|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-213 |
6.03e-83 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 249.21 E-value: 6.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEI 81
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQEPALYPDLTVRENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 TRRLRFIKDPST---VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRD 158
Cdd:COG1131 97 FARLYGLPRKEArerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032538500 159 LAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDakkLHQLRNRTL---FIDL 213
Cdd:COG1131 177 LA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT---PDELKARLLedvFLEL 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-196 |
7.74e-75 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 227.49 E-value: 7.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGcHELWNSVGYLVEIPYSYPELTVWENLEITR 83
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGALIEAPGFYPNLTARENLRLLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 84 RLRFIKDpSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAfNK 163
Cdd:cd03268 98 RLLGIRK-KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLR-DQ 175
|
170 180 190
....*....|....*....|....*....|...
gi 2032538500 164 GVTIFISSHLLGEISRIATRIGIIHEGKLIQEM 196
Cdd:cd03268 176 GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-192 |
1.42e-63 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 197.62 E-value: 1.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEi 81
Cdd:cd03230 17 DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEEPSLYENLTVRENLK- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 trrlrfikdpstvdsiieklkltpykdrkaknLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAf 161
Cdd:cd03230 96 --------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELK- 142
|
170 180 190
....*....|....*....|....*....|.
gi 2032538500 162 NKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:cd03230 143 KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-215 |
1.77e-58 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 186.99 E-value: 1.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEI 81
Cdd:COG4555 18 KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDERGLYDRLTVRENIRY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 TRRLRFIKD---PSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRD 158
Cdd:COG4555 98 FAELYGLFDeelKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 159 LAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIqemDAKKLHQLRNRTLFIDLED 215
Cdd:COG4555 178 LK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVV---AQGSLDELREEIGEENLED 230
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1-195 |
1.24e-57 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 184.14 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGeiiHAGCHELWNSVGYLVEIPYSYPELTVWENLE 80
Cdd:TIGR03740 16 VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG---HPWTRKDLHKIGSLIESPPLYENLTARENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFIKDpSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLA 160
Cdd:TIGR03740 93 VHTTLLGLPD-SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQELRELIRSFP 171
|
170 180 190
....*....|....*....|....*....|....*
gi 2032538500 161 fNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:TIGR03740 172 -EQGITVILSSHILSEVQQLADHIGIISEGVLGYQ 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-265 |
3.06e-54 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 177.61 E-value: 3.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHagcHELWNSVGYLVEIPYSYPELTVWENL-- 79
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYLPEERGLYPKMKVGEQLvy 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 ----------EITRRLrfikdpstvDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGI 149
Cdd:COG4152 95 larlkglskaEAKRRA---------DEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 150 VEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL-HQLRNRTLFIDLEdkkGAQSLLANEGF 228
Cdd:COG4152 166 ELLKDVIRELA-AKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIrRQFGRNTLRLEAD---GDAGWLRALPG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2032538500 229 DSTITEEG---LIEITSEKAlihPEDVNSNLVKAG----FS---PSM 265
Cdd:COG4152 242 VTVVEEDGdgaELKLEDGAD---AQELLRALLARGpvreFEevrPSL 285
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-193 |
3.25e-51 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 167.68 E-value: 3.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYlveIPYS---YPELTVWEN 78
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY---CPQFdalFDELTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEITRRLRFI---KDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:cd03263 96 LRFYARLKGLpksEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 2032538500 156 LRDLAfnKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:cd03263 176 ILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-193 |
1.55e-48 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 160.52 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchELWNSVGYLVEIPYSYPELTVWENLE 80
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYLPEERGLYPKMKVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFIKDP---STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLR 157
Cdd:cd03269 93 YLAQLKGLKKEearRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIR 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 2032538500 158 DLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:cd03269 173 ELA-RAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-195 |
1.96e-48 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 160.61 E-value: 1.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEI 81
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDDELTGWENLYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 TRRLRFIKDP---STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRD 158
Cdd:cd03265 97 HARLYGVPGAerrERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEK 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 2032538500 159 LAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:cd03265 177 LKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-195 |
8.42e-46 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 153.50 E-value: 8.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGeIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEIT 82
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFGVYPNFTVREFLDYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 RRLRFIKD---PSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDL 159
Cdd:cd03264 97 AWLKGIPSkevKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 2032538500 160 AFNKgvTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:cd03264 177 GEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-195 |
1.39e-45 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 152.91 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLE 80
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFIKDP---STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLR 157
Cdd:cd03266 101 YFAGLYGLKGDeltARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 2032538500 158 DLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:cd03266 181 QLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-191 |
1.94e-45 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 163.76 E-value: 1.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLveipyS-----YPELTVWEN 78
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYM-----SqafslYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEITRRLRFIKD---PSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGiveiR-- 153
Cdd:NF033858 360 LELHARLFHLPAaeiAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA----Rdm 435
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2032538500 154 --ELLRDLAFNKGVTIFISSHLLGEISRiATRIGIIHEGK 191
Cdd:NF033858 436 fwRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGR 474
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
3-280 |
3.13e-44 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 152.24 E-value: 3.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEIT 82
Cdd:TIGR03522 20 EVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIGYLPEHNPLYLDMYVREYLQFI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 RRLRFIKDP---STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDL 159
Cdd:TIGR03522 100 AGIYGMKGQllkQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTTGLDPNQLVEIRNVIKNI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 160 AFNKgvTIFISSHLLGEISRIATRIGIIHEGKLIQEmdaKKLHQLR--NRTLFIDLEDKKGAQSLLANEgFDSTITEEGL 237
Cdd:TIGR03522 180 GKDK--TIILSTHIMQEVEAICDRVIIINKGKIVAD---KKLDELSaaNKKQVIEVEFEEQIDLQLFET-LEEISSVKNT 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2032538500 238 IEITSEKALIHPEDVNSNLVKA----GFSPSMLKVEEEELESYFLRI 280
Cdd:TIGR03522 254 GGNTWKLTFETPNDTRPEIFKLaqqkGLKLISLQQNEKNLEQVFREI 300
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
4-281 |
4.50e-44 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 151.77 E-value: 4.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEITR 83
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGRENLEMMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 84 RL----RFIKDpSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDL 159
Cdd:TIGR01188 92 RLyglpKDEAE-ERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 160 AfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL-HQLRNRTLFI---DLEDKKGAQSLLANEgFDSTITEE 235
Cdd:TIGR01188 171 K-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELkRRLGKDTLESrprDIQSLKVEVSMLIAE-LGETGLGL 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 236 GLIEITSEKALIH--------PEDVNSnLVKAGFSPSMLKVEEEELESYFLRII 281
Cdd:TIGR01188 249 LAVTVDSDRIKILvpdgdetvPEIVEA-AIRNGIRIRSISTERPSLDDVFLKLT 301
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-193 |
2.28e-42 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 145.17 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNSVGYLveipYSYPEL-----TV 75
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKdITKKNLRELRRKVGLV----FQNPDDqlfapTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WE-------NL-----EITRRlrfikdpstVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:COG1122 94 EEdvafgpeNLglpreEIRER---------VEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2032538500 144 LDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:COG1122 165 LDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-205 |
2.69e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.23 E-value: 2.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGchelWNSVGYL---VEIPYSYPeLTVWE--N 78
Cdd:COG1121 25 VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYVpqrAEVDWDFP-ITVRDvvL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEITRRLRFIKDPST-----VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:COG1121 100 MGRYGRRGLFRRPSRadreaVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALY 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 154 ELLRDLAfNKGVTIFISSHLLGEISRIATRI-----GIIHEGKLIQEMDAKKLHQLR 205
Cdd:COG1121 180 ELLRELR-REGKTILVVTHDLGAVREYFDRVlllnrGLVAHGPPEEVLTPENLSRAY 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-172 |
2.26e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 139.15 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEI 81
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 TRRLR-FIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLA 160
Cdd:COG4133 99 WAALYgLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHL 178
|
170
....*....|..
gi 2032538500 161 fNKGVTIFISSH 172
Cdd:COG4133 179 -ARGGAVLLTTH 189
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-191 |
1.37e-39 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 136.16 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAG---CHELWNSVGYLVEIPYSYPELTVWE 77
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedeLPPLRRRIGMVFQDFALFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITrrlrfikdpstvdsiieklkltpykdrkaknLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLR 157
Cdd:cd03229 96 NIALG-------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
|
170 180 190
....*....|....*....|....*....|....
gi 2032538500 158 DLAFNKGVTIFISSHLLGEISRIATRIGIIHEGK 191
Cdd:cd03229 145 SLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-195 |
6.00e-39 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 136.41 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNS-VGYLVEIPYSYPELTVWENL 79
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdITGLPPHEIARLgIGRTFQIPRLFPELTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRRLR------FIKDPST-------VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDP 146
Cdd:cd03219 97 MVAAQARtgsgllLARARREerearerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2032538500 147 AGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:cd03219 177 EETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-191 |
8.41e-39 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 135.29 E-value: 8.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGC-HELWNSVGYLveipYSYPE-----LTV 75
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlKELRRKVGLV----FQNPDdqffgPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WE-------NL-----EITRRlrfikdpstVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:cd03225 94 EEevafgleNLglpeeEIEER---------VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2032538500 144 LDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGK 191
Cdd:cd03225 165 LDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1-193 |
8.98e-39 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 135.92 E-value: 8.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchelwNSVGYLVEIPYSYPELT-VWENL 79
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK------RRKKFLRRIGVVFGQKTqLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRRLRFIK-----DPS----TVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIV 150
Cdd:cd03267 111 PVIDSFYLLAaiydlPPArfkkRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032538500 151 EIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-222 |
1.11e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 137.91 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchelwNSVGYLVEIpyS---------YPE 72
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK------RRKEFARRI--GvvfgqrsqlWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 LTVWENLEITRRLRFIKDP---STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGI 149
Cdd:COG4586 111 LPAIDSFRLLKAIYRIPDAeykKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032538500 150 VEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIqeMDaKKLHQLRN-----RTLFIDLEDKKGAQSL 222
Cdd:COG4586 191 EAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII--YD-GSLEELKErfgpyKTIVLELAEPVPPLEL 265
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-194 |
1.59e-38 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 134.57 E-value: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNsVGYLVEIPYSYPELTVWENLEI 81
Cdd:cd03259 17 DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN-IGMVFQDYALFPHLTVAENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 TRRLRFIKDPST---VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRD 158
Cdd:cd03259 96 GLKLRGVPKAEIrarVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 2032538500 159 LAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:cd03259 176 LQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-184 |
2.66e-38 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 133.81 E-value: 2.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHagchELWNSVGYL---VEIPYSYPeLTVWE 77
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----KERKRIGYVpqrRSIDRDFP-ISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITR--RLRFIKDPST-----VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIV 150
Cdd:cd03235 90 VVLMGLygHKGLFRRLSKadkakVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE 169
|
170 180 190
....*....|....*....|....*....|....
gi 2032538500 151 EIRELLRDLAfNKGVTIFISSHLLGEISRIATRI 184
Cdd:cd03235 170 DIYELLRELR-REGMTILVVTHDLGLVLEYFDRV 202
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-193 |
9.32e-38 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 133.63 E-value: 9.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHELWNSVGYLVEIPYSYPELTVWENLE 80
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVPQEPPAPFGLTVRELVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRR--LRFIKDPST-----VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:COG1120 98 LGRYphLGLFGRPSAedreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2032538500 154 ELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:COG1120 178 ELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-195 |
1.38e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 132.24 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEITR 83
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDNLDPDFTVRENLLVFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 84 R---LRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLa 160
Cdd:PRK13537 106 RyfgLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL- 184
|
170 180 190
....*....|....*....|....*....|....*
gi 2032538500 161 FNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:PRK13537 185 LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-192 |
1.50e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.17 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNS-VGYLVEIPYSYPElTVWENLEIT 82
Cdd:COG4619 19 VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRqVAYVPQEPALWGG-TVRDNLPFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 RRLRFIK-DPSTVDSIIEKLKLTP-YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDP--AGIVEirELLRD 158
Cdd:COG4619 98 FQLRERKfDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPenTRRVE--ELLRE 175
|
170 180 190
....*....|....*....|....*....|....
gi 2032538500 159 LAFNKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:COG4619 176 YLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-195 |
3.75e-36 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 128.81 E-value: 3.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHE---LwnSVGYLVEIPYSYPELTVWE 77
Cdd:cd03218 17 NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQdITKLPMHKrarL--GIGYLPQEASIFRKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITrrLRFIKDPST-----VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEI 152
Cdd:cd03218 95 NILAV--LEIRGLSKKereekLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032538500 153 RELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:cd03218 173 QKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-195 |
3.88e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 127.17 E-value: 3.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchelwnsvgylveipysypeltvWENLEI 81
Cdd:cd03214 16 DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS------------------------LSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 TRRLrfikdpSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAF 161
Cdd:cd03214 72 ARKI------AYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLAR 145
|
170 180 190
....*....|....*....|....*....|....
gi 2032538500 162 NKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:cd03214 146 ERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-193 |
6.76e-36 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 129.00 E-value: 6.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE---------IIHAGchelwnsvgyLV---EIPYSYP 71
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphrIARLG----------IArtfQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 72 ELTVWENLEITRRLR--------FIKDPST----------VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPE 133
Cdd:COG0411 93 ELTVLENVLVAAHARlgrgllaaLLRLPRArreerearerAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 134 ILILDEPSNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-193 |
9.18e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 133.88 E-value: 9.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCH----ELWNSVGYLVEIPYSY--PELTV 75
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslrELRRRVQMVFQDPYSSlnPRMTV 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WEnlEITRRLRFIKDPST------VDSIIEKLKLTP-YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAG 148
Cdd:COG1123 362 GD--IIAEPLRLHGLLSRaerrerVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSV 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032538500 149 IVEIRELLRDLAFNKGVT-IFIsSHLLGEISRIATRIGIIHEGKLI 193
Cdd:COG1123 440 QAQILNLLRDLQRELGLTyLFI-SHDLAVVRYIADRVAVMYDGRIV 484
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-201 |
1.53e-35 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 127.78 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNS-VGYLVEIPYSYPELTVWEN- 78
Cdd:TIGR04406 18 NDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdITHLPMHERARLgIGYLPQEASIFRKLTVEENi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 ---LEITRRLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:TIGR04406 98 mavLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032538500 156 LRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:TIGR04406 178 IKHLK-ERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-201 |
9.13e-34 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 122.67 E-value: 9.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIK-----PTTGESYLKGEIIHAGCH---ELWNSVGYLVEIPYSYPeL 73
Cdd:cd03260 17 KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVdvlELRRRVGMVFQKPNPFP-G 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWENLEITRRLRFIKDPSTVDSIIEK-LK---LTPY-KDR-KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPA 147
Cdd:cd03260 96 SIYDNVAYGLRLHGIKLKEELDERVEEaLRkaaLWDEvKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 148 GIVEIRELLRDLAfnKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:cd03260 176 STAKIEELIAELK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-195 |
9.72e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.83 E-value: 9.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA---------GchelwnsVGYLveipysyP- 71
Cdd:COG1137 20 KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhkrarlG-------IGYL-------Pq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 72 ------ELTVWEN----LEIT------RRLRfikdpstVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEIL 135
Cdd:COG1137 86 easifrKLTVEDNilavLELRklskkeREER-------LEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 136 ILDEPSNGLDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLK-ERGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
2-142 |
1.34e-33 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 119.67 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWN-SVGYLVEIPYSYPELTVWENLE 80
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032538500 81 ITRRLRFIKDP---STVDSIIEKLKLTPYKDRKA----KNLSLGNSQRLGLAKALIHNPEILILDEPSN 142
Cdd:pfam00005 82 LGLLLKGLSKRekdARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-192 |
1.92e-33 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 121.44 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELW----NSVGYlveIPYSY---PEL 73
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtDISKLSEKELAafrrRHIGF---VFQSFnllPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWENLEITrrLRFIKDPST-----VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAG 148
Cdd:cd03255 98 TALENVELP--LLLAGVPKKerrerAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSET 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2032538500 149 IVEIRELLRDLAFNKGVTIFISSHLLgEISRIATRIGIIHEGKL 192
Cdd:cd03255 176 GKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1-193 |
2.75e-33 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 121.45 E-value: 2.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIH----AGCHELWNSVGYLVEIPYSYPELTVW 76
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMGMLFQSGALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRFIKDPSTVDSII-EKLK---LTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEI 152
Cdd:cd03261 96 ENVAFPLREHTRLSEEEIREIVlEKLEavgLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2032538500 153 RELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:cd03261 176 DDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-201 |
3.72e-33 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 121.00 E-value: 3.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNS-VGYLVEIPYSYPELTVWENLEI 81
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRdITGLPPHERARAgIGYVPEGRRIFPELTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 TRRLRfikDPSTVDSIIEKL-----KLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELL 156
Cdd:cd03224 99 GAYAR---RRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2032538500 157 RDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:cd03224 176 RELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-191 |
6.43e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 118.12 E-value: 6.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELW-NSVGYLVEipysypeltvwenle 80
Cdd:cd00267 16 DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELrRRIGYVPQ--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 itrrlrfikdpstvdsiieklkltpykdrkaknLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLA 160
Cdd:cd00267 81 ---------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA 127
|
170 180 190
....*....|....*....|....*....|.
gi 2032538500 161 fNKGVTIFISSHLLGEISRIATRIGIIHEGK 191
Cdd:cd00267 128 -EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-194 |
1.07e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 120.13 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNsVGYLVEIPYSYPELTVWENLE 80
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-ISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFI---KDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLR 157
Cdd:cd03299 94 YGLKKRKVdkkEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 2032538500 158 DLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2-193 |
1.08e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 119.28 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGchELWNSVGYLVEIPYSYP-ELTVWEnlE 80
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGYVMQDVDYQLfTDSVRE--E 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFI-KDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDL 159
Cdd:cd03226 93 LLLGLKELdAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL 172
|
170 180 190
....*....|....*....|....*....|....
gi 2032538500 160 AfNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:cd03226 173 A-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-201 |
3.42e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 118.55 E-value: 3.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE---------IIHAGchelwnsVGYLVE---Ipys 69
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphrIARLG-------IGYVPEgrrI--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 70 YPELTVWENLEITRRLRfiKDPSTVDSIIEKL-----KLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGL 144
Cdd:COG0410 90 FPSLTVEENLLLGAYAR--RDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 145 DPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:COG0410 168 APLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-195 |
5.43e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 120.71 E-value: 5.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEIT 82
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 RR---LRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDL 159
Cdd:PRK13536 139 GRyfgMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSL 218
|
170 180 190
....*....|....*....|....*....|....*.
gi 2032538500 160 aFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:PRK13536 219 -LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-203 |
5.49e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.20 E-value: 5.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIH---------AGchelwnsVGYLveipysyPE 72
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdairAG-------IAYV-------PE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 ----------LTVWENLEIT-----RRLRFIKDP---STVDSIIEKLKL-TPYKDRKAKNLSLGNSQRLGLAKALIHNPE 133
Cdd:COG1129 335 drkgeglvldLSIRENITLAsldrlSRGGLLDRRrerALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 134 ILILDEPSNGLDPAGIVEIRELLRDLAfNKGVTI-FISSHlLGEISRIATRIGIIHEGKLIQEMDAKKLHQ 203
Cdd:COG1129 415 VLILDEPTRGIDVGAKAEIYRLIRELA-AEGKAViVISSE-LPELLGLSDRILVMREGRIVGELDREEATE 483
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-195 |
6.17e-32 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 118.16 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHaGCHE------------------LWNSvgylve 65
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDIT-GLSEkelyelrrrigmlfqggaLFDS------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 66 ipysypeLTVWENLEITRRLRFIKDPSTVDSII-EKLK---LTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPS 141
Cdd:COG1127 97 -------LTVFENVAFPLREHTDLSEAEIRELVlEKLElvgLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 142 NGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:COG1127 170 AGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-195 |
1.75e-31 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 116.84 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHEL----WNSVGYLVEIPYSY--PELTV 75
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirRKEIQMVFQDPMSSlnPRMTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLEITRRLRFIKDPSTVDSIIEKLKL------TPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGI 149
Cdd:cd03257 102 GEQIAEPLRIHGKLSKKEARKEAVLLLLvgvglpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032538500 150 VEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:cd03257 182 AQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-193 |
1.82e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 117.94 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAG----CHELWNSVGYLveipYSYPE----- 72
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkkkLKDLRKKVGLV----FQFPEhqlfe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 LTVWE-------NL-----EITRRlrfikdpstVDSIIEKLKLTP-YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDE 139
Cdd:TIGR04521 98 ETVYKdiafgpkNLglseeEAEER---------VKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 140 PSNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:TIGR04521 169 PTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-194 |
2.14e-31 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 117.36 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHE------------LWNSVGYLveipys 69
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrrkkismVFQSFALL------ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 70 yPELTVWEN----LEI------TRRLRFIKdpstvdsIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDE 139
Cdd:cd03294 115 -PHRTVLENvafgLEVqgvpraEREERAAE-------ALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032538500 140 PSNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-194 |
2.31e-31 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 116.63 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHELWNSVGYLVEIPYSYPELTVWENLE 80
Cdd:cd03295 18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYVIQQIGLFPHMTVEENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFIKDP---STVDSIIEKLKLTP--YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:cd03295 98 LVPKLLKWPKEkirERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEE 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 2032538500 156 LRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:cd03295 178 FKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
5-194 |
2.65e-31 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 115.86 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 5 SLNVD---KGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNS-----VGYLVEIPYSYPELTVW 76
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqqrkIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEI-TRRLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:cd03297 94 ENLAFgLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2032538500 156 LRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-194 |
4.57e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.94 E-value: 4.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIhagchelwNSV------------GYLVeipys 69
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--------TDLppkdrniamvfqSYAL----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 70 YPELTVWENL------------EITRRlrfikdpstVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILIL 137
Cdd:COG3839 87 YPHMTVYENIafplklrkvpkaEIDRR---------VREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 138 DEP-SNgLDPAG----IVEIRELLRDLafnkGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:COG3839 158 DEPlSN-LDAKLrvemRAEIKRLHRRL----GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQ 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-199 |
4.79e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 4.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEI---------IHAGchelwnsVGY------LVei 66
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrirsprdaIALG-------IGMvhqhfmLV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 67 pysyPELTVWENL----EITRRLRFikDPSTVDSIIEK------LKLTPykDRKAKNLSLGNSQRLGLAKALIHNPEILI 136
Cdd:COG3845 93 ----PNLTVAENIvlglEPTKGGRL--DRKAARARIRElserygLDVDP--DAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032538500 137 LDEPSNGLDPAgivEIREL---LRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAK 199
Cdd:COG3845 165 LDEPTAVLTPQ---EADELfeiLRRLA-AEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-195 |
1.07e-29 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 112.29 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII----HAGCHELWNSVGYLVEIPYSYPELTVWE 77
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKARRRIGMIFQHFNLLSSRTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 N----LEITRrLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:cd03258 102 NvalpLEIAG-VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032538500 154 ELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:cd03258 181 ALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-204 |
2.11e-29 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 111.51 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNS----VGYLVEIPYSYPELTVWE 77
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqIGMIFQQFNLIERLSVLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLeITRRLRFIkdpSTVDSI---------------IEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSN 142
Cdd:cd03256 98 NV-LSGRLGRR---STWRSLfglfpkeekqralaaLERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 143 GLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI-----QEMDAKKLHQL 204
Cdd:cd03256 174 SLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVfdgppAELTDEVLDEI 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2-193 |
2.23e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.91 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYgFL-GLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHagchELWNSvgylvEIPYsY---------- 70
Cdd:COG2884 19 SDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS----RLKRR-----EIPY-Lrrrigvvfqd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 71 ----PELTVWEN----LEIT-RRLRFIKdpSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPS 141
Cdd:COG2884 88 frllPDRTVYENvalpLRVTgKSRKEIR--RRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 142 NGLDPAGIVEIRELLRDlaFNK-GVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:COG2884 166 GNLDPETSWEIMELLEE--INRrGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-192 |
2.42e-29 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 109.83 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchelwNSVGYLVEIPYSY----------- 70
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR------RSPRDAIRAGIAYvpedrkreglv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 71 PELTVWENLEITRRLrfikdpstvdsiieklkltpykdrkaknlSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIV 150
Cdd:cd03215 91 LDLSVAENIALSSLL-----------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032538500 151 EIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:cd03215 142 EIYRLIRELA-DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-194 |
3.24e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 110.42 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIhagchelwNSVG------YLVEIPYS-YPELT 74
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV--------TDLPpkdrdiAMVFQNYAlYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENLEITRRLRFIKDPST---VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVE 151
Cdd:cd03301 89 VYDNIAFGLKLRKVPKDEIderVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032538500 152 IRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:cd03301 169 MRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-204 |
3.72e-29 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 110.92 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHEL--WNS-VGY------LVeipysyP 71
Cdd:COG3638 20 DDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqDVTALRGRALrrLRRrIGMifqqfnLV------P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 72 ELTVWENLEITR--RLRFIK---------DPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEP 140
Cdd:COG3638 94 RLSVLTNVLAGRlgRTSTWRsllglfppeDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032538500 141 SNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI-----QEMDAKKLHQL 204
Cdd:COG3638 174 VASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVfdgppAELTDAVLREI 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-201 |
5.84e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 114.73 E-value: 5.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIH---------AGCH----ELwNsvgyLVeipy 68
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprdaqaAGIAiihqEL-N----LV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 69 syPELTVWENL----EITRRlRFIKDPSTVD---SIIEKLKLT--PykDRKAKNLSLGNSQRLGLAKALIHNPEILILDE 139
Cdd:COG1129 92 --PNLSVAENIflgrEPRRG-GLIDWRAMRRrarELLARLGLDidP--DTPVGDLSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 140 PSNGLDPAGIVEIRELLRDLAfNKGVTI-FIsSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:COG1129 167 PTASLTEREVERLFRIIRRLK-AQGVAIiYI-SHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-197 |
1.83e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 108.33 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIhAGCHelwNSVGYLVEIPYSYPELTVWENLEITR 83
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-TGPG---PDRGYVFQQDALLPWLTVLDNVALGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 84 RLRFIKDP---STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLA 160
Cdd:cd03293 99 ELQGVPKAearERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIW 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 2032538500 161 FNKGVTIFISSHLLGEISRIATRIGII--HEGKLIQEMD 197
Cdd:cd03293 179 RETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-201 |
3.17e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 113.07 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPT---TGESYLKG-EIIHAGCHELWNSVGYLVEIP-YSYPELTVW 76
Cdd:COG1123 23 DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrDLLELSEALRGRRIGMVFQDPmTQLNPVTVG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRFIKD---PSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:COG1123 103 DQIAEALENLGLSRaeaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEIL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2032538500 154 ELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:COG1123 183 DLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1-194 |
1.53e-27 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 106.55 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHElwNSVGyLVEIPYS-YPELTVWEN 78
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHK--RPVN-TVFQNYAlFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEITRRLRFIKDPST---VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:cd03300 93 IAFGLRLKKLPKAEIkerVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLE 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 2032538500 156 LRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:cd03300 173 LKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ 211
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-195 |
2.39e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 106.35 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG---------EIIHAGchelwnsVGYLVEIPYSYPEL 73
Cdd:COG4674 28 DLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGtdltgldehEIARLG-------IGRKFQKPTVFEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWENLEI----TRR----LRFIKDPSTVDSIIEKLK---LTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSN 142
Cdd:COG4674 101 TVFENLELalkgDRGvfasLFARLTAEERDRIEEVLEtigLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 143 GLDPAGIVEIRELLRDLAfnKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:COG4674 181 GMTDAETERTAELLKSLA--GKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAE 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-200 |
2.66e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 107.24 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII---HAGCHELWNSVGYLVEIP-YSYPELTVW 76
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDPdNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEI-TRRLRFIKDP--STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:PRK13636 102 QDVSFgAVNLKLPEDEvrKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 154 ELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI-----QEMDAKK 200
Cdd:PRK13636 182 KLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVIlqgnpKEVFAEK 233
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1-172 |
3.20e-27 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 104.43 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII---HAGCHELWNSVGYLVEIPYS---YPelT 74
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDPDDqlfAA--D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWE-------NL-----EITRRlrfikdpstVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSN 142
Cdd:TIGR01166 86 VDQdvafgplNLglseaEVERR---------VREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|
gi 2032538500 143 GLDPAGIVEIRELLRDLAfNKGVTIFISSH 172
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLR-AEGMTVVISTH 185
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-204 |
2.40e-26 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 103.53 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWN---SVGYLVEIPYSYPELTVW 76
Cdd:TIGR02315 18 LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtDITKLRGKKLRKlrrRIGMIFQHYNLIERLTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITR--RLRFIK---------DPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:TIGR02315 98 ENVLHGRlgYKPTWRsllgrfseeDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 146 PAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI-----QEMDAKKLHQL 204
Cdd:TIGR02315 178 PKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVfdgapSELDDEVLRHI 241
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-193 |
2.49e-26 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 101.35 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHagchelwnsvgylveipysypeltvwenlei 81
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 trrlrfIKDPstvdsiieklkltpykdRKAKN--------LSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:cd03216 66 ------FASP-----------------RDARRagiamvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2032538500 154 ELLRDLAfNKGVT-IFIsSHLLGEISRIATRIGIIHEGKLI 193
Cdd:cd03216 123 KVIRRLR-AQGVAvIFI-SHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-206 |
1.28e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 101.37 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGEsylkgeiIhagcheLWNSVGYLVEIPYS------------Y 70
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGR-------I------LWNGQDLTALPPAErpvsmlfqennlF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 71 PELTVWEN--LEITRRLRF-IKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPA 147
Cdd:COG3840 84 PHLTVAQNigLGLRPGLKLtAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2032538500 148 GIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQLRN 206
Cdd:COG3840 164 LRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-201 |
1.65e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.11 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNS-VGYLVEIPYSY---PELTVW 76
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdITGLSPRERRRLgVAYIPEDRLGRglvPDMSVA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 EN--LEITRRLRFIK----DPSTV----DSIIEKLKL-TPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:COG3845 355 ENliLGRYRRPPFSRggflDRKAIrafaEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2032538500 146 PAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:COG3845 435 VGAIEFIHQRLLELR-DAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-191 |
2.17e-25 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 98.99 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVEIPYSYPElTVWENLe 80
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvDLRDLDLESLRKNIAYVPQDPFLFSG-TIRENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 itrrlrfikdpstvdsiieklkltpykdrkaknLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLA 160
Cdd:cd03228 97 ---------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALA 143
|
170 180 190
....*....|....*....|....*....|.
gi 2032538500 161 fnKGVTIFISSHLLGEIsRIATRIGIIHEGK 191
Cdd:cd03228 144 --KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-193 |
2.20e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.12 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII-----HAGCHElwnSVGYLVEIPYSYPELTV 75
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplHARARR---GIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WEN----LEITRRLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVE 151
Cdd:PRK10895 96 YDNlmavLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032538500 152 IRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:PRK10895 176 IKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-193 |
4.26e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.28 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII---HAGCHELWNSVGYLVEIP-YSYPELTVW 76
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKKVGLVFQYPeYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRFIKDPSTVDSIIE-----KLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVE 151
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRamnivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032538500 152 IRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:PRK13637 183 ILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-184 |
1.73e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 97.57 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEIT 82
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 RRLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFN 162
Cdd:PRK13538 99 QRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQ 178
|
170 180
....*....|....*....|..
gi 2032538500 163 KGVTIFISSHLLGEISRIATRI 184
Cdd:PRK13538 179 GGMVILTTHQDLPVASDKVRKL 200
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-207 |
1.78e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.83 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIK-----PTTGESYLKGE-IIHAGCHELWNSVGYLVEIPYSYPELT 74
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQdIFKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENLEITRRL-RFIKDPST----VDSIIEKLKL-TPYKDR---KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:PRK14247 99 IFENVALGLKLnRLVKSKKElqerVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 146 PAGIVEIRELLrdLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL-----HQLRNR 207
Cdd:PRK14247 179 PENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVftnprHELTEK 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-195 |
2.34e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.15 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHELWN---SVGYlveIPYSY---PELT 74
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAarrKIGM---IFQHFnllSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWEN----LEIT------RRLRfikdpstVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGL 144
Cdd:COG1135 99 VAENvalpLEIAgvpkaeIRKR-------VAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 145 DPAGIVEIRELLRDLafNK--GVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:COG1135 172 DPETTRSILDLLKDI--NRelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-193 |
4.80e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 96.96 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMI---KPTTGESYLKGEIIHAgcHELWNSVGYLVEIPYSYPELTVWEN 78
Cdd:cd03234 24 NDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKP--DQFQKCVAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEITRRLR-------FIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVE 151
Cdd:cd03234 102 LTYTAILRlprkssdAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032538500 152 IRELLRDLAfNKGVTIFISSHLLG-EISRIATRIGIIHEGKLI 193
Cdd:cd03234 182 LVSTLSQLA-RRNRIVILTIHQPRsDLFRLFDRILLLSSGEIV 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-175 |
5.39e-24 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 96.27 E-value: 5.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEITR 83
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 84 RLrFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNK 163
Cdd:TIGR01189 99 AI-HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARG 177
|
170
....*....|..
gi 2032538500 164 GVTIFISSHLLG 175
Cdd:TIGR01189 178 GIVLLTTHQDLG 189
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-199 |
6.48e-24 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 101.63 E-value: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEITR 83
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 84 RLRFIkdPST-VDSI----IEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPagivEIRELLRD 158
Cdd:TIGR01257 2038 RLRGV--PAEeIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP----QARRMLWN 2111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2032538500 159 LAFN---KGVTIFISSHLLGEISRIATRIGIIHEGKL-----IQEMDAK 199
Cdd:TIGR01257 2112 TIVSiirEGRAVVLTSHSMEECEALCTRLAIMVKGAFqclgtIQHLKSK 2160
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-172 |
9.33e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 100.44 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVEIPYSYPElTVWENLE 80
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvPLADADADSWRDQIAWVPQHPFLFAG-TIAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRR----------------LRFIKD-PSTVDSIIeklkltpykDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:TIGR02857 418 LARPdasdaeirealeraglDEFVAAlPQGLDTPI---------GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180
....*....|....*....|....*....
gi 2032538500 144 LDPAGIVEIRELLRDLAfnKGVTIFISSH 172
Cdd:TIGR02857 489 LDAETEAEVLEALRALA--QGRTVLLVTH 515
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-195 |
1.25e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 100.22 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVEIPYsYPELTVWENLEIT 82
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvDLSDLDPASWRRQIAWVPQNPY-LFAGTIRENLRLG 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 RRlrfikDPST-----------VDSIIEKLKL---TPYKDRkAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAG 148
Cdd:COG4988 435 RP-----DASDeeleaaleaagLDEFVAALPDgldTPLGEG-GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2032538500 149 IVEIRELLRDLAfnKGVTIFISSHLLGEIsRIATRIGIIHEGKLIQE 195
Cdd:COG4988 509 EAEILQALRRLA--KGRTVILITHRLALL-AQADRILVLDDGRIVEQ 552
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-195 |
1.81e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 96.69 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNsVGYLVEIPYSYPE-----LTV 75
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLE-VRKTVGIVFQNPDdqlfaPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENL------------EITRRlrfikdpstVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:PRK13639 97 EEDVafgplnlglskeEVEKR---------VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 144 LDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:PRK13639 168 LDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-193 |
4.69e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 94.77 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESY------LKGEIIHagchELWNSVGYL-VEIPYSYPE-L 73
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVW----ELRKRIGLVsPALQLRFPRdE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWE------------NLEITRRLRfikdpSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPS 141
Cdd:COG1119 96 TVLDvvlsgffdsiglYREPTDEQR-----ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 142 NGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1-192 |
4.80e-23 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 93.75 E-value: 4.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII---HAGCHELWNSVGYLVEIPYSYPELTVWE 77
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGMVFQQFNLFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITRRLRFIKDPSTVDSI----IEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:cd03262 96 NITLAPIKVKGMSKAEAEERalelLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVL 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2032538500 154 ELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:cd03262 176 DVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-191 |
5.14e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.06 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYL-----VEIpysYPELTVWEN 78
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVrtfqhVRL---FREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEIT--RRLR------FIKDP----STVDSI------IEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEP 140
Cdd:PRK11300 101 LLVAqhQQLKtglfsgLLKTPafrrAESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 141 SNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGK 191
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-192 |
5.58e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 94.01 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIhAGCHE-----LWNSVGYLVEIPYSYPELTVWEN 78
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGraipyLRRKIGVVFQDFRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEITRRLRFIKD---PSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:cd03292 99 VAFALEVTGVPPreiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNL 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 2032538500 156 LRDlaFNK-GVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:cd03292 179 LKK--INKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-193 |
6.16e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 6.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGE-SYLKGEiihagchelwnSVGYLVEIPYSYPELTVWENL- 79
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEvSIPKGL-----------RIGYLPQEPPLDDDLTVLDTVl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 -------EITRRLRFIKD---------------------------PSTVDSIIEKLKLTPYK-DRKAKNLSLGNSQRLGL 124
Cdd:COG0488 84 dgdaelrALEAELEELEAklaepdedlerlaelqeefealggweaEARAEEILSGLGFPEEDlDRPVSELSGGWRRRVAL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 125 AKALIHNPEILILDEPSNGLDPAGIVEIRELLRDlaFNKGVtIFIS--SHLLgeiSRIATRIGIIHEGKLI 193
Cdd:COG0488 164 ARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTV-LVVShdRYFL---DRVATRILELDRGKLT 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-194 |
7.73e-23 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 93.94 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIhAGCHELWNSVGYLVEIPYSYPELTVWEN----L 79
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQHYALFRHMTVFDNvafgL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRRLRfiKDPST-----VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRE 154
Cdd:cd03296 100 RVKPRSE--RPPEAeirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2032538500 155 LLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:cd03296 178 WLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-201 |
8.32e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.46 E-value: 8.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRML--LGMIKP---TTGESYLKGEIIHA---GCHELWNSVGYLVEIPYSYPe 72
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSprtDTVDLRKEIGMVFQQPNPFP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 LTVWENLEITRRLRFIKDPSTVDSIIEK-LK----LTPYKDR---KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGL 144
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDEAVEKsLKgasiWDEVKDRlhdSALGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 145 DPAGIVEIRELLrdLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK14239 180 DPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-195 |
1.11e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.61 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEI-----IHAGCHelwnsvgylveipysyPELTVW 76
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsalleLGAGFH----------------PELTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENL------------EITRRLRFIKDPSTvdsiIEKlkltpYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEpsnGL 144
Cdd:COG1134 107 ENIylngrllglsrkEIDEKFDEIVEFAE----LGD-----FIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE---VL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032538500 145 ---DPA----GIVEIRELLRdlafnKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:COG1134 175 avgDAAfqkkCLARIRELRE-----SGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-192 |
1.13e-22 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 97.78 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 10 KGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEITRRLR--- 86
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKgrs 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 87 FIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLrdLAFNKGVT 166
Cdd:TIGR01257 1035 WEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRT 1112
|
170 180
....*....|....*....|....*.
gi 2032538500 167 IFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:TIGR01257 1113 IIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-195 |
2.37e-22 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 96.44 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGY-LVEIpysypEL---TVW 76
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGiDLRQIDPASLRRQIGVvLQDV-----FLfsgTIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENL----------EITRRLRFikdpSTVDSIIEKLKL---TPYKDRkAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:COG2274 567 ENItlgdpdatdeEIIEAARL----AGLHDFIEALPMgydTVVGEG-GSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 144 LDPAGIVEIRELLRDLAfnKGVTIFISSHLLgEISRIATRIGIIHEGKLIQE 195
Cdd:COG2274 642 LDAETEAIILENLRRLL--KGRTVIIIAHRL-STIRLADRIIVLDKGRIVED 690
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-198 |
2.66e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESY-------LKGEIIHAGCHELWNSVGYLVEIPYSYPELTV 75
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDKAIRELRRNVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLeitrrlrfIKDPSTV------------DSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:PRK11124 100 QQNL--------IEAPCRVlglskdqalaraEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032538500 144 LDP---AGIVEIrelLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDA 198
Cdd:PRK11124 172 LDPeitAQIVSI---IRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-198 |
4.06e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.00 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-------IIHAGCHELWNSVGYLVEIPYSYPEL 73
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkPSEKAIRLLRQKVGMVFQQYNLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWENLeitrrlrfIKDPSTV------------DSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPS 141
Cdd:COG4161 98 TVMENL--------IEAPCKVlglskeqarekaMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 142 NGLDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDA 198
Cdd:COG4161 170 AALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-195 |
4.60e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 91.52 E-value: 4.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHELWNSVGYLVEIPYSYPElTVWENL 79
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-TIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 eitrrlRFIKDPSTVDSIIEKLKLTPYKD--------------RKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:cd03254 98 ------RLGRPNATDEEVIEAAKEAGAHDfimklpngydtvlgENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2032538500 146 PAGIVEIRELLRDLafNKGVTIFISSHLLGEIsRIATRIGIIHEGKLIQE 195
Cdd:cd03254 172 TETEKLIQEALEKL--MKGRTSIIIAHRLSTI-KNADKILVLDDGKIIEE 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-197 |
6.61e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.98 E-value: 6.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE---------IIHAG---CHELWNSVGYLveipysyP 71
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirsprdAIRAGimlCPEDRKAEGII-------P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 72 ELTVWENLEITRRLRFI---------KDPSTVDSIIEKLKL-TPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPS 141
Cdd:PRK11288 345 VHSVADNINISARRHHLragclinnrWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2032538500 142 NGLDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMD 197
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA 479
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-184 |
7.10e-22 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 90.63 E-value: 7.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLeitR 83
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL---R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 84 RLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNK 163
Cdd:cd03231 96 FWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARG 175
|
170 180
....*....|....*....|.
gi 2032538500 164 GVTIFISSHLLGEISRIATRI 184
Cdd:cd03231 176 GMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-201 |
1.34e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.06 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRML-----LGMIKPTTGESYLKGEIIHA---GCHELWNSVGYLVEIPYSYPE 72
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 LTVWENLEITRRL-RFIKDPSTVDSIIE-KLKLTPY----KDR---KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:PRK14267 100 LTIYDNVAIGVKLnGLVKSKKELDERVEwALKKAALwdevKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032538500 144 LDPAGIVEIRELLRDLafNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK14267 180 IDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-193 |
1.51e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGEsylkgeiIHAGcHELwnSVGYL----VEIPysyPELTVWE 77
Cdd:COG0488 332 DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-------VKLG-ETV--KIGYFdqhqEELD---PDKTVLD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLeitRRLRFIKDPSTVDSIIEKLKLTPYK-DRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDpagiVEIRELL 156
Cdd:COG0488 399 EL---RDGAPGGTEQEVRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD----IETLEAL 471
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2032538500 157 RDL--AFnKGVTIFIS--SHLLgeiSRIATRIGIIHEGKLI 193
Cdd:COG0488 472 EEAldDF-PGTVLLVShdRYFL---DRVATRILEFEDGGVR 508
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-255 |
1.93e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.59 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGeiihagcHELWNSVGYLVEI-----PYS-YPELT 74
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG-------VDLSHVPPYQRPInmmfqSYAlFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENL------------EITRRlrfikdpstVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSN 142
Cdd:PRK11607 108 VEQNIafglkqdklpkaEIASR---------VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 143 GLDPagivEIRELLR----DLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQ---LRNRTLFIdled 215
Cdd:PRK11607 179 ALDK----KLRDRMQlevvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEhptTRYSAEFI---- 250
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2032538500 216 kkGAQSLLanEGFDSTITEEGLIeITSEkALIHPEDVNSN 255
Cdd:PRK11607 251 --GSVNVF--EGVLKERQEDGLV-IDSP-GLVHPLKVDAD 284
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-197 |
2.98e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.57 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHELWNSVGYLVEIP----YSypeLTV 75
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAeNEKWVRSKVGLVFQDPddqvFS---STV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLE---ITRRLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEI 152
Cdd:PRK13647 98 WDDVAfgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2032538500 153 RELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMD 197
Cdd:PRK13647 178 MEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-194 |
3.29e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 92.94 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLK-GE----IIHAGCHELWNSVGYL--VEIPYS-YPELTV 75
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvdMTKPGPDGRGRAKRYIgiLHQEYDlYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLEITRRLRFIKDPSTVDSIIeKLKLTPYKDRKAKN--------LSLGNSQRLGLAKALIHNPEILILDEPSNGLDPA 147
Cdd:TIGR03269 383 LDNLTEAIGLELPDELARMKAVI-TLKMVGFDEEKAEEildkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2032538500 148 GIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:TIGR03269 462 TKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-195 |
6.30e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 88.36 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGeiihagchelwnSVGYLVEIPYSY-PELTVWENLE 80
Cdd:cd03220 39 KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSLLGLGGGFnPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFIKD---PSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPA----GIVEIR 153
Cdd:cd03220 107 LNGRLLGLSRkeiDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLR 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032538500 154 ELLRdlafnKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:cd03220 187 ELLK-----QGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-192 |
8.91e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.49 E-value: 8.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 5 SLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIiHAGCHELWNSVGYLVEIPYSYPELTVWEN--LEIT 82
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNigLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 RRLRFIKDP-STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAF 161
Cdd:PRK10771 98 PGLKLNAAQrEKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170 180 190
....*....|....*....|....*....|.
gi 2032538500 162 NKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:PRK10771 178 ERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-194 |
9.27e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.86 E-value: 9.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG----EIIHAGCHELWNSVGYLVEIPYS-YPELTV 75
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiaKISDAELREVRRKKIAMVFQSFAlMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLEITRRLRFIKDPSTVDSIIEKLK---LTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEI 152
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032538500 153 RELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-203 |
1.13e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 91.22 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHE--LWNSVGYLVEIPYS---YPELTVW 76
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdgLANGIVYISEDRKRdglVLGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITR---------RLRFIKDPSTVDSIIEKLKL-TPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDP 146
Cdd:PRK10762 349 ENMSLTAlryfsraggSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032538500 147 AGIVEIRELLRDlaFNK-GVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQ 203
Cdd:PRK10762 429 GAKKEIYQLINQ--FKAeGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQ 484
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-196 |
3.77e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII---------HAGC---HELWNSVGYLVEIPYS 69
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInalstaqrlARGLvylPEDRQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 70 YPELTVWENleitrRLRFIKDPSTVDSIIEK------LKLTpYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:PRK15439 360 WNVCALTHN-----RRGFWIKPARENAVLERyrralnIKFN-HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 144 LDPAGIVEIRELLRDLAFNKGVTIFISSHlLGEISRIATRIGIIHEGKLIQEM 196
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSD-LEEIEQMADRVLVMHQGEISGAL 485
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-193 |
3.91e-20 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 86.01 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 5 SLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGeSYLKGEIIHAGCHELWNSVGYLVEIPYSYPELTVWENLEITR- 83
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSG-RVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLs 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 84 -RLRFI-KDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAF 161
Cdd:cd03298 97 pGLKLTaEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|..
gi 2032538500 162 NKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-192 |
4.77e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHElwnSVGYLV-----EIPYSYpELTVWE 77
Cdd:PRK09536 21 GVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR---AASRRVasvpqDTSLSF-EFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITR---RLRFIK----DPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIV 150
Cdd:PRK09536 97 VVEMGRtphRSRFDTwtetDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032538500 151 EIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:PRK09536 177 RTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-195 |
8.51e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 8.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 17 LGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNSVGYLVEIPYSYPELTVWENLEITRRLRFIKDPST-- 93
Cdd:PRK13652 36 IGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpITKENIREVRKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETva 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 94 --VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNKGVTIFISS 171
Cdd:PRK13652 116 hrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFST 195
|
170 180
....*....|....*....|....
gi 2032538500 172 HLLGEISRIATRIGIIHEGKLIQE 195
Cdd:PRK13652 196 HQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-201 |
1.02e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGmIKPT---TGESYLKGE----------------IIHagcHELwnsvgYLV 64
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEelqasnirdteragiaIIH---QEL-----ALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 65 eipysyPELTVWENL----EITR--RLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILD 138
Cdd:PRK13549 95 ------KELSVLENIflgnEITPggIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 139 EPSNGLDPAGIVEIRELLRDLAfNKGVT-IFIsSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLK-AHGIAcIYI-SHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-193 |
1.20e-19 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 84.14 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLG--MIKPTTGESYLKGEIIHAgcHELWNSVGYLVEIPYSYPELTVWENL 79
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDK--RSFRKIIGYVPQDDILHPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRRLRfikdpstvdsiieklkltpykdrkakNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDL 159
Cdd:cd03213 104 MFAAKLR--------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2032538500 160 AfNKGVTIFISSH-LLGEISRIATRIGIIHEGKLI 193
Cdd:cd03213 158 A-DTGRTIICSIHqPSSEIFELFDKLLLLSQGRVI 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-200 |
1.64e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII--HAGCHELWNSVGYLVEIPYS---YPELTVW 76
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESRRDngfFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRFIKDPSTVDSIIEKLKLTPYKDRKAK-------------NLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELlalkchsvnqnitELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 144 LDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKK 200
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-193 |
2.51e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 85.04 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHELWNSVGYLVEIPYS-YPELTVWEN 78
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKeNLKEIRKKIGIIFQNPDNqFIGATVEDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 ----LEiTRRLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRE 154
Cdd:PRK13632 105 iafgLE-NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKK 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 2032538500 155 LLRDLAFNKGVTIFISSHLLGEISrIATRIGIIHEGKLI 193
Cdd:PRK13632 184 IMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLI 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-195 |
2.96e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.04 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGeiIHAGCHELWNSVGYLVEIPYSYPEL-----TV 75
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKLVGIVFQNPETqfvgrTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLEITRR---LRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEI 152
Cdd:PRK13644 96 EEDLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032538500 153 RELLRDLaFNKGVTIFISSHLLGEIsRIATRIGIIHEGKLIQE 195
Cdd:PRK13644 176 LERIKKL-HEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLE 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2-195 |
3.49e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.01 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchelwnsvgylveipYSYPEL-------- 73
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTA----------------LSEKELrkarrqig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 ------------TVWEN----LEITRRLR-FIKdpSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILI 136
Cdd:PRK11153 86 mifqhfnllssrTVFDNvalpLELAGTPKaEIK--ARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 137 LDEPSNGLDPAGIVEIRELLRDLafNK--GVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDI--NRelGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-201 |
3.53e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.76 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYlKGEIIHAG--------CHELWNSVGYLVEIPYSYPe 72
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRY-SGDVLLGGrsifnyrdVLEFRRRVGMLFQRPNPFP- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 LTVWENL-------EITRRLRF-------IKDPSTVDSIIEKLKLTPYKdrkaknLSLGNSQRLGLAKALIHNPEILILD 138
Cdd:PRK14271 115 MSIMDNVlagvrahKLVPRKEFrgvaqarLTEVGLWDAVKDRLSDSPFR------LSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 139 EPSNGLDPAGIVEIRELLRDLAfnKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1-195 |
4.10e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 82.36 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYSYpELTVWENLe 80
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLF-DTTLRNNL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 itrrlrfikdpstvdsiieklkltpykdrkAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLA 160
Cdd:cd03247 96 ------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL 145
|
170 180 190
....*....|....*....|....*....|....*
gi 2032538500 161 FNKGVtIFISSHLLGeISRiATRIGIIHEGKLIQE 195
Cdd:cd03247 146 KDKTL-IWITHHLTG-IEH-MDKILFLENGKIIMQ 177
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-197 |
5.34e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 83.93 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIK--P---TTGESYLKGE-IIHAGC--HELWNSVGYLVEIPYSYPeL 73
Cdd:COG1117 28 KDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEdIYDPDVdvVELRRRVGMVFQKPNPFP-K 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWENLEITRRLRFIKDPSTVDSIIEK-LK-------LtpyKDR---KAKNLSLGNSQRLGLAKALIHNPEILILDEPSN 142
Cdd:COG1117 107 SIYDNVAYGLRLHGIKSKSELDEIVEEsLRkaalwdeV---KDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032538500 143 GLDPAGIVEIRELLRDLAfnKGVTIFISSHLLGEISRIATRIGIIHEGKLIqEMD 197
Cdd:COG1117 184 ALDPISTAKIEELILELK--KDYTIVIVTHNMQQAARVSDYTAFFYLGELV-EFG 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-194 |
8.47e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 8.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAG-------CHELWNSVGYLVEIPYSYPEL 73
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGkdifqidAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWENLEITRRLRFIKDPSTVDSIIEKL--KLTPYK---DR---KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVEEClrKVGLWKevyDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2032538500 146 PAGIVEIRELLRDLafNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:PRK14246 186 IVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-201 |
1.05e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.50 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNSVGYLVEIPYSYPELTVWEnle 80
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhIQHYASKEVARRIGLLAQNATTPGDITVQE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFIKDP----------STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIV 150
Cdd:PRK10253 101 LVARGRYPHQPlftrwrkedeEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 151 EIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-203 |
1.08e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.28 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA----GCHELWNSVGYLVEIPYSYPELTVWEN 78
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEIT-RRLRFIKDP---STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRE 154
Cdd:PRK11831 105 VAYPlREHTQLPAPllhSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2032538500 155 LLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQ 203
Cdd:PRK11831 185 LISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-192 |
1.15e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 81.11 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHELWNSVGYLveipysypeltvwenle 80
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYL----------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 itrrlrfikdPSTV----DSIIEKLkltpykdrkaknLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELL 156
Cdd:cd03246 82 ----------PQDDelfsGSIAENI------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 2032538500 157 RDLAFnKGVTIFISSHLLGEIsRIATRIGIIHEGKL 192
Cdd:cd03246 140 AALKA-AGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-193 |
1.26e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNSVGYLVEIPYSyPE-LTVWENLE 80
Cdd:PRK11231 20 DLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpISMLSSRQLARRLALLPQHHLT-PEgITVRELVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITR--------RLRfIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEI 152
Cdd:PRK11231 99 YGRspwlslwgRLS-AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVEL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2032538500 153 RELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:PRK11231 178 MRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-190 |
1.81e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGylVEIPYS----YPELTVW 76
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG--IGIIYQelsvIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRL------------RFIKDPSTVDSIIEKLKLTPykDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGL 144
Cdd:PRK09700 99 ENLYIGRHLtkkvcgvniidwREMRVRAAMMLLRVGLKVDL--DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032538500 145 DPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEG 190
Cdd:PRK09700 177 TNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-192 |
1.95e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.98 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIK-PTTGESYLKGE--IIHAGCHELWNSVGYLVEIPYSY---PELTVW 76
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPEDRKRDgivPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRF-----IKDPSTVDSI---IEKLKL-TPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPA 147
Cdd:PRK13549 360 KNITLAALDRFtggsrIDDAAELKTIlesIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2032538500 148 GIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:PRK13549 440 AKYEIYKLINQLV-QQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-215 |
2.16e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.91 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVEIPYSYPELTVWENl 79
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRPVRKRIGMVFQFPESQLFED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRRLRFikDPSTVDSIIEKLKLTPYK------------DRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPA 147
Cdd:PRK13646 102 TVEREIIF--GPKNFKMNLDEVKNYAHRllmdlgfsrdvmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 148 GIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQLRNR--TLFIDLED 215
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKlaDWHIGLPE 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-198 |
2.17e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE----------------IIHagcHELwnsvgYLVei 66
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagvaIIY---QEL-----HLV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 67 pysyPELTVWENLEITR---RLRFIKDPSTVDSIIEKLK-----LTPykDRKAKNLSLGNSQRLGLAKALIHNPEILILD 138
Cdd:PRK11288 92 ----PEMTVAENLYLGQlphKGGIVNRRLLNYEAREQLEhlgvdIDP--DTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 139 EPSNGLDPAGIVEIRELLRDLAFNKGVTIFIsSHLLGEISRIATRIGIIHEGKLIQEMDA 198
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYV-SHRMEEIFALCDAITVFKDGRYVATFDD 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-207 |
2.27e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 84.82 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHE-LWNSVGYLVEIPYsypeL---TVWE 77
Cdd:COG4987 352 DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdLRRRIAVVPQRPH----LfdtTLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLeitrrlRFIKDPSTVDSIIEKLK---LTPYKDR-----------KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:COG4987 428 NL------RLARPDATDEELWAALErvgLGDWLAAlpdgldtwlgeGGRRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 144 LDPAGIVEIRELLRDLAFNKGVtIFISSHLLGEisRIATRIGIIHEGKLIQEMDAKKLHQLRNR 207
Cdd:COG4987 502 LDAATEQALLADLLEALAGRTV-LLITHRLAGL--ERMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1-191 |
2.93e-18 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 81.69 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKG-----EIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEiihagchelwnSVGY---LVEIPYsypE 72
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-----------TVSYkpqYIKADY---E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 LTVWENL-EITRrlRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVE 151
Cdd:cd03237 76 GTVRDLLsSITK--DFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2032538500 152 IRELLRDLAFNKGVTIFISSHLLGEISRIATRIgIIHEGK 191
Cdd:cd03237 154 ASKVIRRFAENNEKTAFVVEHDIIMIDYLADRL-IVFEGE 192
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-192 |
3.77e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIH----AGCHELwnsvG-YLV-EIPYSYPELT 74
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArltpAKAHQL----GiYLVpQEPLLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENleITRRL-RFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGI---- 149
Cdd:PRK15439 103 VKEN--ILFGLpKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETerlf 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032538500 150 VEIRELLrdlafNKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:PRK15439 181 SRIRELL-----AQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-172 |
3.90e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELwnSVGYLVEIPYSYPELTVWENLEITR 83
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE--ACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 84 RLRFiKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRD-LAfn 162
Cdd:PRK13539 99 AFLG-GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLA-- 175
|
170
....*....|
gi 2032538500 163 KGVTIFISSH 172
Cdd:PRK13539 176 QGGIVIAATH 185
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-239 |
4.08e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.99 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGeiihagchelwnsvgylveIPYSypELTVWEnle 80
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-------------------MVLS--EETVWD--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFI-KDP------STV----------------------DSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHN 131
Cdd:PRK13635 79 VRRQVGMVfQNPdnqfvgATVqddvafglenigvpreemvervDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 132 PEILILDEPSNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRiATRIGIIHEGKLIQEMDAKKLHQLRNRTLFI 211
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQEI 237
|
250 260 270
....*....|....*....|....*....|...
gi 2032538500 212 --DLEDKKGAQSLLANEGF---DSTITEEGLIE 239
Cdd:PRK13635 238 glDVPFSVKLKELLKRNGIllpNTYLTMESLVD 270
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-194 |
4.62e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.82 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIhAGCHELWNSVGYLVEIPYSYPELTVWENLE-- 80
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQHYALFRHMTVFDNIAfg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ---ITRRLR----FIKdpSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:PRK10851 99 ltvLPRRERpnaaAIK--AKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032538500 154 ELLRDLAFN-KGVTIFIsSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:PRK10851 177 RWLRQLHEElKFTSVFV-THDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-203 |
4.64e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchelWNS------VGYLveiPYSYPE---LT 74
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES-----WSSkafarkVAYL---PQQLPAaegMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENLEITRRL------RF-IKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPA 147
Cdd:PRK10575 102 VRELVAIGRYPwhgalgRFgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2032538500 148 GIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQ 203
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1-191 |
5.55e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.64 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTtgesylKGEIIHAGChelwNSVGYLVEipysypeltvwenle 80
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD------EGIVTWGST----VKIGYFEQ--------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 itrrlrfikdpstvdsiieklkltpykdrkaknLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLa 160
Cdd:cd03221 71 ---------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY- 116
|
170 180 190
....*....|....*....|....*....|.
gi 2032538500 161 fnKGVTIFIsSHLLGEISRIATRIGIIHEGK 191
Cdd:cd03221 117 --PGTVILV-SHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-195 |
6.11e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.67 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGeIIHAGCHELWNS---------------VGYLVE 65
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-LDTSDEENLWDIrnkagmvfqnpdnqiVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 66 IPYSY-PELTVWENLEITRRlrfikdpstVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGL 144
Cdd:PRK13633 105 EDVAFgPENLGIPPEEIRER---------VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 145 DPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRiATRIGIIHEGKLIQE 195
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-193 |
6.22e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.97 E-value: 6.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchelW---------------NSVgylveipy 68
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD-----WspaelarrravlpqhSSL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 69 SYPeLTVWENLEITR---RLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKAL--IHNPE----ILILDE 139
Cdd:PRK13548 88 SFP-FTVEEVVAMGRaphGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqLWEPDgpprWLLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 140 PSNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:PRK13548 167 PTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-195 |
8.08e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.31 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchelWNSVGYLVEIPYSYPE-------L 73
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD-----WQTAKIMREAVAIVPEgrrvfsrM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWENLEITRrlrFIKDPSTVDSIIEKL-----KLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAG 148
Cdd:PRK11614 96 TVEENLAMGG---FFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2032538500 149 IVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:PRK11614 173 IQQIFDTIEQLR-EQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
4-193 |
8.94e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.36 E-value: 8.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIkPTTGESYLKGE-IIHAGCHELWNSVGYLVEIPYSYPELTVWENLEIT 82
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQpLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 R--RLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKAL--IH---NPE--ILILDEPSNGLDPAGIVEIR 153
Cdd:PRK03695 94 QpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWpdiNPAgqLLLLDEPMNSLDVAQQAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2032538500 154 ELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:PRK03695 174 RLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-195 |
1.04e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.91 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYlveIP-----YSypeLTV 75
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvDIRDLTLESLRRQIGV---VPqdtflFS---GTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLeitrrlRFIKDPSTVDSIIEKLKL---------------TPYKDRkAKNLSLGNSQRLGLAKALIHNPEILILDEP 140
Cdd:COG1132 431 RENI------RYGRPDATDEEVEEAAKAaqahefiealpdgydTVVGER-GVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032538500 141 SNGLDPAGIVEIRELLRDLAfnKGVTIFISSHLLGEIsRIATRIGIIHEGKLIQE 195
Cdd:COG1132 504 TSALDTETEALIQEALERLM--KGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQ 555
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-191 |
2.08e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.78 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 5 SLNVDKGEIY-----GFLGLNGAGKTTTIRMLLGMIKPTTGESYLKgeiihagchelwnsvgylVEIPY------SYPEL 73
Cdd:PRK13409 354 SLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------------LKISYkpqyikPDYDG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWENLE-ITRRLrfikDPSTVDS-IIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDpagiVE 151
Cdd:PRK13409 416 TVEDLLRsITDDL----GSSYYKSeIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2032538500 152 IR----ELLRDLAFNKGVTIFISSHLLGEISRIATRIgIIHEGK 191
Cdd:PRK13409 488 QRlavaKAIRRIAEEREATALVVDHDIYMIDYISDRL-MVFEGE 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-192 |
2.29e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 79.05 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEipySYPEL---TVWE 77
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG---QEPVLfarSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEI------TRRLRFIKDPSTVDSIIEKLKLTPYKD--RKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGI 149
Cdd:cd03248 107 NIAYglqscsFECVKEAAQKAHAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032538500 150 VEIRELLRDlaFNKGVTIFISSHLLGEISRiATRIGIIHEGKL 192
Cdd:cd03248 187 QQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-193 |
2.44e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 78.79 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG----EIIHAgchELWNSVGYLVEIPYsypeL---TVW 76
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirQLDPA---DLRRNIGYVPQDVT----LfygTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENleITRRLRFIKDPSTVDsIIEKLKLTPYKDRKAK-----------NLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:cd03245 96 DN--ITLGAPLADDERILR-AAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 146 PAGIVEIRELLRDLAfnKGVTIFISSH---LLgeisRIATRIGIIHEGKLI 193
Cdd:cd03245 173 MNSEERLKERLRQLL--GDKTLIIITHrpsLL----DLVDRIIVMDSGRIV 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-192 |
4.74e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.64 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPT-TGESYLKG---------EIIHAGchelwnsvgyLVEIPYS--- 69
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpvdirnpaQAIRAG----------IAMVPEDrkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 70 ---YPELTVWENLEITRRLRF-----IKDPSTVDSI---IEKLKL-TPYKDRKAKNLSLGNSQRLGLAKALIHNPEILIL 137
Cdd:TIGR02633 348 hgiVPILGVGKNITLSVLKSFcfkmrIDAAAELQIIgsaIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032538500 138 DEPSNGLDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-178 |
6.05e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHElwNSVGYLV---EIPYSYPELTvwE 77
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK--NLVAYVPqseEVDWSFPVLV--E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITRR------LRFIK--DPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGI 149
Cdd:PRK15056 99 DVVMMGRyghmgwLRRAKkrDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180
....*....|....*....|....*....
gi 2032538500 150 VEIRELLRDLAfNKGVTIFISSHLLGEIS 178
Cdd:PRK15056 179 ARIISLLRELR-DEGKTMLVSTHNLGSVT 206
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-217 |
6.23e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 77.91 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVEipysypeltvwENL 79
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhDLALADPAWLRRQVGVVLQ-----------ENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRRLR---FIKDPS-TVDSIIEKLKLTPYKD--------------RKAKNLSLGNSQRLGLAKALIHNPEILILDEPS 141
Cdd:cd03252 87 LFNRSIRdniALADPGmSMERVIEAAKLAGAHDfiselpegydtivgEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032538500 142 NGLDPAGIVEIRELLRDLAfnKGVTIFISSHLLGEISRiATRIGIIHEGKLIQEMDAKKLhqLRNRTLFIDLEDKK 217
Cdd:cd03252 167 SALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL--LAENGLYAYLYQLQ 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-222 |
6.76e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.62 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLkGEIIHAGCHE------LWNSVGYLVEIPYSYP-ELTV 75
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKqkeikpVRKKVGVVFQFPESQLfEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLEITRRLRFIKDPSTVDSIIEKLKLT----PYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVE 151
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIAAEKLEMVgladEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 152 IRELLRDLaFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI---------QEMDAKKLHQL--RNRTLFIDLEDKKGAQ 220
Cdd:PRK13643 183 MMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIscgtpsdvfQEVDFLKAHELgvPKATHFADQLQKTGAV 261
|
..
gi 2032538500 221 SL 222
Cdd:PRK13643 262 TF 263
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-244 |
1.03e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgcHELWN---SVGYLVEIP-YSYPELTVWENL 79
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA--ENVWNlrrKIGMVFQNPdNQFVGATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRRLRFIKDPSTVDSIIEKL---KLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELL 156
Cdd:PRK13642 104 AFGMENQGIPREEMIKRVDEALlavNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 157 RDLAFNKGVTIFISSHLLGEISRiATRIGIIHEGKLIQEMDAKKLHQLRNRTLFIDLEDKKGAQSL--LANEGFD---ST 231
Cdd:PRK13642 184 HEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVPFSSNLMkdLRKNGFDlpeKY 262
|
250
....*....|...
gi 2032538500 232 ITEEGLIEITSEK 244
Cdd:PRK13642 263 LSEDELVELLADK 275
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-201 |
1.13e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.44 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII---HAGCHELWNSVGYLVEIPYSYPELTVWE 77
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERLIRQEAGMVFQQFYLFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEI-TRRLRFIKDPSTVD---SIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:PRK09493 97 NVMFgPLRVRGASKEEAEKqarELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2032538500 154 ELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK09493 177 KVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-191 |
1.17e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 79.83 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIY-----GFLGLNGAGKTTTIRMLLGMIKPTTGEsyLKGEIihagchelwnSVGY---LVEIPYsypELT 74
Cdd:COG1245 353 GFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDL----------KISYkpqYISPDY---DGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENLEITRrlrfikdPSTVDS------IIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDpag 148
Cdd:COG1245 418 VEEFLRSAN-------TDDFGSsyykteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--- 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2032538500 149 iVEIR----ELLRDLAFNKGVTIFISSHLLGEISRIATRIgIIHEGK 191
Cdd:COG1245 488 -VEQRlavaKAIRRFAENRGKTAMVVDHDIYLIDYISDRL-MVFEGE 532
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-203 |
1.42e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAG------ChelwnsvgyLVEIPYS-YPELTV 75
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdVTHRSiqqrdiC---------MVFQSYAlFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENleITRRLRFIKDPST-----VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIV 150
Cdd:PRK11432 96 GEN--VGYGLKMLGVPKEerkqrVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 151 EIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQ 203
Cdd:PRK11432 174 SMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-195 |
1.56e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 76.81 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHELWNSVGYLVEIPYSYpELTVWENLe 80
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLF-DGTIAENI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 itrrlRFIKDPSTVDSIIEKLKLT---------PYKDR-----KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDP 146
Cdd:cd03249 98 -----RYGKPDATDEEVEEAAKKAnihdfimslPDGYDtlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2032538500 147 AGIVEIRELLRDLAfnKGVTIFISSHLLGEISRiATRIGIIHEGKLIQE 195
Cdd:cd03249 173 ESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-201 |
2.27e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.71 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLkGEI-IHAGCH---------ELWNSVGYLVEIPYSY 70
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDItIDTARSlsqqkglirQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 71 PELTVWENLeitrrlrfIKDPSTVD------------SIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILD 138
Cdd:PRK11264 98 PHRTVLENI--------IEGPVIVKgepkeeatararELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 139 EPSNGLDPAGIVEIRELLRDLAFNKGvTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-194 |
2.94e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMikpttgeSYLKGEIIHAGCHELWNSVGY-----------LVEIPYSYPE 72
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-------NELESEVRVEGRVEFFNQNIYerrvnlnrlrrQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 L---TVWENLEITRRLRFIKDPSTVDSIIEK-LKLTPYKD-------RKAKNLSLGNSQRLGLAKALIHNPEILILDEPS 141
Cdd:PRK14258 99 LfpmSVYDNVAYGVKIVGWRPKLEIDDIVESaLKDADLWDeikhkihKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032538500 142 NGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIH--EGKLIQ 194
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnENRIGQ 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
4.67e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.94 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHELWNSVGYLVEIPY-----SYPELT 74
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLRKHIGIVFQNPDnqfvgSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENLEiTRRLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRE 154
Cdd:PRK13648 105 VAFGLE-NHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 155 LLRDLAFNKGVTIFISSHLLGEISRiATRIGIIHEGKLIQEMDAKKLHQLRNRTLFIDLE---DKKGAQSLlaneGFDST 231
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGLDlpfPIKINQML----GHQTS 258
|
....*....
gi 2032538500 232 -ITEEGLIE 239
Cdd:PRK13648 259 fLTYEGLVD 267
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-194 |
4.98e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.29 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIH--AGCHELWNSVGylveipYSY---PELTV 75
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvPAENRHVNTVF------QSYalfPHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLEITRRLRFIKDPSTVDSIIEKLK---LTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD----PAG 148
Cdd:PRK09452 104 FENVAFGLRMQKTPAAEITPRVMEALRmvqLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2032538500 149 IVEIRELLRDLafnkGVT-IFIsSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:PRK09452 184 QNELKALQRKL----GITfVFV-THDQEEALTMSDRIVVMRDGRIEQ 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-207 |
6.51e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.60 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGchelwnsvgylveiPYSYPeltvwenle 80
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG--------------DYSYR--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 iTRRLRFI-KDPST-------VDSIIE-----KLKLTPYKDRKAKNLSL-------------------GNSQRLGLAKAL 128
Cdd:PRK15112 86 -SQRIRMIfQDPSTslnprqrISQILDfplrlNTDLEPEQREKQIIETLrqvgllpdhasyyphmlapGQKQRLGLARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 129 IHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNKGVT-IFISSHlLGEISRIATRIGIIHEGKLIQ-----EMDAKKLH 202
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISyIYVTQH-LGMMKHISDQVLVMHQGEVVErgstaDVLASPLH 243
|
....*
gi 2032538500 203 QLRNR 207
Cdd:PRK15112 244 ELTKR 248
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-195 |
6.65e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.03 E-value: 6.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHEL-------------WNsvgyLveipy 68
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrrkvgmvfqqFN----L----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 69 sYPELTVWENleITRRLRFIK--DPSTVDSI----IEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSN 142
Cdd:COG1126 89 -FPHLTVLEN--VTLAPIKVKkmSKAEAEERamelLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2032538500 143 GLDPAGIVEIRELLRDLAfNKGVTIFISSHllgEIS---RIATRIGIIHEGKLIQE 195
Cdd:COG1126 166 ALDPELVGEVLDVMRDLA-KEGMTMVVVTH---EMGfarEVADRVVFMDGGRIVEE 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-193 |
7.85e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIH---AGCHELWNSVGYLVEIP---------- 67
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskRGLLALRQQVATVFQDPeqqifytdid 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 68 ----YSYPELTVWENlEITRRlrfikdpstVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:PRK13638 97 sdiaFSLRNLGVPEA-EITRR---------VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2032538500 144 LDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-201 |
9.15e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.07 E-value: 9.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNSVGYLVEIPYSYPElTVWENl 79
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVpLVQYDHHYLHRQVALVGQEPVLFSG-SVREN- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 eITRRLRFIKDP--------STVDSIIEKLKLTPYKD--RKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDpagi 149
Cdd:TIGR00958 575 -IAYGLTDTPDEeimaaakaANAHDFIMEFPNGYDTEvgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD---- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 150 VEIRELLRDLAFNKGVTIFISSHLLGEISRiATRIGIIHEGKLIQEMDAKKL 201
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-194 |
1.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.44 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHE-----LWNSVGylveIPYSYPELTV 75
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkpLRKKVG----IVFQFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WE------------NLEITRRlrfiKDPSTVDSIIEKLKLTP-YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSN 142
Cdd:PRK13634 99 FEetvekdicfgpmNFGVSEE----DAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 143 GLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-174 |
1.08e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGEsylkgeIIHAgcHELwnSVGYLVEIPYSYPELTvwenLE 80
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV------IKRN--GKL--RIGYVPQKLYLDTTLP----LT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFikDPSTVDSII----EKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELL 156
Cdd:PRK09544 86 VNRFLRL--RPGTKKEDIlpalKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
170
....*....|....*...
gi 2032538500 157 RDLAFNKGVTIFISSHLL 174
Cdd:PRK09544 164 DQLRRELDCAVLMVSHDL 181
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-153 |
1.19e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIhagchelwN-------SVGyLVEIPYS-YPEL 73
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM--------NdvppaerGVG-MVFQSYAlYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWENLEITRRLRFIKDP---STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIV 150
Cdd:PRK11000 91 SVAENMSFGLKLAGAKKEeinQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
...
gi 2032538500 151 EIR 153
Cdd:PRK11000 171 QMR 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-195 |
1.36e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.72 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYS------YPELT 74
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQdsisavNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENL-EITRRLRFIKDP---STVDSIIEKLKLTP-YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGI 149
Cdd:PRK10419 108 VREIIrEPLRHLLSLDKAerlARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032538500 150 VEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQE 195
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-195 |
1.36e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.38 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGM--IKPTTGESylkgeIIHAGCHElwnSVGYlVEIP----------- 67
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRI-----IYHVALCE---KCGY-VERPskvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 68 --YSYPELTVWeNLEITRRLRFIK--------------DPSTVDSIIEKLKLTPYKDRK--------------------- 110
Cdd:TIGR03269 87 gtLEPEEVDFW-NLSDKLRRRIRKriaimlqrtfalygDDTVLDNVLEALEEIGYEGKEavgravdliemvqlshrithi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 111 AKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEG 190
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENG 245
|
....*
gi 2032538500 191 KLIQE 195
Cdd:TIGR03269 246 EIKEE 250
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-172 |
1.41e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.62 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 11 GEIYGFLGLNGAGKTTTIRMLLGMIKPTT---GESYLKGEIIHAGCHELWNsvGYLVEIPYSYPELTVWENLEITRRLRF 87
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAKEMRAIS--AYVQQDDLFIPTLTVREHLMFQAHLRM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 88 IKDPST------VDSIIEKLKLTPYKDRK------AKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:TIGR00955 129 PRRVTKkekrerVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170
....*....|....*..
gi 2032538500 156 LRDLAfNKGVTIFISSH 172
Cdd:TIGR00955 209 LKGLA-QKGKTIICTIH 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-239 |
1.45e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.77 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgcHELWNS---------------VGYLVE 65
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE--ENVWDIrhkigmvfqnpdnqfVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 66 IPYSYPeltvWENLEITRRLRfikdPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:PRK13650 101 DDVAFG----LENKGIPHEEM----KERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 146 PAGIVEIRELLRDLAFNKGVTIFISSHLLGEISrIATRIGIIHEGKLIQEMDAKKLHQLRNRTLFIDLEDKKGAQ--SLL 223
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDLLQLGLDIPFTTSlvQSL 251
|
250
....*....|....*....
gi 2032538500 224 ANEGFD---STITEEGLIE 239
Cdd:PRK13650 252 RQNGYDlpeGYLTEKELEE 270
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-196 |
2.12e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 73.70 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIH----AGCHELWN-SVGYLVEIPYSYPELTV 75
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssAAKAELRNqKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLEITRRLRFIKDPSTVDSIIEKLKLTPYKDR---KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEI 152
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRanhRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2032538500 153 RELLRDLAFNKGVTIFISSHLLGEISRIATRIGiIHEGKLIQEM 196
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAEL 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-200 |
2.56e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.60 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGmIKPT---TGESYLKGE----------------IIHagcHELwnsvgYLV 64
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEvcrfkdirdsealgivIIH---QEL-----ALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 65 eipysyPELTVWENL----EITRRlRFIKDPSTVDSIIEKLK---LTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILIL 137
Cdd:NF040905 91 ------PYLSIAENIflgnERAKR-GVIDWNETNRRARELLAkvgLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 138 DEPSNGLDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKK 200
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLELK-AQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-203 |
4.32e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.63 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGC-----HELWNSVGYLVEIPYSYP-ELTVW 76
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdiKQIRKKVGLVFQFPESQLfEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRFIKDPSTVDSIIEKLKLT----PYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEI 152
Cdd:PRK13649 105 KDVAFGPQNFGVSQEEAEALAREKLALVgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 153 RELLRDLaFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQ 203
Cdd:PRK13649 185 MTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-173 |
4.89e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 74.70 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCH-ELWNSVGYLVEIPYSYpELTVWENL--- 79
Cdd:TIGR02868 354 VSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQDAHLF-DTTVRENLrla 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 -------EITRRLRFIKDPSTVDSIIEKL--KLTPykdrKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGiv 150
Cdd:TIGR02868 433 rpdatdeELWAALERVGLADWLRALPDGLdtVLGE----GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET-- 506
|
170 180
....*....|....*....|....*
gi 2032538500 151 eIRELLRDL--AFNKGVTIFISSHL 173
Cdd:TIGR02868 507 -ADELLEDLlaALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-193 |
6.73e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.91 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKP-TTGESYLKGEIIHAGCHELWNsVGYLVEIPYSYPE-----LT 74
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPdDNPNSKITVDGITLTAKTVWD-IREKVGIVFQNPDnqfvgAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENLEITRRLRFIKDP---STVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVE 151
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPemiKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032538500 152 IRELLRDLAFNKGVTIFISSHLLGEISrIATRIGIIHEGKLI 193
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLL 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-199 |
7.04e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.83 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHE---LWNSVGYLVEIPYSYPELTVW 76
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhDITRLKNREvpfLRRQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENL------------EITRRlrfikdpstVDSIIEKLKLTPykdrKAKN----LSLGNSQRLGLAKALIHNPEILILDEP 140
Cdd:PRK10908 98 DNVaipliiagasgdDIRRR---------VSAALDKVGLLD----KAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 141 SNGLDPAGIVEIRELLRDlaFNK-GVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAK 199
Cdd:PRK10908 165 TGNLDDALSEGILRLFEE--FNRvGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-204 |
7.41e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.12 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 5 SLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELwNSVGYL---VEIPYSYPELTVWENlEI 81
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKI-KEVKRLrkeIGLVFQFPEYQLFQE-TI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 TRRLRF------IKDPSTVDSIIEKLKLTP----YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVE 151
Cdd:PRK13645 109 EKDIAFgpvnlgENKQEAYKKVPELLKLVQlpedYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 152 IRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ-----------------EMDAKKLHQL 204
Cdd:PRK13645 189 FINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISigspfeifsnqelltkiEIDPPKLYQL 258
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
70-146 |
8.27e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.39 E-value: 8.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 70 YPELTVWENLEITRRLrFIKDPSTVDSIIEKL----KLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:NF033858 90 YPTLSVFENLDFFGRL-FGQDAAERRRRIDELlratGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
.
gi 2032538500 146 P 146
Cdd:NF033858 169 P 169
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-156 |
8.65e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.42 E-value: 8.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEiiHAGCHELWNSVGYLVEIPYSYPELTVWENLEITR 83
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGDRSRFMAYLGHLPGLKADLSTLENLHFLC 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 84 RLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELL 156
Cdd:PRK13543 108 GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1-195 |
8.88e-15 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 71.88 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVE------------IP 67
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhDVRDYTLASLRRQIGLVSQdvflfndtvaenIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 68 YSYPELT---VWENLEITRRLRFIKD-PSTVDSIIEklkltpykDRKAKnLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:cd03251 98 YGRPGATreeVEEAARAANAHEFIMElPEGYDTVIG--------ERGVK-LSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 144 LDPAGIVEIRELLRDLAfnKGVTIFISSHLLGEIsRIATRIGIIHEGKLIQE 195
Cdd:cd03251 169 LDTESERLVQAALERLM--KNRTTFVIAHRLSTI-ENADRIVVLEDGKIVER 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-145 |
8.89e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.20 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIihagchelwnSVGYLVEIPYSYPELTVWENLE 80
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI----------KVGYLPQEPQLDPTKTVRENVE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 --------ITRRL-----RFIKDPSTVDSIIEK--------------------------LKLTPyKDRKAKNLSLGNSQR 121
Cdd:TIGR03719 91 egvaeikdALDRFneisaKYAEPDADFDKLAAEqaelqeiidaadawdldsqleiamdaLRCPP-WDADVTKLSGGERRR 169
|
170 180
....*....|....*....|....
gi 2032538500 122 LGLAKALIHNPEILILDEPSNGLD 145
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-201 |
1.65e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.78 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-----GCHELWNSVGYLVEIPYSYP-ELTVW 76
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnkNLKKLRKKVSLVFQFPEAQLfENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEI-------------TRRLRFIKDPSTVDSIIEKlklTPYKdrkaknLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:PRK13641 105 KDVEFgpknfgfsedeakEKALKWLKKVGLSEDLISK---SPFE------LSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032538500 144 LDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-201 |
1.98e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.94 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTT--GESYLKGEIIHAGCHELWNSVGYLV---EIPYsYPELTVWEN 78
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIVIihqELTL-VPELSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 L----EITRRLRFIKDPSTV---DSIIEKLKLTPYKD-RKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIV 150
Cdd:TIGR02633 99 IflgnEITLPGGRMAYNAMYlraKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 151 EIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:TIGR02633 179 ILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-201 |
3.67e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 72.46 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII-HAGCHELWNSVGYLVEIPYSYPElTVWENL 79
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLkDIDRHTLRQFINYLPQEPYIFSG-SILENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 -----------EITRRLRFIKdpstVDSIIEKLKLTPYKD--RKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDP 146
Cdd:TIGR01193 569 llgakenvsqdEIWAACEIAE----IKDDIENMPLGYQTElsEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032538500 147 agIVEiRELLRDLAFNKGVTIFISSHLLgEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:TIGR01193 645 --ITE-KKIVNNLLNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-181 |
4.67e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRML--LGMIKPT---TGESYLKGEIIHAG---CHELWNSVGYLVEIPYSYPE 72
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYAPdvdPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 lTVWENLEITRRL------------RFIKDPSTVDSIIEKLKltpykdRKAKNLSLGNSQRLGLAKALIHNPEILILDEP 140
Cdd:PRK14243 106 -SIYDNIAYGARIngykgdmdelveRSLRQAALWDEVKDKLK------QSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2032538500 141 SNGLDPAGIVEIRELLRDLAfnKGVTIFISSHLLGEISRIA 181
Cdd:PRK14243 179 CSALDPISTLRIEELMHELK--EQYTIIIVTHNMQQAARVS 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-198 |
5.72e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.36 E-value: 5.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMI--KPTTGESYLKGEIIHAgchelwNSVGYLVEIPYSYpeltVWE-- 77
Cdd:NF040905 277 DDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDV------STVSDAIDAGLAY----VTEdr 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 -----NLE--ITR-----RLRFIKDPSTVDSIIE---------KLKL-TPYKDRKAKNLSLGNSQRLGLAKALIHNPEIL 135
Cdd:NF040905 347 kgyglNLIddIKRnitlaNLGKVSRRGVIDENEEikvaeeyrkKMNIkTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVL 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 136 ILDEPSNGLDPAGIVEIRELLRDLAFN-KGVtIFISSHlLGEISRIATRIGIIHEGKLIQEMDA 198
Cdd:NF040905 427 ILDEPTRGIDVGAKYEIYTIINELAAEgKGV-IVISSE-LPELLGMCDRIYVMNEGRITGELPR 488
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-204 |
5.91e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMI--------------KPTTGESYLKGEIIHAGCHelwnsVGYLVEIPYS 69
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksagshiellgRTVQREGRLARDIRKSRAN-----TGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 70 YPELTVWENLEITRR---------LRFIKDPSTVDSI--IEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILD 138
Cdd:PRK09984 98 VNRLSVLENVLIGALgstpfwrtcFSWFTREQKQRALqaLTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 139 EPSNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI-----QEMDAKKLHQL 204
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFydgssQQFDNERFDHL 248
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-192 |
1.13e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGEsYLKGEiihAGCHELWNSVGYLVEIPYSYPELTVWEN-- 78
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGT---APLAEAREDTRLMFQDARLLPWKKVIDNvg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEITRRLRfikdpstvDSIIEKLKLTPYKDRKAK---NLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:PRK11247 104 LGLKGQWR--------DAALQALAAVGLADRANEwpaALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 2032538500 156 LRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:PRK11247 176 IESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-172 |
1.93e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGEsylkgeiIHAGCHelwnsvgylVEIPY--SY-----PELT 74
Cdd:PRK11147 336 KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR-------IHCGTK---------LEVAYfdQHraeldPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENL-------EITRRLR--------FIKDPstvdsiieKLKLTPykdrkAKNLSLGNSQRLGLAKALIHNPEILILDE 139
Cdd:PRK11147 400 VMDNLaegkqevMVNGRPRhvlgylqdFLFHP--------KRAMTP-----VKALSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|...
gi 2032538500 140 PSNGLDpagiVEIRELLRDLAFNKGVTIFISSH 172
Cdd:PRK11147 467 PTNDLD----VETLELLEELLDSYQGTVLLVSH 495
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-172 |
1.94e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 11 GEIYGFLGLNGAGKTTTIRMLLGMIKpttgESYLKGEIIHAG---CHELWNSVGYLVEIPYSYPELTVWENLEITRRLRF 87
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQ----GNNFTGTILANNrkpTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 88 IKDPS------TVDSIIEKLKLTpykdrKAKNLSLGNS----------QRLGLAKALIHNPEILILDEPSNGLDPAGIVE 151
Cdd:PLN03211 170 PKSLTkqekilVAESVISELGLT-----KCENTIIGNSfirgisggerKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180
....*....|....*....|.
gi 2032538500 152 IRELLRDLAfNKGVTIFISSH 172
Cdd:PLN03211 245 LVLTLGSLA-QKGKTIVTSMH 264
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-198 |
2.85e-13 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 67.52 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVEIPY------------ 68
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvDISKIGLHDLRSRISIIPQDPVlfsgtirsnldp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 69 --SYPELTVWENLEITRRLRFIKD-PSTVDSIIEklkltpykdRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:cd03244 101 fgEYSDEELWQALERVGLKEFVESlPGGLDTVVE---------EGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032538500 146 PAGIVEIRELLRDlAFnKGVTIFISSHllgeisRIAT-----RIGIIHEGKLIqEMDA 198
Cdd:cd03244 172 PETDALIQKTIRE-AF-KDCTVLTIAH------RLDTiidsdRILVLDKGRVV-EFDS 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-194 |
3.71e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIH----AGCHELWNSVGYLVEIPYSY--PELT 74
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspGKLQALRRDIQFIFQDPYASldPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 V----WENLEITRRLRFIKDPSTVDSIIEKLKLTP-YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGI 149
Cdd:PRK10261 420 VgdsiMEPLRVHGLLPGKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2032538500 150 VEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-197 |
5.95e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGEsylkgeIIHAGCHELWNSVGYLVEIPYSypELTVweNLE 80
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGT------IEWIFKDEKNKKKTKEKEKVLE--KLVI--QKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFIKD-----------------PSTVDSII------------EKLKLT-----------PYKDRKAKNLSLGNSQ 120
Cdd:PRK13651 93 RFKKIKKIKEirrrvgvvfqfaeyqlfEQTIEKDIifgpvsmgvskeEAKKRAakyielvgldeSYLQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 121 RLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLaFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMD 197
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-145 |
7.92e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.22 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIihagchelwnSVGYLVEIPYSYPELTVWENLE- 80
Cdd:PRK11819 24 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGI----------KVGYLPQEPQLDPEKTVRENVEe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 -------ITRRLRFI---------------------------KDPSTVDSIIEK----LKLTPyKDRKAKNLSLGNSQRL 122
Cdd:PRK11819 94 gvaevkaALDRFNEIyaayaepdadfdalaaeqgelqeiidaADAWDLDSQLEIamdaLRCPP-WDAKVTKLSGGERRRV 172
|
170 180
....*....|....*....|...
gi 2032538500 123 GLAKALIHNPEILILDEPSNGLD 145
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-198 |
7.94e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 68.17 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIkPTTGESYLKGEIIHAGCHELWNSVGYLVEI----PYSY--PELTV 75
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVvfqdPFGSlsPRMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 W----ENLEI--------TRRLRfikdpstVDSIIEKLKLTP-YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSN 142
Cdd:COG4172 382 GqiiaEGLRVhgpglsaaERRAR-------VAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 143 GLDPAGIVEIRELLRDLAFNKGVT-IFIsSHLLGEISRIATRIGIIHEGKLIQEMDA 198
Cdd:COG4172 455 ALDVSVQAQILDLLRDLQREHGLAyLFI-SHDLAVVRALAHRVMVMKDGKVVEQGPT 510
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-201 |
9.40e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 5 SLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE----------------IIHagcHELwNSVgylveipy 68
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfngpkssqeagigIIH---QEL-NLI-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 69 syPELTVWENL----EITRRLRFI---KDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPS 141
Cdd:PRK10762 92 --PQLTIAENIflgrEFVNRFGRIdwkKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 142 NGL----DPAGIVEIRElLRDlafnKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK10762 170 DALtdteTESLFRVIRE-LKS----QGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-194 |
1.14e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.18 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYL-------------VEIPYSY 70
Cdd:PRK13631 45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYskkiknfkelrrrVSMVFQF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 71 PELTVWENlEITRRLRF---------IKDPSTVDSIIEKLKL-TPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEP 140
Cdd:PRK13631 125 PEYQLFKD-TIEKDIMFgpvalgvkkSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEP 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 141 SNGLDPAGIVEIRELLRDlAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:PRK13631 204 TAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-172 |
1.16e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.89 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 10 KGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGE-----------SYLKGEIIHAGCHELWNS-------VGYLVEIPYSYp 71
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdevlKRFRGTELQDYFKKLANGeikvahkPQYVDLIPKVF- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 72 ELTVWENLEITrrlrfiKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDpagive 151
Cdd:COG1245 177 KGTVRELLEKV------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD------ 244
|
170 180
....*....|....*....|....*..
gi 2032538500 152 IRE------LLRDLAfNKGVTIFISSH 172
Cdd:COG1245 245 IYQrlnvarLIRELA-EEGKYVLVVEH 270
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-182 |
1.39e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.88 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHE---LWNSVGYLveipysyPELTVWE 77
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvVFQNEGLL-------PWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITRRLRFIKDPSTVDSIIEKLK---LTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRE 154
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKkvgLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180
....*....|....*....|....*...
gi 2032538500 155 LLRDLAFNKGVTIFISSHLLGEISRIAT 182
Cdd:PRK11248 170 LLLKLWQETGKQVLLITHDIEEAVFMAT 197
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-201 |
2.33e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIH-----------AGCHELWNSVGYLVEIPYS 69
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 70 Y---PELTVWEN--------LEITR---RLRFIKDPSTVdSIIEKLKltpykDRKAKNLSLGNSQRLGLAKALIHNPEIL 135
Cdd:PRK10619 101 FnlwSHMTVLENvmeapiqvLGLSKqeaRERAVKYLAKV-GIDERAQ-----GKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032538500 136 ILDEPSNGLDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-172 |
2.34e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.06 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGmiKPTTGesYLKGEIIHAGCHELWNS----VGYLVEIPYSYPELTVW 76
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG--VITGGDRLVNGRPLDSSfqrsIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRFIKDPST------VDSIIEKLKLTPYKDR----KAKNLSLGNSQRLGLAKALIHNPEILI-LDEPSNGLD 145
Cdd:TIGR00956 855 ESLRFSAYLRQPKSVSKsekmeyVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
170 180
....*....|....*....|....*..
gi 2032538500 146 PAGIVEIRELLRDLAfNKGVTIFISSH 172
Cdd:TIGR00956 935 SQTAWSICKLMRKLA-DHGQAILCTIH 960
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1-195 |
3.19e-12 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 64.56 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNSVGYLveipysyPELTVWENL 79
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdIREVTLDSLRRAIGVV-------PQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRRLRFIKDPSTVDSIIEKLKL---------------TPYKDRKAKnLSLGNSQRLGLAKALIHNPEILILDEPSNGL 144
Cdd:cd03253 90 TIGYNIRYGRPDATDEEVIEAAKAaqihdkimrfpdgydTIVGERGLK-LSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 145 DPAGIVEIRELLRDLAFNKgVTIFIsSHLLGEISRiATRIGIIHEGKLIQE 195
Cdd:cd03253 169 DTHTEREIQAALRDVSKGR-TTIVI-AHRLSTIVN-ADKIIVLKDGRIVER 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
18-193 |
3.97e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.67 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 18 GLNGAGKTTTIRMLLGMIKPTTGEsylkgeiIHAGCHELWNS------------VGYLVEIPYSYPELTVWENLE--ITR 83
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGR-------IVLNGRVLFDAekgiclppekrrIGYVFQDARLFPHYKVRGNLRygMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 84 rlrfiKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDpagIVEIREL---LRDLA 160
Cdd:PRK11144 104 -----SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD---LPRKRELlpyLERLA 175
|
170 180 190
....*....|....*....|....*....|...
gi 2032538500 161 FNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:PRK11144 176 REINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-194 |
4.30e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 5 SLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGE--------SYLKGEIIHAGCHELW--NSVGYLVEipysYPELT 74
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDEWqrNNTDMLSP----GEDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 75 VWENLEITrrLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRE 154
Cdd:PRK10938 99 GRTTAEII--QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2032538500 155 LLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQ 194
Cdd:PRK10938 177 LLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
92-193 |
4.62e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 92 STVDSIIEKLKLTPykDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLafnKGVTIFIsS 171
Cdd:PRK11147 137 NRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGSIIFI-S 210
|
90 100
....*....|....*....|..
gi 2032538500 172 HLLGEISRIATRIGIIHEGKLI 193
Cdd:PRK11147 211 HDRSFIRNMATRIVDLDRGKLV 232
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
95-280 |
6.09e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.14 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 95 DSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAfNKGVTIFISSHLL 174
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYM 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 175 GEISRIATRIGIIHEGKLIQEMDAKKLH-QLRNRTLFI------DLEDKKGAqslLANEGFD-----STITEEGLIE--I 240
Cdd:NF000106 205 EEAEQLAHELTVIDRGRVIADGKVDELKtKVGGRTLQIrpahaaELDRMVGA---IAQAGLDgiagaTADHEDGVVNvpI 281
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2032538500 241 TSEKALihpEDVNSNLVKAGFSPSMLKVEEEELESYFLRI 280
Cdd:NF000106 282 VSDEQL---SAVVGMLGERGFTISGHQHPSAQL*EVFLAI 318
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-204 |
7.06e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIhagcHELWNS---------VGYLVEIPYSYP 71
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV----ATLDADalaqlrrehFGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 72 ELTVWENLEI----------TRRLRFIkdpstvdSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPS 141
Cdd:PRK10535 100 HLTAAQNVEVpavyaglerkQRLLRAQ-------ELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 142 NGLDPAGIVEIRELLRDLAfNKGVTIFISSHlLGEISRIATRIGIIHEGKLIQEMDAKKLHQL 204
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLR-DRGHTVIIVTH-DPQVAAQAERVIEIRDGEIVRNPPAQEKVNV 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-165 |
9.33e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 10 KGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGES-----------YLKGEIIHAGCHELWNS-------VGYLVEIPySYP 71
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTELQNYFKKLYNGeikvvhkPQYVDLIP-KVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 72 ELTVWENLEIT-RRLRFikdpstvDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDpagiv 150
Cdd:PRK13409 177 KGKVRELLKKVdERGKL-------DEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD----- 244
|
170 180
....*....|....*....|.
gi 2032538500 151 eIRE------LLRDLAFNKGV 165
Cdd:PRK13409 245 -IRQrlnvarLIRELAEGKYV 264
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-194 |
9.93e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 62.81 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYlveIPYSyPEL---TVW 76
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGiDISTIPLEDLRSSLTI---IPQD-PTLfsgTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITrrlrfikDPSTVDSIIEKLKLTpykdRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELL 156
Cdd:cd03369 100 SNLDPF-------DEYSDEEIYGALRVS----EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 2032538500 157 RDLAfnKGVTIFISSHLLGEISRIAtRIGIIHEGKLIQ 194
Cdd:cd03369 169 REEF--TNSTILTIAHRLRTIIDYD-KILVMDAGEVKE 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-191 |
1.04e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 62.49 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGeiihagchelwnSVGYLVEIPYSYPElTVWENle 80
Cdd:cd03250 21 LKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG-TIREN-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFikDPSTVDSIIEK------LKLTPYKDR-----KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDP--- 146
Cdd:cd03250 86 ILFGKPF--DEERYEKVIKAcalepdLEILPDGDLteigeKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAhvg 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2032538500 147 AGIVE--IRELLRDlafnkGVTIFISSHLLGEISRiATRIGIIHEGK 191
Cdd:cd03250 164 RHIFEncILGLLLN-----NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
114-207 |
1.92e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.08 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 114 LSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNKGVtIFIsSHLLGEISRIaTRIGIIHEGKLI 193
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV-LMI-THRLTGLEQF-DRICVMDNGQII 552
|
90
....*....|....
gi 2032538500 194 QEMDAKKLHQLRNR 207
Cdd:PRK11160 553 EQGTHQELLAQQGR 566
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-203 |
2.78e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII--HAGCHELWNSVGYLVEIPYS---YPELTV 75
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAINHGFALVTEERRStgiYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLEI---------TRRLRFIKDPSTVDSIIEKLKL-TPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:PRK10982 344 GFNSLIsnirnyknkVGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032538500 146 PAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQ 203
Cdd:PRK10982 424 VGAKFEIYQLIAELA-KKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQ 480
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-190 |
3.25e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.80 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWN---------------------SVGY 62
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdiqmifqdplaslnprmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 63 LVEIPYS--YPELTVWEnleitrrlrfIKDpsTVDSIIEKLKLTP-YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDE 139
Cdd:PRK15079 120 IIAEPLRtyHPKLSRQE----------VKD--RVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 140 PSNGLDPAGIVEIRELLRDLAFNKGVT-IFIsSHLLGEISRIATRIGIIHEG 190
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSlIFI-AHDLAVVKHISDRVLVMYLG 238
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-181 |
5.50e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.90 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLgMI-KPTTGESYLKGEII----HAGCHELWNSVGYLVEIPYSY--PELTVW 76
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLT-MIeTPTGGELYYQGQDLlkadPEAQKLLRQKIQIVFQNPYGSlnPRKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ----ENLEITRRLRFIKDPSTVDSIIEKLKLTP-YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDpagiVE 151
Cdd:PRK11308 113 qileEPLLINTSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD----VS 188
|
170 180 190
....*....|....*....|....*....|....*
gi 2032538500 152 IR----ELLRDLAFNKGVT-IFIsSHLLGEISRIA 181
Cdd:PRK11308 189 VQaqvlNLMMDLQQELGLSyVFI-SHDLSVVEHIA 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-207 |
6.59e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.43 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHE-LWNSVGYLVEIPY----------- 68
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvLRQGVAMVQQDPVvladtflanvt 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 69 ---SYPELTVWENLEITRRLRFIKDPStvDSIIEKLkltpykDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:PRK10790 437 lgrDISEEQVWQALETVQLAELARSLP--DGLYTPL------GEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 146 PAGIVEIRELLRdlAFNKGVTIFISSHLLGEISRiATRIGIIHEGKLIQEMDAKKLHQLRNR 207
Cdd:PRK10790 509 SGTEQAIQQALA--AVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQGR 567
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-201 |
9.44e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 9.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIkPTTGESYLKGEIIHagcheLWNSVGYL---------VEIPYSY- 70
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLH-----NLNRRQLLpvrhriqvvFQDPNSSl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 71 -PELTVW----ENLEITRR-LRFIKDPSTVDSIIEKLKLTP-YKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:PRK15134 376 nPRLNVLqiieEGLRVHQPtLSAAQREQQVIAVMEEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2032538500 144 LDPAGIVEIRELLRDLAFNKGVT-IFIsSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAyLFI-SHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-158 |
1.29e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.46 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 11 GEIYGFLGLNGAGKTTTIRMLLGMIKPTTGE-----------SYLKGEIIHAGCHELWN-------SVGYLVEIPYSYpE 72
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeilDEFRGSELQNYFTKLLEgdvkvivKPQYVDLIPKAV-K 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 LTVWENLEITrrlrfiKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD-----PA 147
Cdd:cd03236 105 GKVGELLKKK------DERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqrlNA 178
|
170
....*....|.
gi 2032538500 148 GIVeIRELLRD 158
Cdd:cd03236 179 ARL-IRELAED 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-201 |
1.47e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIkPTTGESYLKGEI-------IHAGCHELWNSVGYLVEIPYSYP---- 71
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSPPVVYPSGDIrfhgeslLHASEQTLRGVRGNKIAMIFQEPmvsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 72 ------ELTVWENLEITRRLRFIKDPSTVDSIIEKLKLTPYKDRKAK---NLSLGNSQRLGLAKALIHNPEILILDEPSN 142
Cdd:PRK15134 106 nplhtlEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTT 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2032538500 143 GLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK15134 186 ALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-194 |
1.65e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.13 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA-GCHELWNSVGylveipysypelTVWE----- 77
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIA------------VVFQdaglf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITRRLRFIKDPSTVDSIIEKLKLTPYKD---RKAKN-----------LSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:PRK13657 422 NRSIEDNIRVGRPDATDEEMRAAAERAQAHDfieRKPDGydtvvgergrqLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 144 LDPAGIVEIRELLRDLAfnKGVTIFISSHLLGEIsRIATRIGIIHEGKLIQ 194
Cdd:PRK13657 502 LDVETEAKVKAALDELM--KGRTTFIIAHRLSTV-RNADRILVFDNGRVVE 549
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-201 |
1.87e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII--HAGCHELWNSVGYLVEIPYSYPELTVWENLEI 81
Cdd:PRK10982 17 VNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQELNLVLQRSVMDNMWL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 TRRLR---FI---KDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:PRK10982 97 GRYPTkgmFVdqdKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032538500 156 LRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK10982 177 IRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-172 |
1.97e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGesylkgeiihAGCHELWNSVgylveipySYPELTVWENLEI 81
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV----------AGCVDVPDNQ--------FGREASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 trrlrfIKDPSTVdsiIEKLKLTPYKD-----RKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELL 156
Cdd:COG2401 109 ------KGDFKDA---VELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL 179
|
170
....*....|....*.
gi 2032538500 157 RDLAFNKGVTIFISSH 172
Cdd:COG2401 180 QKLARRAGITLVVATH 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-195 |
2.05e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHE-----LWNSVGYLVEIPYSYPELTVWEN 78
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraklRAKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEITRRLRFIKDPSTVDS---IIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:PRK10584 109 VELPALLRGESSRQSRNGakaLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2032538500 156 LRDLAFNKGVTIFISSHLLGEISRIATRIGIIhEGKLIQE 195
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLAARCDRRLRLV-NGQLQEE 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-194 |
2.08e-10 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 60.89 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVE------------IPYSY 70
Cdd:TIGR02203 351 ISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhDLADYTLASLRRQVALVSQdvvlfndtiannIAYGR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 71 PELTVWEnlEITRRLRFIKDPSTVDSIIEKLKlTPYKDrKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIV 150
Cdd:TIGR02203 431 TEQADRA--EIERALAAAYAQDFVDKLPLGLD-TPIGE-NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2032538500 151 EIRELLRDLAfnKGVTIFISSHLLGEISRiATRIGIIHEGKLIQ 194
Cdd:TIGR02203 507 LVQAALERLM--QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVE 547
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-192 |
2.46e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.83 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEI----IHAGCHelwnsvgylveipysyPELTVW 76
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVsviaISAGLS----------------GQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRFIKD---PSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDP------- 146
Cdd:PRK13546 104 ENIEFKMLCMGFKRkeiKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQtfaqkcl 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032538500 147 AGIVEIREllrdlafnKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:PRK13546 184 DKIYEFKE--------QNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-172 |
3.53e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.02 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGmiKPTTGesYLKGEIIHAG---CHELWNSVGYLVEIPYSYPELTVWE 77
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAG--VITGEILINGrplDKNFQRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITRRLRfikdpstvdsiieklkltpykdrkakNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLR 157
Cdd:cd03232 99 ALRFSALLR--------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
170
....*....|....*
gi 2032538500 158 DLAfNKGVTIFISSH 172
Cdd:cd03232 153 KLA-DSGQAILCTIH 166
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-173 |
3.59e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.34 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 18 GLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLVEIPYsypELTVWENLEITRrlRFIKDPSTVDSI 97
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKL---EMTVFENLKFWS--EIYNSAETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032538500 98 IEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPagivEIRELLRDLAF---NKGVTIFISSHL 173
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK----ENRDLLNNLIVmkaNSGGIVLLSSHL 182
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-201 |
4.81e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE----IIHAGCHElwnsvgylveipysypELTVW 76
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaaliAISSGLNG----------------QLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRFIKDPST---VDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:PRK13545 104 ENIELKGLMMGLTKEKIkeiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2032538500 154 ELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK13545 184 DKMNEFK-EQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-206 |
5.37e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.92 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGM--IKPTTGESYLKGE-IIHAGCHE-LWNSVGYLVEIPYSYPELTVwE 77
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEdITDLPPEErARLGIFLAFQYPPEIPGVKN-A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLeitrrLRFIKDpstvdsiieklkltpykdrkakNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLR 157
Cdd:cd03217 96 DF-----LRYVNE----------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 158 DLAfNKGVTIFISSH---LLGEIsrIATRIGIIHEGKLIQEMDAKKLHQLRN 206
Cdd:cd03217 149 KLR-EEGKSVLIITHyqrLLDYI--KPDRVHVLYDGRIVKSGDKELALEIEK 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-184 |
5.78e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.56 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLkGEIIHagchelwnsVGYLVEIPYSY-PELTVWEnlEIT 82
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK---------LAYVDQSRDALdPNKTVWE--EIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 RRLRFIKdpstvdsiIEKLKLT--PYKDR----------KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDpagiV 150
Cdd:TIGR03719 409 GGLDIIK--------LGKREIPsrAYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD----V 476
|
170 180 190
....*....|....*....|....*....|....*.
gi 2032538500 151 EIRELLRD--LAFnKGVTIFIsSHLLGEISRIATRI 184
Cdd:TIGR03719 477 ETLRALEEalLNF-AGCAVVI-SHDRWFLDRIATHI 510
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-160 |
6.64e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.09 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchelwnsvgylVEiP-----------YS- 69
Cdd:PRK11650 21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE------------LE-PadrdiamvfqnYAl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 70 YPELTVWENL------------EITRRlrfIKDPSTVdsiiekLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILIL 137
Cdd:PRK11650 88 YPHMSVRENMayglkirgmpkaEIEER---VAEAARI------LELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180
....*....|....*....|....*....
gi 2032538500 138 DEP-SNgLDpAGI-----VEIRELLRDLA 160
Cdd:PRK11650 159 DEPlSN-LD-AKLrvqmrLEIQRLHRRLK 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-172 |
7.62e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIH---AGCHELWNSVGYLVEIPysyPELTVWE 77
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlCTYQKQLCFVGHRSGIN---PYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITrrLRFIKDPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLR 157
Cdd:PRK13540 94 NCLYD--IHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....*
gi 2032538500 158 DLAfNKGVTIFISSH 172
Cdd:PRK13540 172 EHR-AKGGAVLLTSH 185
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-150 |
9.32e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.47 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGmiKPTTGesYLKGEIIHAGC---HELWNSV-GYLVEIPYSYPELTVW 76
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEGDIRISGFpkkQETFARIsGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRFIKDPST------VDSIIEKLKLTPYKDR-----KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:PLN03140 972 ESLIYSAFLRLPKEVSKeekmmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
....*..
gi 2032538500 146 --PAGIV 150
Cdd:PLN03140 1052 arAAAIV 1058
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-190 |
1.29e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTtgesylKGEIIHAGchelwnSVGYLVEIPYSYPElTVWENLE 80
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS------EGKIKHSG------RISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFIKDPSTVDS--IIEKLKLTPYKDRK-----AKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:TIGR01271 509 FGLSYDEYRYTSVIKAcqLEEDIALFPEKDKTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
170 180 190
....*....|....*....|....*....|....*...
gi 2032538500 154 E-LLRDLAFNKgVTIFISSHLlgEISRIATRIGIIHEG 190
Cdd:TIGR01271 589 EsCLCKLMSNK-TRILVTSKL--EHLKKADKILLLHEG 623
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
98-201 |
1.96e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 98 IEKLKLTPYKDRKA------KNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNKGVTIFISS 171
Cdd:PRK15093 137 IELLHRVGIKDHKDamrsfpYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLIS 216
|
90 100 110
....*....|....*....|....*....|
gi 2032538500 172 HLLGEISRIATRIGIIHEGKLIQEMDAKKL 201
Cdd:PRK15093 217 HDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-193 |
2.14e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGEsyLKgeiihagchelW---NSVGYLVEIPYSYPE--LTVW 76
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT--VK-----------WsenANIGYYAQDHAYDFEndLTLF 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 77 ENLEITRRLRfiKDPSTVDSIIEKLKLTpyKD---RKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIveir 153
Cdd:PRK15064 403 DWMSQWRQEG--DDEQAVRGTLGRLLFS--QDdikKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI---- 474
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032538500 154 ELLrDLAFNK--GVTIFIsSHLLGEISRIATRIGIIHEGKLI 193
Cdd:PRK15064 475 ESL-NMALEKyeGTLIFV-SHDREFVSSLATRIIEITPDGVV 514
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-204 |
3.61e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 56.25 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGE-IIHAGCHELWNSVGYLVEIPY--SYPELTVWEN 78
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYKRAKYIGRVFQDPMmgTAPSMTIEEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 79 LEI------TRRLRFIKDPSTVDSIIEKLKLTP--YKDR---KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPA 147
Cdd:COG1101 103 LALayrrgkRRGLRRGLTKKRRELFRELLATLGlgLENRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 148 GIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQL 204
Cdd:COG1101 183 TAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEEKKKL 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-178 |
4.11e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.49 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELW-NSVGYLVEIPYSYPElTVWENLEIT 82
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYrQQVSYCAQTPTLFGD-TVYDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 RRLRFIK-DPSTVDSIIEKLKLTPYKDRKAKN-LSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLA 160
Cdd:PRK10247 105 WQIRNQQpDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYV 184
|
170
....*....|....*...
gi 2032538500 161 FNKGVTIFISSHLLGEIS 178
Cdd:PRK10247 185 REQNIAVLWVTHDKDEIN 202
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-172 |
4.16e-09 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 54.47 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKpttgesYLKGEIIHAGCHELWnsvgYLVEIPYsYPELTvwenlei 81
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP------WGSGRIGMPEGEDLL----FLPQRPY-LPLGT------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 trrLRfikdpstvDSIIeklklTPYKDRkaknLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLaf 161
Cdd:cd03223 80 ---LR--------EQLI-----YPWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL-- 137
|
170
....*....|.
gi 2032538500 162 nkGVTIFISSH 172
Cdd:cd03223 138 --GITVISVGH 146
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-203 |
4.86e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKP----TTGESYLKGEIIHA----GCHelwnsVGYLVEIPYSY--PEL 73
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPcalrGRK-----IATIMQNPRSAfnPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 TVWENLEITrrLRFIKDPSTVDSIIEKLKLTPYKDRK------AKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPA 147
Cdd:PRK10418 97 TMHTHARET--CLALGKPADDATLTAALEAVGLENAArvlklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2032538500 148 GIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLIQEMDAKKLHQ 203
Cdd:PRK10418 175 AQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-172 |
7.47e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAgchelwnsvgylvEIPYSYPEL--TVWENLEI 81
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-------------EQPEDYRKLfsAVFTDFHL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 82 TRRL----RFIKDPSTVDSIIEKLKL---TPYKDRKAKNLSL--GNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEI 152
Cdd:PRK10522 409 FDQLlgpeGKPANPALVEKWLERLKMahkLELEDGRISNLKLskGQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180
....*....|....*....|
gi 2032538500 153 RELLRDLAFNKGVTIFISSH 172
Cdd:PRK10522 489 YQVLLPLLQEMGKTIFAISH 508
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-145 |
9.73e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 5 SLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGEsyLKgeiihagchelwnsVGYLVEIpySY---------PELTV 75
Cdd:PRK11819 344 SFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT--IK--------------IGETVKL--AYvdqsrdaldPNKTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WEnlEITRRLRFIK-----DPSTVdsiieklkltpYKDR----------KAKNLSLGNSQRLGLAKALIHNPEILILDEP 140
Cdd:PRK11819 406 WE--EISGGLDIIKvgnreIPSRA-----------YVGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
....*
gi 2032538500 141 SNGLD 145
Cdd:PRK11819 473 TNDLD 477
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-218 |
1.04e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.11 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVEIPY----------- 68
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlNIAKIGLHDLRFKITIIPQDPVlfsgslrmnld 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 69 ---SYPELTVWENLEITRRLRFikdpstVDSIIEKLKLTPYKDrkAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:TIGR00957 1382 pfsQYSDEEVWWALELAHLKTF------VSALPDKLDHECAEG--GENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 146 PAGIVEIRELLRDlAFNKgVTIFISSHLLGEISRIaTRIGIIHEGKlIQEMDAKKlHQLRNRTLFIDLEDKKG 218
Cdd:TIGR00957 1454 LETDNLIQSTIRT-QFED-CTVLTIAHRLNTIMDY-TRVIVLDKGE-VAEFGAPS-NLLQQRGIFYSMAKDAG 1521
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-187 |
1.15e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTtgesylKGEIIHAGCHEL-------WNS-VGYLVEIP------ 67
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT------EGDIIINDSHNLkdinlkwWRSkIGVVSQDPllfsns 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 68 ---------YSYPELTVWEN---------------------------------------LEITRRLRFIKDPSTVDS--- 96
Cdd:PTZ00265 476 iknnikyslYSLKDLEALSNyynedgndsqenknkrnscrakcagdlndmsnttdsnelIEMRKNYQTIKDSEVVDVskk 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 97 --IIEKLKLTPYK-----DRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNKGVTIFI 169
Cdd:PTZ00265 556 vlIHDFVSALPDKyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITII 635
|
250
....*....|....*...
gi 2032538500 170 SSHLLGEIsRIATRIGII 187
Cdd:PTZ00265 636 IAHRLSTI-RYANTIFVL 652
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-275 |
1.16e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPttgesylkgeiIHAGCHELWNSVGYLVEIPYSYpELTVWENL- 79
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------AETSSVVIRGSVAYVPQVSWIF-NATVRENIl 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 -----EITRRLRFIKdpstVDSIIEKLKLTPYKDR-----KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGI 149
Cdd:PLN03232 701 fgsdfESERYWRAID----VTALQHDLDLLPGRDLteigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 150 VEIRE--LLRDLAFNKGVTIFISSHLLGEISRIAtrigIIHEGKLIQEMDAKKLHqlRNRTLFidledkkgaQSLLANEG 227
Cdd:PLN03232 777 HQVFDscMKDELKGKTRVLVTNQLHFLPLMDRII----LVSEGMIKEEGTFAELS--KSGSLF---------KKLMENAG 841
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 228 -FDSTI---TEEGLIEITSEKALIHPEDVNSNLVKAGFSPSMLKVEEEELES 275
Cdd:PLN03232 842 kMDATQevnTNDENILKLGPTVTIDVSERNLGSTKQGKRGRSVLVKQEERET 893
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
111-172 |
6.34e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.27 E-value: 6.34e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 111 AKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNkgvTIFIS-SH 172
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG---TTVISvGH 542
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-145 |
9.22e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.92 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIkPTTGESYLKGEIIHAGCHELW-NSVGYLVEIPySYPELTVWENLEIT 82
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWrKHLSWVGQNP-QLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 83 R------RLRFIKDPSTVDSIIEKLKL---TPYKDRKAKnLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:PRK11174 447 NpdasdeQLQQALENAWVSEFLPLLPQgldTPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
8-191 |
2.03e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 8 VDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGEsylkgeiihagchelwnsvgylveipysypelTVWENLEITRRLRF 87
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN--------------------------------DEWDGITPVYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 88 IKdpstvdsiieklkltpykdrkaknLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNKGVTI 167
Cdd:cd03222 70 ID------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
170 180
....*....|....*....|....
gi 2032538500 168 FISSHLLGEISRIATRIgIIHEGK 191
Cdd:cd03222 126 LVVEHDLAVLDYLSDRI-HVFEGE 148
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1-190 |
2.48e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.01 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTtgesylKGEIIHAGchelwnSVGYLVEIPYSYPElTVWENLE 80
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS------EGKIKHSG------RISFSSQFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 81 ITRRLRFIKDPSTVDS--IIEKLKLTPYKDRK-----AKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIR 153
Cdd:cd03291 120 FGVSYDEYRYKSVVKAcqLEEDITKFPEKDNTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIF 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 2032538500 154 E-LLRDLAFNKgVTIFISSHLlgEISRIATRIGIIHEG 190
Cdd:cd03291 200 EsCVCKLMANK-TRILVTSKM--EHLKKADKILILHEG 234
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-203 |
2.71e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.64 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWNSVGYLV-EIPYSYPElTVWENL 79
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVsQTPFLFSD-TVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRrlrfikdPSTVDSIIEK-----------LKL-----TPYKDRKAKnLSLGNSQRLGLAKALIHNPEILILDEPSNG 143
Cdd:PRK10789 410 ALGR-------PDATQQEIEHvarlasvhddiLRLpqgydTEVGERGVM-LSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032538500 144 LDpaGIVEiRELLRDLA-FNKGVTIFISSHLLGEISRiATRIGIIHEGKLIQEMDAKKLHQ 203
Cdd:PRK10789 482 VD--GRTE-HQILHNLRqWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
114-193 |
4.68e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 50.84 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 114 LSLGNSQRLGLAKALIHNPEILILDEPSNGLDpagiV----EIRELLRDL--AFNKGVtIFIsSHLLGEISRIATRIGII 187
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALD----VtvqaQILDLLKDLqrELGMAL-LLI-THDLGVVRRFADRVAVM 230
|
....*.
gi 2032538500 188 HEGKLI 193
Cdd:COG4172 231 RQGEIV 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-179 |
7.09e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 78 NLEITRRLRFIKDPST------------VDSIIEKL------KLTPYkdrkAKNLSLGNSQRLGLAKALIHNPEILILDE 139
Cdd:PTZ00265 1309 NMSIYENIKFGKEDATredvkrackfaaIDEFIESLpnkydtNVGPY----GKSLSGGQKQRIAIARALLREPKILLLDE 1384
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2032538500 140 PSNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISR 179
Cdd:PTZ00265 1385 ATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-272 |
8.55e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGesylkGEIIHAGchelwnSVGYLVEIPYSYpELTVWENL---- 79
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-----ASVVIRG------TVAYVPQVSWIF-NATVRDNIlfgs 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 --EITRRLRFIKdpstVDSIIEKLKLTPYKD-----RKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDP--AGIV 150
Cdd:PLN03130 704 pfDPERYERAID----VTALQHDLDLLPGGDlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhvGRQV 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 151 -------EIRELLRDLAFNKgvtifisSHLLGEISRIAtrigIIHEGKLIQEMDAKKLhqLRNRTLFIDLEDKKGAQSLL 223
Cdd:PLN03130 780 fdkcikdELRGKTRVLVTNQ-------LHFLSQVDRII----LVHEGMIKEEGTYEEL--SNNGPLFQKLMENAGKMEEY 846
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2032538500 224 ANEGFDSTITEEGLIEITSEKALIHPEDVNSNLVKAGFSPSMLKVEEEE 272
Cdd:PLN03130 847 VEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERE 895
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1-145 |
8.81e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 48.87 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHAGCHELWN-----SVGYLVEIPYSYpELTV 75
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrySVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLEI-----TRRLRFIKDPSTVDSIIEklkLTPYKDR-----KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:cd03290 96 EENITFgspfnKQRYKAVTDACSLQPDID---LLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
114-201 |
9.48e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 114 LSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
....*...
gi 2032538500 194 QEMDAKKL 201
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-172 |
9.57e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKpTTGESYLKGEIihagchelWNSV-------GYLVeIPYSYPEL 73
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVS--------WNSVtlqtwrkAFGV-IPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 T-----------VWENLEITRrlrfIKDPSTVDSIIEKL--KLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEP 140
Cdd:TIGR01271 1305 SgtfrknldpyeQWSDEEIWK----VAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190
....*....|....*....|....*....|..
gi 2032538500 141 SNGLDPAGIVEIRELLRDLAFNkgVTIFISSH 172
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLKQSFSN--CTVILSEH 1410
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-195 |
1.01e-06 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 49.03 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEII---HAGCHE----------------------- 55
Cdd:COG4598 25 KGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkPDRDGElvpadrrqlqrirtrlgmvfqsf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 56 -LWnsvgylveipysyPELTVWENLeitrrlrfIKDPSTV------------DSIIEKLKLTPYKDRKAKNLSLGNSQRL 122
Cdd:COG4598 105 nLW-------------SHMTVLENV--------IEAPVHVlgrpkaeaieraEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 123 GLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAfNKGVTIFISSHLLGEISRIATRIGIIHEGkLIQE 195
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLA-EEGRTMLVVTHEMGFARDVSSHVVFLHQG-RIEE 234
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
59-172 |
1.41e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.02 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 59 SVGYLVEIpYSYPELtVWENLEITRRLRFIKDPStvdsiIEKLKLtpykDRKAKNLSLGNSQRLGLAKALIHNPE--ILI 136
Cdd:cd03270 94 TVGTVTEI-YDYLRL-LFARVGIRERLGFLVDVG-----LGYLTL----SRSAPTLSGGEAQRIRLATQIGSGLTgvLYV 162
|
90 100 110
....*....|....*....|....*....|....*.
gi 2032538500 137 LDEPSNGLDPAGIVEIRELLRDLAfNKGVTIFISSH 172
Cdd:cd03270 163 LDEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVVEH 197
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-210 |
1.44e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.70 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIkpttgesYLKGEIIHAGCHelWNSV---------GYLVEI----- 66
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-------NTEGDIQIDGVS--WNSVplqkwrkafGVIPQKvfifs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 67 --------PYSYpeltvWENLEITRrlrfIKDPSTVDSIIEKL--KLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILI 136
Cdd:cd03289 91 gtfrknldPYGK-----WSDEEIWK----VAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032538500 137 LDEPSNGLDPAGIVEIRELLRDlAFnKGVTIFISSHLLgEISRIATRIGIIHEGKLIQEMDAKKLhqLRNRTLF 210
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQ-AF-ADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKL--LNEKSHF 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-145 |
1.57e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.56 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGeiihagchelwnSVGYLVEIPYsYPELTVWENLEITR 83
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQAW-IQNDSLRENILFGK 723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032538500 84 RLRFIKDPSTVDS--IIEKLKLTPYKDR-----KAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:TIGR00957 724 ALNEKYYQQVLEAcaLLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
80-193 |
2.16e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRRLRFIkDPSTVD----SIIEKLKLTPYKDRKA-KNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRE 154
Cdd:PLN03073 307 EIYKRLELI-DAYTAEaraaSILAGLSFTPEMQVKAtKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLET 385
|
90 100 110
....*....|....*....|....*....|....*....
gi 2032538500 155 LLrdLAFNKgvTIFISSHLLGEISRIATRIGIIHEGKLI 193
Cdd:PLN03073 386 YL--LKWPK--TFIVVSHAREFLNTVVTDILHLHGQKLV 420
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
10-184 |
2.19e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 10 KGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESylkgeiihagchelwnsvgylveipysypeltvwenleitrrlrFIK 89
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------------------IYI 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 90 DPSTVDSIIEKLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAF-----NKG 164
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKN 116
|
170 180
....*....|....*....|
gi 2032538500 165 VTIFISSHLLGEISRIATRI 184
Cdd:smart00382 117 LTVILTTNDEKDLGPALLRR 136
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
109-194 |
7.56e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 109 RKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLA--FNKGVtIFIsSHLLGEISRIATRIGI 186
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkeMSMGV-IFI-THDMGVVAEIADRVLV 241
|
....*...
gi 2032538500 187 IHEGKLIQ 194
Cdd:PRK10261 242 MYQGEAVE 249
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
108-172 |
9.35e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.01 E-value: 9.35e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032538500 108 DRKAKNLSLGNSQRLGLAKALIHNPE--ILILDEPSNGLDPAGIVEIRELLRDLAfNKGVTIFISSH 172
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLI-DLGNTVILIEH 147
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
114-194 |
1.08e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.55 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 114 LSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAFNKgvTIFISSHLLGEISRiATRIGIIHEGKLI 193
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
.
gi 2032538500 194 Q 194
Cdd:PRK11176 558 E 558
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
114-172 |
1.60e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.60e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032538500 114 LSLGNsQRLGL-AKALIHNPEILILDEPSNGLDPAGiveiRELLR---DLAFNKGVT--IFISSH 172
Cdd:PRK10938 402 LSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLN----RQLVRrfvDVLISEGETqlLFVSHH 461
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-145 |
1.89e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYL-KGeiIHAGC---HELwnsvGYLVEIPYSYPELTVWENL 79
Cdd:PRK10636 331 IKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKG--IKLGYfaqHQL----EFLRADESPLQHLARLAPQ 404
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 80 EITRRLR-------FIKDpstvdsiieklKLTPYKDRkaknLSLGNSQRLGLAKALIHNPEILILDEPSNGLD 145
Cdd:PRK10636 405 ELEQKLRdylggfgFQGD-----------KVTEETRR----FSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-193 |
2.67e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.18 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGesyLKGEIIHAGCHELWNSVGYLVEIPYS------YPELTV 75
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS---VEGDIHYNGIPYKEFAEKYPGEIIYVseedvhFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 76 WENLEITRRLRfikdpstvdsiieklkltpyKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIREL 155
Cdd:cd03233 101 RETLDFALRCK--------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2032538500 156 LRDLAFNKGVTIFISshLL---GEISRIATRIGIIHEGKLI 193
Cdd:cd03233 161 IRTMADVLKTTTFVS--LYqasDEIYDLFDKVLVLYEGRQI 199
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-191 |
4.49e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.33 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 3 EISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKP---TTGESYLKG-EIIHAGCHEL----WNSVGYLVEIPYSY--PE 72
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGrEILNLPEKELnklrAEQISMIFQDPMTSlnPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 73 LTVWENL-----------------EITRRLRFIKDPSTVdsiiEKLKLTPYKdrkaknLSLGNSQRLGLAKALIHNPEIL 135
Cdd:PRK09473 114 MRVGEQLmevlmlhkgmskaeafeESVRMLDAVKMPEAR----KRMKMYPHE------FSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2032538500 136 ILDEPSNGLDPAGIVEIRELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGK 191
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
121-172 |
7.80e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 7.80e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2032538500 121 RLGLAKALIHNPEILILDEPSNGLDpagIVEIReLLRDLAFNKGVTIFISSH 172
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD---INTIR-WLEDVLNERNSTMIIISH 210
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-147 |
1.56e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.20 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 1 MKEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVEIPYSY--------- 70
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTLRSRLSIILQDPILFsgsirfnld 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 71 PEL-----TVWENLEITRRLRFIKD-PSTVDSIIEKlkltpykdrKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGL 144
Cdd:cd03288 117 PECkctddRLWEALEIAQLKNMVKSlPGGLDAVVTE---------GGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
...
gi 2032538500 145 DPA 147
Cdd:cd03288 188 DMA 190
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
113-172 |
1.64e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.38 E-value: 1.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 113 NLSLGNSQRLGLAKALI---HNPEILILDEPSNGLDPAGIVEIRELLRDLAfNKGVTIFISSH 172
Cdd:pfam13304 236 ELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELS-RNGAQLILTTH 297
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-197 |
2.17e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYlveIPYSyPELtvwenleIT 82
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcDISKFGLMDLRKVLGI---IPQA-PVL-------FS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 83 RRLRFIKDP----STVDsIIEKLKLTPYKD--RK------------AKNLSLGNSQRLGLAKALIHNPEILILDEPSNGL 144
Cdd:PLN03130 1327 GTVRFNLDPfnehNDAD-LWESLERAHLKDviRRnslgldaevseaGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 145 DPAGIVEIRELLRDlAFnKGVTIFISSHLLGEISRiATRIGIIHEGKlIQEMD 197
Cdd:PLN03130 1406 DVRTDALIQKTIRE-EF-KSCTMLIIAHRLNTIID-CDRILVLDAGR-VVEFD 1454
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
115-194 |
3.05e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.45 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 115 SLGNSQRLGLAKALIHNPEILILDEPSNGLDPAgiVEIR--ELLRDLAFNKGVTIFISSHLLGEISRIATRIGIIHEGKL 192
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS--VQARllDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
..
gi 2032538500 193 IQ 194
Cdd:PRK11701 231 VE 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-194 |
7.23e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 4 ISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKG-EIIHAGCHELWNSVGYLVEIPYSYP----------- 71
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcDVAKFGLTDLRRVLSIIPQSPVLFSgtvrfnidpfs 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 72 ---ELTVWENLEITRrlrfIKDPSTVDSiiekLKLTPYKDRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAG 148
Cdd:PLN03232 1335 ehnDADLWEALERAH----IKDVIDRNP----FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032538500 149 IVEIRELLRDlAFnKGVTIFISSHLLGEISRiATRIGIIHEGKLIQ 194
Cdd:PLN03232 1407 DSLIQRTIRE-EF-KSCTMLVIAHRLNTIID-CDKILVLSSGQVLE 1449
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
122-172 |
9.80e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 9.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 122 LGLAKALIHN--PEILILDEPSNGLDPAGIVEIRELLRDLAfnKGVTIFISSH 172
Cdd:COG4637 267 LALLAALLSPrpPPLLCIEEPENGLHPDLLPALAELLREAS--ERTQVIVTTH 317
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-192 |
1.91e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 2 KEISLNVDKGEIYGFLGLNGAGKTTTIRMLLGMIKPTTGESYLKGEIIHA--------GCHELWNSVGYLVEIPYSYPEl 73
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAvfsqhhvdGLDLSSNPLLYMMRCFPGVPE- 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 74 tvwenleitRRLRfikdpSTVDS--IIEKLKLTPykdrkAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDpagIVE 151
Cdd:PLN03073 605 ---------QKLR-----AHLGSfgVTGNLALQP-----MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDA 662
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032538500 152 IRELLRDLAFNKGVTIFIS--SHLlgeISRIATRIGIIHEGKL 192
Cdd:PLN03073 663 VEALIQGLVLFQGGVLMVShdEHL---ISGSVDELWVVSEGKV 702
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-170 |
2.24e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.71 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 11 GEIYGFLGLNGAGKTTtirmllgMIKPTTGESY-----LKGEIIHAGC--HELWN----SVGYLVEIPYSYPELTVWENL 79
Cdd:TIGR00956 87 GELTVVLGRPGSGCST-------LLKTIASNTDgfhigVEGVITYDGItpEEIKKhyrgDVVYNAETDVHFPHLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 80 EITRRLR-------------FIKdpSTVDSIIEKLKLTPYKDRKAKN-----LSLGNSQRLGLAKALIHNPEILILDEPS 141
Cdd:TIGR00956 160 DFAARCKtpqnrpdgvsreeYAK--HIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170 180
....*....|....*....|....*....
gi 2032538500 142 NGLDPAGIVEIRELLRDLAFNKGVTIFIS 170
Cdd:TIGR00956 238 RGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
108-170 |
4.34e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.61 E-value: 4.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032538500 108 DRKAKNLSLGNSQRLGLAKALIHNPEILILDEPSNGLDPAGIVEIRELLRDLAfnkGVTIFIS 170
Cdd:PRK10636 144 ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQ---GTLILIS 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
18-172 |
5.76e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.20 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 18 GLNGAGKTTTIRMLL----GMIKPTTGESYLKGEIIHAGchelwnSVGYLVEIPYsypELTVWENLEITRRLRFIkdpst 93
Cdd:cd03240 29 GQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLIREG------EVRAQVKLAF---ENANGKKYTITRSLAIL----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032538500 94 vDSII-----EKLKLTPykdRKAKNLSLGN------SQRLGLAKALIHNPEILILDEPSNGLDPAGIVE-IRELLRDLAF 161
Cdd:cd03240 95 -ENVIfchqgESNWPLL---DMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKS 170
|
170
....*....|.
gi 2032538500 162 NKGVTIFISSH 172
Cdd:cd03240 171 QKNFQLIVITH 181
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
114-172 |
7.48e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 37.81 E-value: 7.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2032538500 114 LSLGNSQRLGLAKALIHNPEILILDEPSNgldpAGIVEIRELLRDLAFNKGVTIFISSH 172
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| |
