Searching for up to 100 curated homologs for 206067 MicrobesOnline__882:206067 (271 a.a.)
Found high-coverage hits (≥70%) to 100 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.
FPUD_BACAN / Q81V82 Petrobactin import ATP-binding protein FpuD; EC 7.2.2.- from Bacillus anthracis (see paper)
34% identity, 99% coverage of query (170 bits)
TC 3.A.1.14.7 / Q9X665 FhuC aka FhuA, component of Iron (Fe3+)-hydroxamate porter (transports Fe3+-ferrichrome and Fe3+-ferrioxamine B with FhuD1, and these compounds plus aerobactin and coprogen with FhuD2) (see 2 papers)
35% identity, 90% coverage of query (165 bits)
YUSV_BACSU / O32188 Probable siderophore transport system ATP-binding protein YusV from Bacillus subtilis (strain 168) (see 2 papers)
34% identity, 96% coverage of query (158 bits)
FepC / b0588 ferric enterobactin ABC transporter ATP binding subunit (EC 7.2.2.17) from Escherichia coli K-12 substr. MG1655 (see 4 papers)
FepC / P23878 ferric enterobactin ABC transporter ATP binding subunit (EC 7.2.2.17) from Escherichia coli (strain K12) (see 3 papers)
FEPC_ECOLI / P23878 Ferric enterobactin transport ATP-binding protein FepC; EC 7.2.2.17 from Escherichia coli (strain K12) (see 3 papers)
TC 3.A.1.14.2 / P23878 FepC aka B0588, component of Iron (Fe3+)-enterobactin porter from Escherichia coli (see 3 papers)
36% identity, 89% coverage of query (156 bits)
FhuC / b0151 iron(III) hydroxamate ABC transporter ATP binding subunit (EC 7.2.2.16) from Escherichia coli K-12 substr. MG1655 (see 3 papers)
FhuC / P07821 iron(III) hydroxamate ABC transporter ATP binding subunit (EC 7.2.2.16) from Escherichia coli (strain K12) (see paper)
FHUC_ECOLI / P07821 Iron(3+)-hydroxamate import ATP-binding protein FhuC; Ferric hydroxamate uptake protein C; Ferrichrome transport ATP-binding protein FhuC; Iron(III)-hydroxamate import ATP-binding protein FhuC; EC 7.2.2.16 from Escherichia coli (strain K12) (see 3 papers)
TC 3.A.1.14.3 / P07821 FhuC aka B0151, component of Iron (Fe3+)-hydroxamate (ferrichrome, coprogen, aerobactin, ferrioxamine B, schizakinen, rhodotorulic acid) porter, albomycin porter from Escherichia coli (see 6 papers)
fhuC / GB|BAB96727.2 ferrichrome transport ATP-binding protein FhuC; EC 3.6.3.34 from Escherichia coli K12 (see 8 papers)
38% identity, 86% coverage of query (155 bits)
TC 3.A.1.14.6 / Q9RCF3 ViuC, component of The iron-vibriobactin/enterobactin uptake porter from Vibrio cholerae (see 2 papers)
37% identity, 92% coverage of query (150 bits)
TC 3.A.1.14.8 / Q8GRB0 PvuE, component of The iron-vibrioferrin uptake porter from Vibrio parahaemolyticus (see paper)
33% identity, 92% coverage of query (147 bits)
TC 3.A.1.14.4 / Q47087 CbrD, component of Iron-chrysobactine porter from Erwinia chrysanthemi (see paper)
cbrD / GB|CAA60669.1 achromobactin ABC transporter, ATP-binding protein CbrD from Erwinia chrysanthemi str. 3937 (see paper)
35% identity, 88% coverage of query (147 bits)
FecE / b4287 ferric citrate ABC transporter ATP binding subunit (EC 7.2.2.18) from Escherichia coli K-12 substr. MG1655 (see 2 papers)
FecE / P15031 ferric citrate ABC transporter ATP binding subunit (EC 7.2.2.18) from Escherichia coli (strain K12) (see 2 papers)
FECE_ECOLI / P15031 Fe(3+) dicitrate transport ATP-binding protein FecE; Iron(III) dicitrate transport ATP-binding protein FecE; EC 7.2.2.18 from Escherichia coli (strain K12) (see 3 papers)
TC 3.A.1.14.1 / P15031 Fe(3+) dicitrate transport ATP-binding protein FecE, component of Iron (Fe3+) or ferric-dicitrate porter from Escherichia coli (strain K12) (see 4 papers)
fecE / GB|AAC77243.1 iron(III) dicitrate transport ATP-binding protein FecE from Escherichia coli K12 (see 6 papers)
33% identity, 90% coverage of query (145 bits)
TC 3.A.1.14.14 / Q9A197 Putative ferrichrome ABC transporter aka SiuA aka Spy0386, component of The Fe3+ /Fe3+ferrichrome/Fe3+heme uptake porter; SiuABDG (FTSABCD) from Streptococcus pyogenes serotype M1 (see 2 papers)
32% identity, 90% coverage of query (144 bits)
fhuC / GI|2832798 ferrichrome transport ATP-binding protein FhuC from Bacillus subtilis (see paper)
33% identity, 92% coverage of query (141 bits)
BTUDA_HALSA / Q9HQ18 Cobalamin import ATP-binding protein BtuD; Vitamin B12-transporting ATPase; EC 7.6.2.8 from Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) (see paper)
41% identity, 94% coverage of query (138 bits)
TC 3.A.1.14.13 / Q9RK11 CchE, component of Ferric iron-coelichelin uptake porter, CchCDEF from Streptomyces coelicolor (see paper)
39% identity, 92% coverage of query (137 bits)
TC 3.A.1.14.12 / Q9L177 DesC, component of Desferrioxamine B uptake porter, DesABC from Streptomyces coelicolor (see paper)
40% identity, 87% coverage of query (136 bits)
FPUC_BACAN / Q81LM1 Petrobactin import ATP-binding protein FpuC; EC 7.2.2.- from Bacillus anthracis (see paper)
34% identity, 85% coverage of query (136 bits)
YCLP_BACSU / P94420 Petrobactin import ATP-binding protein YclP; EC 7.2.2.- from Bacillus subtilis (strain 168) (see paper)
32% identity, 89% coverage of query (135 bits)
TC 3.A.1.14.5 / Q56993 HmuV aka YPO0279 aka Y0539, component of Heme (hemin) uptake porter. The receptor, HmuT, binds two parallel stacked heme molecules, and two are transported per reaction cycle from Yersinia pestis (see 4 papers)
hmuV hemin import ATP-binding protein hmuV; EC 3.6.3.- from Yersinia pestis KIM (see paper)
35% identity, 92% coverage of query (134 bits)
MNTB_BACSU / O34338 Manganese transport system ATP-binding protein MntB from Bacillus subtilis (strain 168) (see paper)
34% identity, 88% coverage of query (131 bits)
TC 3.A.1.14.10 / Q99YA4 Putative ABC transporter aka SiaC, component of The heme porter, Shp/SiaABC (HtsABC). Shp is a cell surface heme binding protein that transfers the heme directly to HstA (Nygaard et al., 2006). The crystal structure of the heme binding domain of Shp has been solved (Aranda et al., 2007). HtsABC is required for the uptake of staphyloferrin A (Beasley et al. 2009). The Shp cell surface heme receptor feeds iron-heme to the transporter in preparation for uptake from Streptococcus pyogenes serotype M1 (see 2 papers)
33% identity, 86% coverage of query (129 bits)
TC 3.A.1.14.18 / Q32AY3 Hemin import ATP-binding protein hmuV, component of The heme uptake porter, ShuTUV (Burkhard and Wilks, 2008). Transports a single heme per reaction cycle (Mattle et al., 2010). (3-d structure of ShuT is known (2RG7) from Shigella dysenteriae serotype 1 (strain Sd197) (see paper)
35% identity, 82% coverage of query (125 bits)
TC 3.A.1.15.8 / P96117 TroB, component of Manganese (Mn2+), zinc (Zn2+) and possibly iron (Fe2+) uptake porter, TroABCD from Treponema pallidum (see 2 papers)
35% identity, 88% coverage of query (125 bits)
TC 3.A.1.14.21 / O68877 Hemin import ATP-binding protein HmuV, component of The heme uptake porter, PhuTUV (transports one heme per reaction cycle) from Pseudomonas aeruginosa (see 2 papers)
38% identity, 92% coverage of query (124 bits)
Q832Z4 ABC-type Mn2+ transporter (subunit 3/3) (EC 7.2.2.5) from Enterococcus faecalis (see paper)
33% identity, 85% coverage of query (122 bits)
4u00A / Q5SJ55 Crystal structure of ttha1159 in complex with adp (see paper)
31% identity, 83% coverage of query (103 bits)
LolD / b1117 lipoprotein release complex - ATP binding subunit from Escherichia coli K-12 substr. MG1655 (see 2 papers)
LolD / P75957 lipoprotein release complex - ATP binding subunit from Escherichia coli (strain K12) (see paper)
LOLD_ECOLI / P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
TC 3.A.1.125.1 / P75957 LolD aka B1117, component of Lipoprotein translocation system (translocates lipoproteins from the inner membrane to periplasmic chaperone, LolA, which transfers the lipoproteins to an outer membrane receptor, LolB, which anchors the lipoprotein to the outer membrane of the Gram-negative bacterial cell envelope) (see 1.B.46; Narita et al., 2003; Ito et al., 2006; Watanabe et al., 2007). The structure of ligand-bound LolCDE has been solved (Ito et al., 2006). LolC and LolE each have 4 TMSs (1+3). Unlike most ATP binding cassette transporters mediating the transmembrane flux of substrates, the LolCDE complex catalyzes the extrusion of lipoproteins anchored to the outer leaflet of the inner membrane. The LolCDE complex is unusual in that it can be purified as a liganded form, which is an intermediate of the lipoprotein release reaction (Taniguchi and Tokuda, 2008). LolCDE has been reconstituted from separated subunits from Escherichia coli (see 5 papers)
lolD / GB|BAA35937.2 lipoprotein releasing system, ATP-binding protein; EC 3.6.3.- from Escherichia coli K12 (see 5 papers)
31% identity, 79% coverage of query (101 bits)
7arlD Lolcde in complex with lipoprotein and adp
31% identity, 79% coverage of query (101 bits)
7mdyC Lolcde nucleotide-bound
31% identity, 79% coverage of query (101 bits)
7v8iD / P75957 Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
31% identity, 79% coverage of query (100 bits)
Build an alignment for 206067 and 28 homologs with ≥ 30% identity
Or download the sequences
3c4jA Abc protein artp in complex with atp-gamma-s
29% identity, 83% coverage of query (99.4 bits)
3c41J / D0VWX4 Abc protein artp in complex with amp-pnp/mg2+
29% identity, 83% coverage of query (99.4 bits)
2olkA Abc protein artp in complex with adp-beta-s
29% identity, 83% coverage of query (99.4 bits)
2oljA Abc protein artp in complex with adp/mg2+
29% identity, 83% coverage of query (99.4 bits)
4ymuJ / Q8RCC2 Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
27% identity, 83% coverage of query (96.3 bits)
1ji0A / Q9X0M3 Crystal structure analysis of the abc transporter from thermotoga maritima
27% identity, 86% coverage of query (96.3 bits)
6mjpA / O30650 Lptb(e163q)fgc from vibrio cholerae (see paper)
25% identity, 86% coverage of query (92.4 bits)
2pclA / O66646 Crystal structure of abc transporter with complex (aq_297) from aquifex aeolicus vf5
34% identity, 77% coverage of query (89.4 bits)
5x40A / O68106 Structure of a cbio dimer bound with amppcp (see paper)
34% identity, 79% coverage of query (89.4 bits)
6b89A E. Coli lptb in complex with adp and novobiocin
27% identity, 86% coverage of query (87.8 bits)
4p31A Crystal structure of a selenomethionine derivative of e. Coli lptb in complex with adp-magensium
27% identity, 86% coverage of query (87.8 bits)
6b8bA E. Coli lptb in complex with adp and a novobiocin derivative
27% identity, 86% coverage of query (87.8 bits)
6mhzA Vanadate trapped cryo-em structure of e.Coli lptb2fg transporter
27% identity, 86% coverage of query (87.8 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)
32% identity, 79% coverage of query (87.4 bits)
6s8nB Cryo-em structure of lptb2fgc in complex with lipopolysaccharide
27% identity, 86% coverage of query (87.4 bits)
6s8gA Cryo-em structure of lptb2fgc in complex with amp-pnp
27% identity, 86% coverage of query (87.4 bits)
6mbnA / P0A9V1 Lptb e163q in complex with atp (see paper)
27% identity, 86% coverage of query (86.3 bits)
5ws4A / A0A0D8G707 Crystal structure of tripartite-type abc transporter macb from acinetobacter baumannii (see paper)
31% identity, 80% coverage of query (86.3 bits)
1f3oA / Q58206 Crystal structure of mj0796 atp-binding cassette (see paper)
30% identity, 79% coverage of query (83.6 bits)
8g4cB / O34697 Bceabs atpgs high res tm (see paper)
27% identity, 79% coverage of query (83.6 bits)
6tejB / A0A100XE85 Structure of apo irtab devoid sid in complex with sybody syb_nl5 (see paper)
32% identity, 83% coverage of query (83.6 bits)
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette
29% identity, 79% coverage of query (82.0 bits)
8j5qD / P9WQJ5 Cryo-em structure of mycobacterium tuberculosis oppabcd in the pre- translocation state (see paper)
32% identity, 79% coverage of query (82.0 bits)
7tchB Bceab e169q variant atp-bound conformation
26% identity, 79% coverage of query (82.0 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)
28% identity, 79% coverage of query (81.6 bits)
TGD3_ARATH / Q9AT00 Protein TRIGALACTOSYLDIACYLGLYCEROL 3, chloroplastic; ABC transporter I family member 13; ABC transporter ABCI.13; AtABCI13; Non-intrinsic ABC protein 11; AtNAP11 from Arabidopsis thaliana (Mouse-ear cress) (see 6 papers)
TC 3.A.1.27.2 / Q9AT00 Tdg3, component of The chloroplast lipid (trigalactosyl diacyl glycerol (TDG)) transporter, Tdg1,2,3 (Lu et al., 2007). Lipids such as mono- and digalactolipids are synthesized in the endoplasmic reticulum (ER) of plant cells and transferred to the thylakoid membranes of chloroplasts. Mutations in an outer chloroplastic envelope protein with 350 aas and 7 putative TMSs in the last 250 residues may catalyze translocation as part of a lipid transfer complex from Arabidopsis thaliana (Mouse-ear cress) (see 7 papers)
28% identity, 83% coverage of query (81.3 bits)
5xu1B / Q8DQF8 Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
27% identity, 79% coverage of query (80.9 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)
28% identity, 82% coverage of query (80.9 bits)
8j5tD Cryo-em structure of mycobacterium tuberculosis oppabcd in the catalytic intermediate state
31% identity, 79% coverage of query (80.5 bits)
8j5sD Cryo-em structure of mycobacterium tuberculosis oppabcd in the pre- catalytic intermediate state
31% identity, 79% coverage of query (80.5 bits)
6cvlD / P30750 Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
28% identity, 82% coverage of query (79.7 bits)
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form
28% identity, 82% coverage of query (79.3 bits)
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form
28% identity, 82% coverage of query (79.3 bits)
Q8TTZ3 ABC-type molybdate transporter (EC 7.3.2.5) from Methanosarcina acetivorans (see paper)
3d31A / Q8TTZ3 Modbc from methanosarcina acetivorans (see paper)
27% identity, 84% coverage of query (78.2 bits)
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter
23% identity, 83% coverage of query (77.4 bits)
1g6hA / Q58663 Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
23% identity, 83% coverage of query (77.0 bits)
4f4cA / P34712 The crystal structure of the multi-drug transporter (see paper)
26% identity, 80% coverage of query (76.6 bits)
7vfiA Cryo-em structure of the mouse tapl (9mer-peptide bound)
31% identity, 81% coverage of query (76.3 bits)
7v5cA / Q9JJ59 Cryo-em structure of the mouse abcb9 (adp.Bef3-bound) (see paper)
31% identity, 81% coverage of query (76.3 bits)
5lilA / Q2EHL8 Structure of aggregatibacter actinomycetemcomitans macb bound to atpys (p21) (see paper)
27% identity, 83% coverage of query (76.3 bits)
5lj7A / Q2EHL8 Structure of aggregatibacter actinomycetemcomitans macb bound to atp (p21) (see paper)
27% identity, 83% coverage of query (76.3 bits)
ECFA2_STRT2 / Q5M244 Energy-coupling factor transporter ATP-binding protein EcfA2; ECF transporter A component EcfA2; EC 3.6.3.- from Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) (see paper)
TC 3.A.1.25.6 / Q5M244 Energy-coupling factor transporter ATP-binding protein EcfA 1, component of Riboflavin ECF transport system, EcfAA'T/RibU from Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
29% identity, 79% coverage of query (75.9 bits)
ABCB9_HUMAN / Q9NP78 ABC-type oligopeptide transporter ABCB9; ATP-binding cassette sub-family B member 9; ATP-binding cassette transporter 9; ABC transporter 9 protein; hABCB9; TAP-like protein; TAPL; EC 7.4.2.6 from Homo sapiens (Human) (see 16 papers)
Q9NP78 bacterial ABC-type protein transporter (EC 7.4.2.5) from Homo sapiens (see 2 papers)
TC 3.A.1.209.2 / Q9NP78 Homodimeric transporter ABCB9 or TAPL. Transports a broad spectrum of peptides (low affinity) from the cytosol to the lysosomal lumen. It exists in two forms (812 aas and 1257 aas). The latter full length protein confers resistance to taxanes and anthracyclines (Kawanobe et al., 2012). Resistance and transport were demonstrated for paclitaxel and docetaxel. TapL transports a broad range of peptides of 6-60aas (23aas optimal). It has also been detected in the ER. It is stabilized by interaction with LAMP-1 and LAMP-2 (see 9.A.16) from Homo sapiens (see 18 papers)
30% identity, 81% coverage of query (75.9 bits)
8wm7D / Q8YZ75 Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
31% identity, 77% coverage of query (75.9 bits)
8f5bA / P78363 Human abca4 structure in complex with amp-pnp
28% identity, 74% coverage of query (75.1 bits)
7m1qA / P78363 Human abca4 structure in complex with n-ret-pe (see paper)
28% identity, 74% coverage of query (75.1 bits)
7lkpA Structure of atp-free human abca4
28% identity, 74% coverage of query (75.1 bits)
7e7oA / P78363 Cryo-em structure of human abca4 in nrpe-bound state (see paper)
28% identity, 74% coverage of query (75.1 bits)
ABCA4_HUMAN / P78363 Retinal-specific phospholipid-transporting ATPase ABCA4; ATP-binding cassette sub-family A member 4; RIM ABC transporter; RIM proteinv; RmP; Retinal-specific ATP-binding cassette transporter; Stargardt disease protein; EC 7.6.2.1 from Homo sapiens (Human) (see 38 papers)
TC 3.A.1.211.2 / P78363 The retinal-specific ABC transporter (RIM protein, ABCR or ABCA4) (Stargardt's disease protein, involved in retinal/macular degeneration) in the rod outer segment. Changes in the oligomeric state of the nucleotide binding domains of ABCR are coupled to ATP hydrolysis and might represent a signal for the TMDs of ABCR to export the bound substrate (Biswas-Fiss 2006). The ABCA4 porter flips N-retinylidene-phosphatidylethanolamine, a product generated from the photobleaching of rhodopsin, from the lumen to the cytoplasmic side of disc membranes following the photobleaching of rhodopsin, insuring that retinoids do not accumulate in disc membranes (Molday, 2007; Molday et al. 2009; Tsybovsky et al. 2013). It also transports several vitamin A derivatives (Sun, 2011) and phosphatidylethanolamine in the same direction. Mutations, known to cause Stargardt disease, decrease N-retinylidene-phosphatidylethanolamine and phosphatidylethanolamine transport activities (Quazi et al. 2012). It functions as an inwardly directed retinoid flippase in the visual cycle from Homo sapiens (Human) (see 28 papers)
28% identity, 74% coverage of query (75.1 bits)
8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp
30% identity, 77% coverage of query (74.7 bits)
4hluC / Q9X1Z1 Structure of the ecfa-a' heterodimer bound to adp (see paper)
32% identity, 72% coverage of query (74.7 bits)
7zdkC If(apo/asym) conformation of cyddc in amp-pnp(cydc)/amp-pnp(cydd) bound state (dataset-8)
28% identity, 79% coverage of query (73.9 bits)
7zdfC If(heme/confined) conformation of cyddc in amp-pnp(cydd) bound state (dataset-4)
28% identity, 79% coverage of query (73.9 bits)
7zdaC If(apo/asym) conformation of cyddc in adp+pi(cydc)/atp(cydd) bound state (dataset-2)
28% identity, 79% coverage of query (73.9 bits)
8ipsA / P23886 Cryo-em structure of heme transporter cyddc from escherichia coli in the inward facing heme loading state (see paper)
28% identity, 79% coverage of query (73.9 bits)
2ixfA / P36370 Crystal structure of the atpase domain of tap1 with atp (d645q, q678h mutant) (see paper)
29% identity, 81% coverage of query (73.6 bits)
7lkzA Structure of atp-bound human abca4
27% identity, 74% coverage of query (73.6 bits)
7e7qA / P78363 Cryo-em structure of human abca4 in atp-bound state (see paper)
27% identity, 74% coverage of query (73.6 bits)
4hluA / Q9WY65 Structure of the ecfa-a' heterodimer bound to adp (see paper)
28% identity, 76% coverage of query (73.6 bits)
MRP8_HUMAN / Q96J66 ATP-binding cassette sub-family C member 11; Multidrug resistance-associated protein 8; EC 7.6.2.2; EC 7.6.2.3 from Homo sapiens (Human) (see 10 papers)
TC 3.A.1.208.13 / Q96J66 Cyclic nucleotide (cAMP and cGMP) efflux pump, MRP8 (ABCC11); also exports other nucleoside and nucleotide analogues, and confers resistance to fluoropyrimidines and the anti-AIDS drug, 2',3'-dideoxycytidine (Guo et al., 2003). Human earwax consists of wet and dry types. Dry earwax is frequent in East Asians, whereas wet earwax is common in other populations. A SNP, 538G --> A (rs17822931), in the ABCC11 gene is responsible for determination of earwax type. Cells with allele A show a lower excretory activity for cGMP than those with allele G. The 538G --> A SNP is the first example of DNA polymorphism determining a visible genetic trait (see 6 papers)
28% identity, 76% coverage of query (73.6 bits)
3fvqB / Q5FA19 Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
32% identity, 78% coverage of query (73.2 bits)
MALK_SALTY / P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
30% identity, 79% coverage of query (73.2 bits)
1jj7A / Q03518 Crystal structure of thE C-terminal atpase domain of human tap1 (see paper)
28% identity, 79% coverage of query (72.8 bits)
7zdtC Occ(apo/return) conformation of cyddc mutant (e500q.C) in atp(cydc) bound state (dataset-18)
27% identity, 79% coverage of query (72.8 bits)
6z67B Ftse structure of streptococcus pneumoniae in complex with amppnp at 2.4 a resolution
25% identity, 80% coverage of query (72.4 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)
28% identity, 79% coverage of query (72.4 bits)
FTSE_STRP2 / A0A0H2ZM82 Cell division ATP-binding protein FtsE from Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) (see 3 papers)
FTSE_STRR6 / Q8DQH4 Cell division ATP-binding protein FtsE from Streptococcus pneumoniae (strain ATCC BAA-255 / R6) (see paper)
6z4wA / Q8DQH4 Ftse structure from streptococcus pneumoniae in complex with adp (space group p 1) (see paper)
25% identity, 80% coverage of query (72.4 bits)
ABCAD_MOUSE / Q5SSE9 ATP-binding cassette sub-family A member 13; EC 7.6.2.- from Mus musculus (Mouse) (see 3 papers)
31% identity, 77% coverage of query (72.4 bits)
4zirA Crystal structure of ecfaa' heterodimer bound to amppnp
28% identity, 76% coverage of query (72.0 bits)
4yerA / Q9X1C3 Crystal structure of an abc transporter atp-binding protein (tm_1403) from thermotoga maritima msb8 at 2.35 a resolution
25% identity, 76% coverage of query (72.0 bits)
FtsE / b3463 cell division protein FtsE from Escherichia coli K-12 substr. MG1655 (see 9 papers)
FTSE_ECOLI / P0A9R7 Cell division ATP-binding protein FtsE from Escherichia coli (strain K12) (see 4 papers)
ftsE cell division ATP-binding protein ftsE from Escherichia coli K12 (see 3 papers)
30% identity, 73% coverage of query (72.0 bits)
8w6iD / P0A9R7 Cryo-em structure of escherichia coli str k12 ftsex complex with atp- gamma-s in peptidisc
30% identity, 73% coverage of query (72.0 bits)
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Lawrence Berkeley National Laboratory