECSA_BACSU / P55339 ABC-type transporter ATP-binding protein EcsA from Bacillus subtilis (strain 168) (see paper)
TC 3.A.1.143.1 / P55339 ABC-type transporter ATP-binding protein EcsA, component of The exoprotein (including α-amylase) secretion system, EcsAB(C) (Leskelä et al., 1999). Also may play roles in sporulation, competence (Leskelä et al., 1996) and transformation using purified DNA (Takeno et al., 2011). An involvement of EcsC in transport is not established, but it is homologous to the C-terminus of the P-type ATPase, 3.A.3.31.2 from Bacillus subtilis (strain 168) (see 3 papers)
    26% identity, 70% coverage of query (61.6 bits)

ABCG2_HUMAN / Q9UNQ0 Broad substrate specificity ATP-binding cassette transporter ABCG2; ATP-binding cassette sub-family G member 2; Breast cancer resistance protein; CDw338; Mitoxantrone resistance-associated protein; Placenta-specific ATP-binding cassette transporter; Urate exporter; CD338 antigen; EC 7.6.2.2 from Homo sapiens (Human) (see 29 papers)
Q9UNQ0 ABC-type xenobiotic transporter (EC 7.6.2.2); ABC-type glutathione-S-conjugate transporter (EC 7.6.2.3) from Homo sapiens (see 11 papers)
TC 3.A.1.204.2 / Q9UNQ0 Drug resistance transporter, ABCG2 (MXR; ABCP) (human breast cancer resistance protein, BCRP) (Moitra et al., 2011). It exports urate and haem in haempoietic cells (Latunde-Dada et al., 2006) as well as cytotoxic agents (mitoxantrone, flavopiridol, methotrexate, 7-hydroxymethotrexate, methotrexate diglutamate, topotecan, rosurvastatin, and resveratrol), fluorescent dyes (Hoechst 33342) and other toxic substances (PhIP and pheophorbide a) (Özvegy-Laczka et al., 2005; Nigam 2015). It also transports folate and sterols: estradiol, and probably cholesterol, progesterone, testosterone and tamoxifen (Janvilisri et al., 2003; Breedveld et al., 2007). It is a homotetramer (Xu et al., 2004). It forms a homodimer bound via a disulfide bond at Cys-603 which stabilizes the protein against ubiquitin-mediated degradation in proteosomes (Wakabayashi et al., 2007), and can for dodecamers with 12 subunits (Xu et al. 2007). It has 6 established TMSs with the N- and C- termini inside (Wang et al., 2008). The following drugs are exported from human breast cancer cell line MCF-7: miloxantrone, daunorubicin, doxorubicin and rhodamine123). Also transports reduced folates and mono-, di- and tri-glutamate derivatives of folic acid and methotrexate (Assaraf et al., 2006). It is an active glutathione efflux pump (Brechbuhl et al., 2010). Mutations in ABCG2 cause hyperuricemia and gout , which led to the identification of urate as a physiological subsrate for ABCG2; it catalyzes elimination of urate across the renal tubular apical membrane (see 17 papers)
ABCG2 / GB|ABI97388.1 ATP-binding cassette sub-family G member 2 from Homo sapiens (see paper)
    25% identity, 72% coverage of query (61.2 bits)

STE6_YEAST / P12866 Alpha-factor-transporting ATPase; Mating factor A secretion protein STE6; Multiple drug resistance protein homolog; P-glycoprotein; EC 7.4.2.7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
P12866 ABC-type alpha-factor-pheromone transporter (EC 7.4.2.7) from Saccharomyces cerevisiae (see paper)
TC 3.A.1.206.1 / P12866 a-Factor sex pheromone (a hydrophobic isoprenylated (farnesylated) carboxymethylated peptide) exporter, Ste6 from Saccharomyces cerevisiae (Baker's yeast) (see 9 papers)
STE6 / RF|NP_012713.1 alpha-factor-transporting ATPase from Saccharomyces cerevisiae
    26% identity, 73% coverage of query (60.8 bits)

6hijA Cryo-em structure of the human abcg2-mz29-fab complex with cholesterol and pe lipids docked
    25% identity, 72% coverage of query (60.1 bits)

AB12G_ARATH / Q9C8K2 ABC transporter G family member 12; ABC transporter ABCG.12; AtABCG12; Protein ECERIFERUM 5; White-brown complex homolog protein 12; AtWBC12 from Arabidopsis thaliana (Mouse-ear cress) (see 6 papers)
TC 3.A.1.204.4 / Q9C8K2 The plant cuticular wax and/or lipid metabolite exporter, CER5; ABCG12; WBC12 (in the plasma membrane of epidermal cells; secretes wax to the plant surface) from Arabidopsis thaliana (Mouse-ear cress) (see 8 papers)
WBC12 / RF|NP_175561.1 white-brown complex homolog protein 12 from Arabidopsis thaliana (see paper)
    26% identity, 75% coverage of query (59.7 bits)

6hbuA / Q9UNQ0 Cryo-em structure of the abcg2 e211q mutant bound to atp and magnesium (see paper)
    25% identity, 72% coverage of query (58.9 bits)

3bk7A / Q9UZA4 Structure of the complete abce1/rnaase-l inhibitor protein from pyrococcus abysii (see paper)
    23% identity, 70% coverage of query (54.3 bits)

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by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory