|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-253 |
1.50e-118 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 339.37 E-value: 1.50e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHT---LEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGhTS 77
Cdd:COG1116 1 MSAAapaLELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 78 PKIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 158 ILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAHPGEIINEIKIDLEtdSPLIPERRM 237
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLP--RPRDRELRT 237
|
250
....*....|....*.
gi 495091093 238 SRRFNDYYEMIWHNIG 253
Cdd:COG1116 238 SPEFAALRAEILDLLR 253
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-225 |
1.20e-113 |
|
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: 325.20 E-value: 1.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHtSPKIGYVL 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-GPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESY 164
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 165 KALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAHPGEIINEIKIDL 225
Cdd:cd03293 160 SALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
1.86e-77 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 235.14 E-value: 1.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHtLEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGhTSPKI 80
Cdd:COG4525 1 MSM-LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILM 160
Cdd:COG4525 79 GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 161 DESYKALDyplkiALESE-----LLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAHPGEIINEIKID 224
Cdd:COG4525 159 DEPFGALD-----ALTREqmqelLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELD 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-218 |
6.75e-74 |
|
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: 224.32 E-value: 6.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP---KIG 81
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPerrNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 162 ESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE--GRIV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
1.54e-73 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 228.06 E-value: 1.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP-- 78
Cdd:COG3842 2 AMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPek 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 -KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:COG3842 77 rNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 158 ILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRIE 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-218 |
4.56e-67 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 211.16 E-value: 4.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MShtLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP-- 78
Cdd:COG1118 1 MS--IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 -KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:COG1118 75 rRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 158 ILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ--GRIE 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
9.42e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 206.43 E-value: 9.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP-- 78
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 ------KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMI 152
Cdd:COG1136 81 arlrrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 153 TDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDiEEAVTMSDRVYVMKAhpGEIINEI 221
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRD--GRIVSDE 226
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
5-244 |
9.09e-66 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 204.98 E-value: 9.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPKIGYVL 84
Cdd:NF040729 2 LKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVT-KPGPDRGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESY 164
Cdd:NF040729 81 QNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 165 KALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAHPGEIINEIKIDLETdspliPERRMSRRFNDY 244
Cdd:NF040729 161 GAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPR-----PRNRESEKYLEY 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-217 |
1.06e-62 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 200.30 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MShTLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK- 79
Cdd:COG3839 1 MA-SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-DLPPKd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 --IGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:COG3839 75 rnIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 158 ILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEI 217
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND--GRI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-220 |
1.91e-62 |
|
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: 197.10 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 17 AAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHT--------SPKIGYVLQKDL 88
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrelrRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 89 LFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 169 YPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK-------AHPGEIINE 220
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKdgrlvqvGTPEEILTN 251
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-211 |
2.98e-62 |
|
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: 194.63 E-value: 2.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP------ 78
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 --KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQ 156
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 157 IILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDiEEAVTMSDRVYVMK 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELR 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-217 |
1.07e-61 |
|
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: 193.99 E-value: 1.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 10 ISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK--IGYVLQKD 87
Cdd:cd03300 6 VSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrpVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 88 LLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKAL 167
Cdd:cd03300 82 ALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495091093 168 DYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEI 217
Cdd:cd03300 162 DLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK--GKI 209
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
39-218 |
4.86e-58 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 189.16 E-value: 4.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 39 FV--GPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP---------KIGYVLQKDLLFPWRTVIDNVVLGLEIAG 107
Cdd:COG4175 56 FVimGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDIT-KLSKkelrelrrkKMSMVFQHFALLPHRTVLENVAFGLEIQG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 108 VSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLkI--ALESELLSIVKK 185
Cdd:COG4175 135 VPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALD-PL-IrrEMQDELLELQAK 212
|
170 180 190
....*....|....*....|....*....|...
gi 495091093 186 ERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG4175 213 LKKTIVFITHDLDEALRLGDRIAIMKD--GRIV 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-224 |
5.15e-58 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 185.29 E-value: 5.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAagPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKiGYVL 84
Cdd:PRK11248 2 LQISHLYADYGGK--PA--LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESY 164
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 165 KALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAHPGEIINEIKID 224
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLN 216
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-218 |
1.78e-57 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 185.29 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYegaAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGhTSP-----KIGYV 83
Cdd:COG1125 6 NVTKRY---PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD-LDPvelrrRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 84 LQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRM--EGYEDKFPSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 162 ESYKALDyPL-KIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG1125 162 EPFGALD-PItREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMRE--GRIV 216
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-218 |
2.64e-57 |
|
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: 182.89 E-value: 2.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGAAGPVQilhKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP-----KIGYV 83
Cdd:cd03295 5 NVTKRYGGGKKAVN---NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-EQDPvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 84 LQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRME--GYEDKFPSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 162 ESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN--GEIV 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-218 |
8.59e-56 |
|
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: 178.68 E-value: 8.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP----KI 80
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelrrKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQkdllFPWR-----TVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDP 155
Cdd:COG1122 78 GLVFQ----NPDDqlfapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495091093 156 QIILMDESYKALDYPLKIALESELLSIvKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDD--GRIV 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-212 |
9.86e-56 |
|
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: 177.83 E-value: 9.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGhTSPK---IG 81
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD-LPPKdrdIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495091093 162 ESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-212 |
1.23e-54 |
|
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: 173.91 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS------P 78
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelpplrR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 KIGYVLQKDLLFPWRTVIDNVVLGLeiagvskrearerakallqtyrmegyedkfpsqiSGGMRQRVALMRTMITDPQII 158
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495091093 159 LMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
35-218 |
1.47e-54 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 179.66 E-value: 1.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 35 EFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNR--------ETTGHTSPKIGYVLQKDLLFPWRTVIDNVVLGLEIA 106
Cdd:TIGR01186 20 EIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGEnimkqspvELREVRRKKIGMVFQQFALFPHMTILQNTSLGPELL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 107 GVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKE 186
Cdd:TIGR01186 100 GWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQDELKKLQATL 179
|
170 180 190
....*....|....*....|....*....|..
gi 495091093 187 RKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:TIGR01186 180 QKTIVFITHDLDEAIRIGDRIVIMKA--GEIV 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-218 |
7.32e-54 |
|
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: 174.06 E-value: 7.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK--IG 81
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPWRTVIDNVVLGLEIAGVSKR----EARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 158 ILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVM--NKGRIE 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-211 |
8.90e-54 |
|
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: 172.65 E-value: 8.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHT----SPKIGYVL 84
Cdd:cd03225 4 NLSFSYPDGARPA--LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkelRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QK-DLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDES 163
Cdd:cd03225 82 QNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495091093 164 YKALDYPLKIALeSELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:cd03225 162 TAGLDPAGRREL-LELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-218 |
2.53e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.86 E-value: 2.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS---PKIG 81
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAevrRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 162 ESYKALDyPLKIAlesELLSIVKKER---KTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG1131 157 EPTSGLD-PEARR---ELWELLRELAaegKTVLLSTHYLEEAERLCDRVAIIDK--GRIV 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-217 |
3.45e-50 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 168.59 E-value: 3.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGAagpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK---IGYVLQ 85
Cdd:PRK09452 19 GISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAEnrhVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 86 KDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYK 165
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495091093 166 ALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEI 217
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRD--GRI 223
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-211 |
4.03e-50 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 166.90 E-value: 4.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK---IGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARER 116
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-NVPPHlrhINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 117 AKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHD 196
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170
....*....|....*
gi 495091093 197 IEEAVTMSDRVYVMK 211
Cdd:TIGR01187 161 QEEAMTMSDRIAIMR 175
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-218 |
4.72e-50 |
|
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: 171.24 E-value: 4.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISK-FYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS------ 77
Cdd:COG1123 261 LEVRNLSKrYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 78 -PKIGYVLQkD---LLFPWRTVIDNVVLGLEIAGV-SKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVALMRTM 151
Cdd:COG1123 341 rRRVQMVFQ-DpysSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 152 ITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--GRIV 484
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-218 |
3.19e-49 |
|
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: 161.90 E-value: 3.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHT-------S 77
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 78 PKIGYVLQKDL--LFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRM---EGYEDKFPSQISGGMRQRVALMRTMI 152
Cdd:cd03257 82 KEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 153 TDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA--GKIV 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-232 |
4.69e-49 |
|
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: 161.69 E-value: 4.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP------ 78
Cdd:COG1127 6 IEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 -KIGYVLQKDLLFPWRTVIDNVVLGL-EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQ 156
Cdd:COG1127 82 rRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 157 IILMDESYKALDyPL-KIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINEIKID--LETDSPLI 232
Cdd:COG1127 162 ILLYDEPTAGLD-PItSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVL--ADGKIIAEGTPEelLASDDPWV 237
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
35-247 |
5.13e-49 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 161.48 E-value: 5.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 35 EFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPKIGYVLQKDLLFPWRTVIDNVVLGLE--IAGVSKRE 112
Cdd:TIGR01184 12 EFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EPGPDRMVVFQNYSLLPWLTVRENIALAVDrvLPDLSKSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 113 ARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVF 192
Cdd:TIGR01184 91 RRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 193 ITHDIEEAVTMSDRVYVMKAHPGEIINEIkidLETDSPLiPERRMsRRFND--YYEM 247
Cdd:TIGR01184 171 VTHDVDEALLLSDRVVMLTNGPAANIGQI---LEVPFPR-PRDRL-EVVEDpsYYDL 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-212 |
4.24e-47 |
|
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: 155.92 E-value: 4.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 25 HKMKFHADAN-EFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNR-----ETTGHTSP---KIGYVLQKDLLFPWRTV 95
Cdd:cd03297 13 FTLKIDFDLNeEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPqqrKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 96 IDNVVLGLEiaGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIAL 175
Cdd:cd03297 93 RENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 495091093 176 ESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-218 |
4.53e-47 |
|
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: 163.54 E-value: 4.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPD---NGSILVDNRETTGHT- 76
Cdd:COG1123 1 MTPLLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 77 ---SPKIGYVLQ--KDLLFPWrTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTM 151
Cdd:COG1123 79 alrGRRIGMVFQdpMTQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 152 ITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIV 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-220 |
4.78e-47 |
|
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: 156.20 E-value: 4.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGhTSPK--------I 80
Cdd:cd03258 6 NVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTL-LSGKelrkarrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILM 160
Cdd:cd03258 85 GMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 161 DESYKALDyPLKIALESELLSIVKKERK-TVVFITHDIEEAVTMSDRVYVMkaHPGEIINE 220
Cdd:cd03258 165 DEATSALD-PETTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVM--EKGEVVEE 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-232 |
7.82e-46 |
|
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: 153.43 E-value: 7.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP-------KIGYVLQKDLLFP 91
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrlrrRMGMLFQSGALFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 92 WRTVIDNVVLGL-EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYP 170
Cdd:cd03261 91 SLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495091093 171 LKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINEIKID--LETDSPLI 232
Cdd:cd03261 171 ASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVL--YDGKIVAEGTPEelRASDDPLV 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-211 |
8.78e-46 |
|
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: 153.47 E-value: 8.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP---KIG 81
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREarrQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495091093 162 ESYKALDYPLKIALESELLSIvKKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:COG4555 158 EPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILH 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-218 |
2.18e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 152.07 E-value: 2.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP------ 78
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 KIGYVLQKDLLFPWRTVIDNVVLGLEIA-GVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495091093 158 ILMDESYKALDyPlkiALESELLSIVK---KERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG1126 158 MLFDEPTSALD-P---ELVGEVLDVMRdlaKEGMTMVVVTHEMGFAREVADRVVFMDG--GRIV 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-224 |
7.18e-45 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 151.11 E-value: 7.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT----GHTSPKI 80
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTrrrrKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQkD---LLFPWRTVIDNVVLGLEIAGVskREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVALMRTMITDPQ 156
Cdd:COG1124 82 QMVFQ-DpyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 157 IILMDESYKALDYPL--KIAlesELLSIVKKERK-TVVFITHDIEEAVTMSDRVYVMKAhpGEIINEIKID 224
Cdd:COG1124 159 LLLLDEPTSALDVSVqaEIL---NLLKDLREERGlTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTVA 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-217 |
1.22e-44 |
|
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: 149.60 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP------ 78
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelrq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 KIGYVLQKDLLFPWRTVIDNVVLGL-EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495091093 158 ILMDESYKALDYPLKialeSELLSIVK---KERKTVVFITHDIEEAVTMSDRVYVMkaHPGEI 217
Cdd:cd03262 157 MLFDEPTSALDPELV----GEVLDVMKdlaEEGMTMVVVTHEMGFAREVADRVIFM--DDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-218 |
5.04e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 151.38 E-value: 5.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP-------KIG 81
Cdd:COG1135 6 NLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraarrKIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:COG1135 86 MIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495091093 162 ESYKALDyP------LkiALeseLLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG1135 166 EATSALD-PettrsiL--DL---LKDINRELGLTIVLITHEMDVVRRICDRVAVLEN--GRIV 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-218 |
8.34e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.51 E-value: 8.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS---P--- 78
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 -KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:COG2884 79 rRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495091093 158 ILMDESYKALDYPL--KIAlesELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG2884 159 LLADEPTGNLDPETswEIM---ELLEEINRRGTTVLIATHDLELVDRMPKRVLELED--GRLV 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-162 |
9.09e-44 |
|
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: 145.10 E-value: 9.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG----HTSPKIGYVLQKDLLFPWRTVIDNV 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDderkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 100 VLGLEIAGVSKREARERAKALLQTYRMEGYED----KFPSQISGGMRQRVALMRTMITDPQIILMDE 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-218 |
1.14e-42 |
|
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: 145.17 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK--IGYVLQKDLLFPWRTVIDNVVL 101
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 102 GLEIAGVSKREARERakaLLQTYRMEGYE---DKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESE 178
Cdd:cd03299 95 GLKKRKVDKKEIERK---VLEIAEMLGIDhllNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495091093 179 LLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03299 172 LKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLN--GKLI 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-207 |
3.58e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 143.74 E-value: 3.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP---KIGYVLQKDLLFPWRTVIDNVVLGLEI 105
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT-ALPPaerPVSMLFQENNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 106 AGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyplkIALESELLSIVK- 184
Cdd:COG3840 99 GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD----PALRQEMLDLVDe 174
|
170 180
....*....|....*....|....*.
gi 495091093 185 --KERK-TVVFITHDIEEAVTMSDRV 207
Cdd:COG3840 175 lcRERGlTVLMVTHDPEDAARIADRV 200
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-220 |
9.36e-42 |
|
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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 143.72 E-value: 9.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVD-----NRETTGHTSPK 79
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgldtlDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQK-DLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQII 158
Cdd:TIGR04520 79 VGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 159 LMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVtMSDRVYVMKAhpGEIINE 220
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNK--GKIVAE 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-217 |
1.08e-41 |
|
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: 140.61 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILV---DNRETTGHTSPKIG 81
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkDIKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPWRTVIDNVVLgleiagvskrearerakallqtyrmegyedkfpsqiSGGMRQRVALMRTMITDPQIILMD 161
Cdd:cd03230 77 YLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 162 ESYKALDYPLKIALESELLSIvKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEI 217
Cdd:cd03230 121 EPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNN--GRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-220 |
2.43e-41 |
|
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: 142.10 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK----- 79
Cdd:COG1120 2 LEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSRRelarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQkDLLFPWR-TVIDNVVLG----LEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITD 154
Cdd:COG1120 77 IAYVPQ-EPPAPFGlTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 155 PQIILMDE--SYkaLDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA-------HPGEIINE 220
Cdd:COG1120 156 PPLLLLDEptSH--LDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDgrivaqgPPEEVLTP 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-218 |
6.67e-41 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 140.26 E-value: 6.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG--------HT 76
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedararLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 77 SPKIGYVLQKDLLFPWRTVIDNVVLGLEIAGVskREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQ 156
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 157 IILMDESYKALDYP--LKIAlesELLSIVKKERK-TVVFITHDIEEAvTMSDRVYVMKAhpGEII 218
Cdd:COG4181 167 ILFADEPTGNLDAAtgEQII---DLLFELNRERGtTLVLVTHDPALA-ARCDRVLRLRA--GRLV 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-240 |
1.19e-40 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 140.58 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDN------RETTGhtspkigY 82
Cdd:PRK11247 17 AVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTaplaeaREDTR-------L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 83 VLQKDLLFPWRTVIDNVVLGLeiagvsKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDE 162
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 163 SYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpgeiiNEIKIDLETDSPLiPERRMSRR 240
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEE------GKIGLDLTVDLPR-PRRRGSAR 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-213 |
1.29e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.80 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAagpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP----KI 80
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewrrQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQKDLLFPwRTVIDNVVLGLEIAGvsKREARERAKALLQT-YRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIIL 159
Cdd:COG4619 77 AYVPQEPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERlGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495091093 160 MDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAH 213
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
37-218 |
3.17e-40 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 142.17 E-value: 3.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 37 VSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK---IGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREA 113
Cdd:PRK11432 35 VTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT-HRSIQqrdICMVFQSYALFPHMSLGENVGYGLKMLGVPKEER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 114 RERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFI 193
Cdd:PRK11432 114 KQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYV 193
|
170 180
....*....|....*....|....*
gi 495091093 194 THDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:PRK11432 194 THDQSEAFAVSDTVIVM--NKGKIM 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-210 |
3.57e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGaagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNREtTGHTSPKI 80
Cdd:COG1121 3 MMPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-PRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQK---DLLFPwRTVIDNVVLGL----EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMIT 153
Cdd:COG1121 78 GYVPQRaevDWDFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 154 DPQIILMDESYKALDYPLKIALeSELLSIVKKERKTVVFITHDIEEAVTMSDRVYVM 210
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEAL-YELLRELRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-212 |
4.95e-40 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 141.71 E-value: 4.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK---IGYVLQ 85
Cdd:PRK11000 8 NVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAergVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 86 KDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYK 165
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495091093 166 ALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-210 |
1.55e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 140.22 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MShtLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG-HTSP- 78
Cdd:PRK10851 1 MS--IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlHARDr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKR----EARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITD 154
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 155 PQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVM 210
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVM 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-200 |
3.41e-39 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 135.30 E-value: 3.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPD---NGSILVDNRE-TTGHTSPK-IGYVLQKDLLFPWRTVID 97
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRlTALPAEQRrIGILFQDDLLFPHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 98 NVVLGLEiAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALES 177
Cdd:COG4136 96 NLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRE 174
|
170 180
....*....|....*....|...
gi 495091093 178 ELLSIVKKERKTVVFITHDIEEA 200
Cdd:COG4136 175 FVFEQIRQRGIPALLVTHDEEDA 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-214 |
4.22e-39 |
|
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: 135.35 E-value: 4.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGhTSPKIGYVLQK---DLLFPWrTVIDNV 99
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-ERKRIGYVPQRrsiDRDFPI-SVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 VLGL----EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIAL 175
Cdd:cd03235 92 LMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 495091093 176 eSELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAHP 214
Cdd:cd03235 172 -YELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
32-259 |
8.03e-39 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 139.40 E-value: 8.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 32 DANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVD--------NRETTGHTSPKIGYVLQKDLLFPWRTVIDNVVLGL 103
Cdd:PRK10070 52 EEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 104 EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIV 183
Cdd:PRK10070 132 ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQ 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 184 KKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEIINeikidletdsPLIPERRMSRRFNDYYEMIWHNIGITPVLA 259
Cdd:PRK10070 212 AKHQRTIVFISHDLDEAMRIGDRIAIMQN--GEVVQ----------VGTPDEILNNPANDYVRTFFRGVDISQVFS 275
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-211 |
1.03e-38 |
|
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: 134.46 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT---GHTSP--- 78
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrGRAIPylr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 -KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:cd03292 78 rKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495091093 158 ILMDESYKALDyPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:cd03292 158 LIADEPTGNLD-PDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALE 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-218 |
4.11e-38 |
|
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: 133.05 E-value: 4.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK----- 79
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrarlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIIL 159
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 160 MDESYKALDyPLKIaleSELLSIVK--KERKTVVFIT-HDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:cd03218 157 LDEPFAGVD-PIAV---QDIQKIIKilKDRGIGVLITdHNVRETLSITDRAYII--YEGKVL 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-212 |
4.23e-38 |
|
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: 132.40 E-value: 4.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKIGYVL 84
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESY 164
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495091093 165 KALDyPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:cd03269 157 SGLD-PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-218 |
6.71e-38 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 135.18 E-value: 6.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKP---DNGSILVDNRETTGHTSP--- 78
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 -----KIGYVLQKDL--LFPWRTVIDNVVLGLEI-AGVSKREARERAKALLQTYRM---EGYEDKFPSQISGGMRQRVAL 147
Cdd:COG0444 82 kirgrEIQMIFQDPMtsLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 148 MRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYA--GRIV 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-220 |
6.97e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.99 E-value: 6.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVD----NRETTGHT 76
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYA--LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 77 SPKIGYVLQK-DLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDP 155
Cdd:PRK13635 80 RRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 156 QIILMDESYKALDyPlkiALESELLSIV----KKERKTVVFITHDIEEAVTmSDRVYVMKAhpGEIINE 220
Cdd:PRK13635 160 DIIILDEATSMLD-P---RGRREVLETVrqlkEQKGITVLSITHDLDEAAQ-ADRVIVMNK--GEILEE 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-218 |
9.51e-38 |
|
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: 130.63 E-value: 9.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK-----IGYVLQkdllfpwr 93
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA-SLSPKelarkIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 94 tvidnvvlgleiagvskrearerakaLLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKI 173
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495091093 174 ALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03214 135 ELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD--GRIV 177
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-211 |
9.74e-38 |
|
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: 130.20 E-value: 9.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS----PKI 80
Cdd:cd03228 1 IEFKNVSFSYPG--RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLeslrKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQKDLLFPwRTVIDNVvlgleiagvskrearerakallqtyrmegyedkfpsqISGGMRQRVALMRTMITDPQIILM 160
Cdd:cd03228 79 AYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495091093 161 DESYKALDYPLKIALESELLSIvkKERKTVVFITHDIeEAVTMSDRVYVMK 211
Cdd:cd03228 121 DEATSALDPETEALILEALRAL--AKGKTVIVIAHRL-STIRDADRIIVLD 168
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-211 |
1.54e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 133.32 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHT----SPKIGYVLQK-DLLFPWRTVID 97
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdiRHKIGMVFQNpDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 98 NVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALES 177
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190
....*....|....*....|....*....|....
gi 495091093 178 ELLSIVKKERKTVVFITHDIEEaVTMSDRVYVMK 211
Cdd:PRK13650 182 TIKGIRDDYQMTVISITHDLDE-VALSDRVLVMK 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-212 |
2.29e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 134.59 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKFYEGaagPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK---I 80
Cdd:PRK11650 3 GLKLQAVRKSYDG---KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-ELEPAdrdI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILM 160
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495091093 161 DESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:PRK11650 159 DEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNG 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-220 |
2.90e-37 |
|
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: 130.57 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETtgHTSP-----K 79
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV--VKEPaearrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIIL 159
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 160 MDESYKALDYPLKIALEsELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINE 220
Cdd:cd03266 160 LDEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVL--HRGRVVYE 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-218 |
3.32e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 133.77 E-value: 3.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 6 EAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP------- 78
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQII 158
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 159 LMDESYKALDyPLKIALESELLSIVKKERK-TVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:PRK11153 163 LCDEATSALD-PATTRSILELLKDINRELGlTIVLITHEMDVVKRICDRVAVIDA--GRLV 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-218 |
3.78e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.90 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDisKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNG--SILVDNRETTGHTSP 78
Cdd:PRK11124 1 MSIQLNGIN--CFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHFDFSKTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 K--------IGYVLQKDLLFPWRTVIDNVVLG-LEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMR 149
Cdd:PRK11124 75 KairelrrnVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 150 TMITDPQIILMDESYKALDyPlkiALESELLSIVKKERKT---VVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALD-P---EITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYMEN--GHIV 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-220 |
7.08e-37 |
|
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: 137.66 E-value: 7.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 14 YEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK-----IGYVLQKDL 88
Cdd:COG2274 483 YPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR-QIDPAslrrqIGVVLQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 89 LFPwRTVIDNVVLGLEiaGVSKREARERAKAL------------LQTYRMEGYedkfpSQISGGMRQRVALMRTMITDPQ 156
Cdd:COG2274 560 LFS-GTIRENITLGDP--DATDEEIIEAARLAglhdfiealpmgYDTVVGEGG-----SNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495091093 157 IILMDESYKALDYPLKIALESELLSIVKKerKTVVFITHDiEEAVTMSDRVYVMKAhpGEIINE 220
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHR-LSTIRLADRIIVLDK--GRIVED 690
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-220 |
9.58e-37 |
|
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: 129.86 E-value: 9.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK----- 79
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQKDLLFPWRTVIDNVVLGLEIAGVS----------KREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMR 149
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 150 TMITDPQIILMDESYKALDYPLKIALeSELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINE 220
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEEL-AELIRELRERGITVLLVEHDMDVVMSLADRVTVL--DQGRVIAE 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
35-210 |
1.74e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 132.65 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 35 EFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP---KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKR 111
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-HVPPyqrPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 112 EARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVV 191
Cdd:PRK11607 125 EIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCV 204
|
170
....*....|....*....
gi 495091093 192 FITHDIEEAVTMSDRVYVM 210
Cdd:PRK11607 205 MVTHDQEEAMTMAGRIAIM 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-218 |
2.34e-36 |
|
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: 128.45 E-value: 2.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLK-----PDNGSILVDNRETTGHTSP- 78
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 -----KIGYVLQKDLLFPwRTVIDNVVLGLEIAGVSKREAR-ERAKALLQTYRMEGYEDK--FPSQISGGMRQRVALMRT 150
Cdd:cd03260 77 lelrrRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 151 MITDPQIILMDESYKALDYPLKIALESELLSIvkKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFL--LNGRLV 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-212 |
2.54e-36 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 131.76 E-value: 2.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNR----ETTGHTSP----KIGYVLQKDLLFPWRTVIDNVV 100
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPphrrRIGYVFQEARLFPHLSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 101 LGLEIAGVSKREAR-ERAKALLQtyrMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKialeSEL 179
Cdd:COG4148 100 YGRKRAPRAERRISfDEVVELLG---IGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK----AEI 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 495091093 180 LSIVKKERKT----VVFITHDIEEAVTMSDRVYVMKA 212
Cdd:COG4148 173 LPYLERLRDEldipILYVSHSLDEVARLADHVVLLEQ 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
8.57e-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: 127.85 E-value: 8.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKI 80
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 -----GYVLQKDLLFPWRTVIDNVVLGLEIAGVSK---------------REARERAKALLQTYRMEGYEDKFPSQISGG 140
Cdd:COG0411 77 arlgiARTFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 141 MRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL--DFGRVI 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-218 |
8.60e-36 |
|
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: 126.85 E-value: 8.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS---PKIG 81
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKaarQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 162 ESYKALDyplkIALESELLSIVKKERK--TVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03263 159 EPTSGLD----PASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSD--GKLR 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-211 |
1.12e-35 |
|
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: 124.66 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 6 EAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP----KIG 81
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelrrRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVlqkdllfpwrtvidnvvlgleiagvskrearerakallqtyrmegyedkfpSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:cd00267 77 YV---------------------------------------------------PQLSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495091093 162 ESYKALDYPLKIALEsELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:cd00267 106 EPTSGLDPASRERLL-ELLRELAEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-219 |
1.27e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 127.13 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGhtsPKI---------GYVLQKDLL 89
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND---PKVderlirqeaGMVFQQFYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 90 FPWRTVIDNVVLG-LEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:PRK09493 89 FPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 169 YPLKialeSELLSIVK---KERKTVVFITHDIEEAVTMSDRVYVMKA-------HPGEIIN 219
Cdd:PRK09493 169 PELR----HEVLKVMQdlaEEGMTMVIVTHEIGFAEKVASRLIFIDKgriaedgDPQVLIK 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
2.94e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 126.28 E-value: 2.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MShtLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP-- 78
Cdd:COG4161 1 MS--IQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPse 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 --------KIGYVLQKDLLFPWRTVIDNVVLG-LEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMR 149
Cdd:COG4161 75 kairllrqKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 150 TMITDPQIILMDESYKALDyPlkiALESELLSIVKKERK---TVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALD-P---EITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEK--GRII 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-206 |
6.61e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.08 E-value: 6.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 26 KMKF--HADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK---IGYVLQKDLLFPWRTVIDNVV 100
Cdd:PRK10771 15 PMRFdlTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT-TTPPSrrpVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 101 LGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPlkiALESELL 180
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD-P---ALRQEML 169
|
170 180 190
....*....|....*....|....*....|
gi 495091093 181 SIVK---KERK-TVVFITHDIEEAVTMSDR 206
Cdd:PRK10771 170 TLVSqvcQERQlTLLMVSHSLEDAARIAPR 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-210 |
6.95e-35 |
|
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: 124.14 E-value: 6.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHAD----ANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK---IGYVLQKDLLFPWRTVI 96
Cdd:cd03298 10 YGEQPMHFDltfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT-AAPPAdrpVSMLFQENNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 97 DNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALE 176
Cdd:cd03298 89 QNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....
gi 495091093 177 SELLSIVKKERKTVVFITHDIEEAVTMSDRVYVM 210
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-232 |
9.11e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.49 E-value: 9.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVD----NRETTGHTSPKIGYVLQK-DLLFPWRTVI 96
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDgitiSKENLKEIRKKIGIIFQNpDNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 97 DNVVLGLEiagvSKREARERAKALLQTYR----MEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLK 172
Cdd:PRK13632 103 DDIAFGLE----NKKVPPKKMKDIIDDLAkkvgMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 173 IALESELLSIVKKERKTVVFITHDIEEAVtMSDRVYVMK-------AHPGEIINEIKI--DLETDSPLI 232
Cdd:PRK13632 179 REIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSegkliaqGKPKEILNNKEIleKAKIDSPFI 246
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-210 |
1.46e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.48 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS------- 77
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 78 -----PKIGYVLQKDLLFPWRTVIDNVVLG-LEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTM 151
Cdd:PRK11264 80 irqlrQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 152 ITDPQIILMDESYKALDyPlkiALESELLSIVK---KERKTVVFITHDIEEAVTMSDRVYVM 210
Cdd:PRK11264 160 AMRPEVILFDEPTSALD-P---ELVGEVLNTIRqlaQEKRTMVIVTHEMSFARDVADRAIFM 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-212 |
3.69e-34 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 125.99 E-value: 3.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 26 KMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNR-----ETTGHTSP---KIGYVLQKDLLFPWRTVID 97
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsRKGIFLPPekrRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 98 NVVLGLEIAGVSKREAREraKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALES 177
Cdd:TIGR02142 95 NLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 495091093 178 ELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-218 |
1.94e-33 |
|
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: 127.18 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKFYEGAAgpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP----K 79
Cdd:COG4988 336 SIELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswrrQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQKDLLFPWrTVIDNVVLGleiagvsKREA-RERAKALLQTYRMEGYEDKFP-----------SQISGGMRQRVAL 147
Cdd:COG4988 413 IAWVPQNPYLFAG-TIRENLRLG-------RPDAsDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495091093 148 MRTMITDPQIILMDESYKALDyplkIALESELLSIVKK--ERKTVVFITHDIeEAVTMSDRVYVMKAhpGEII 218
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLD----AETEAEILQALRRlaKGRTVILITHRL-ALLAQADRILVLDD--GRIV 550
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-218 |
2.47e-33 |
|
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: 121.14 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK----- 79
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 --IGYVLQKDLLFPWRTVIDNVVLGL--------EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMR 149
Cdd:cd03256 78 rqIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 150 TMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRIV 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-228 |
3.34e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.91 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHtSPK- 79
Cdd:COG3845 2 MPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR-SPRd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 -----IGYVLQKDLLFPWRTVIDNVVLGLEIAG---VSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTM 151
Cdd:COG3845 77 aialgIGMVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 152 ITDPQIILMDESYKALDyPLKIAlesELLSIVKK---ERKTVVFITHDIEEAVTMSDRVYVMKAhpGEIINEIKIDlETD 228
Cdd:COG3845 157 YRGARILILDEPTAVLT-PQEAD---ELFEILRRlaaEGKSIIFITHKLREVMAIADRVTVLRR--GKVVGTVDTA-ETS 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-196 |
3.44e-33 |
|
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: 119.51 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 3 HTLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP---K 79
Cdd:COG4133 1 MMLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQKDLLFPWRTVIDNVVLGLEIAGVskREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIIL 159
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 495091093 160 MDESYKALDyPLKIALESELLSIVKKERKTVVFITHD 196
Cdd:COG4133 155 LDEPFTALD-AAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-211 |
1.11e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.36 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK----- 79
Cdd:COG1129 5 LEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRdaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 -IGYVLQKDLLFPWRTVIDNVVLGLEIAG---VSKREARERAKALLQTYRMEgyEDkfP----SQISGGMRQRVALMRTM 151
Cdd:COG1129 80 gIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLD--ID--PdtpvGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 152 ITDPQIILMDESYKALDyplkialESE---LLSIV---KKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:COG1129 156 SRDARVLILDEPTASLT-------EREverLFRIIrrlKAQGVAIIYISHRLDEVFEIADRVTVLR 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-222 |
1.70e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 120.21 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKIGYv 83
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGY- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 84 lqkdL-----LFPWRTVIDNVV-LGlEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:COG4152 76 ----LpeergLYPKMKVGEQLVyLA-RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495091093 158 ILMDESYKALDyPlkIA---LESELLSIvKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII-----NEIK 222
Cdd:COG4152 151 LILDEPFSGLD-P--VNvelLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINK--GRKVlsgsvDEIR 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-222 |
2.03e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.42 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISK-FYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK---- 79
Cdd:COG1101 2 LELKNLSKtFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQKDLL--FPWRTVIDNVVL--------GLEIaGVSKREaRERAKALLQTYRMeGYEDKFPSQI---SGGMRQRVA 146
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLALayrrgkrrGLRR-GLTKKR-RELFRELLATLGL-GLENRLDTKVgllSGGQRQALS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 147 L-MRTMiTDPQIILMDESYKALDyP----LKIALESEllsIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINEI 221
Cdd:COG1101 159 LlMATL-TKPKLLLLDEHTAALD-PktaaLVLELTEK---IVEENNLTTLMVTHNMEQALDYGNRLIMM--HEGRIILDV 231
|
.
gi 495091093 222 K 222
Cdd:COG1101 232 S 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-210 |
2.19e-32 |
|
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: 117.92 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK----- 79
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErarag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREAR-ERAKALlqtyrmegyedkFP----------SQISGGMRQRVALM 148
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARlERVYEL------------FPrlkerrkqlaGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 149 RTMITDPQIILMDESYKALDyPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVM 210
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLA-PKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-220 |
2.48e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.41 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAgpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP------ 78
Cdd:PRK13639 2 LETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 KIGYVLQK--DLLFPwRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQ 156
Cdd:PRK13639 79 TVGIVFQNpdDQLFA-PTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495091093 157 IILMDESYKALDyPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINE 220
Cdd:PRK13639 158 IIVLDEPTSGLD-PMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVM--SDGKIIKE 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-221 |
3.49e-31 |
|
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: 114.62 E-value: 3.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP--KIGYVLQK 86
Cdd:cd03268 5 DLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAlrRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 87 DLLFPWRTVIDNVVLGLEIAGVSKREARErakaLLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKA 166
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 167 LDyPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINEI 221
Cdd:cd03268 157 LD-PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGII--NKGKLIEEG 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-211 |
6.49e-31 |
|
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: 113.89 E-value: 6.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 6 EAIDISKFYEGAAGPVQILHkmkFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK-IGYVL 84
Cdd:cd03226 1 RIENISFSYKKGTEILDDLS---LDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKsIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 Q--KDLLFPwRTVIDNVVLGLEIAGvskrEARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDE 162
Cdd:cd03226 78 QdvDYQLFT-DSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495091093 163 SYKALDYPLKIALeSELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:cd03226 153 PTSGLDYKNMERV-GELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-210 |
2.38e-30 |
|
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: 111.15 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT----GHTSPKI 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwdpNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQKDLLFPwRTVIDNVvlgleiagvskrearerakallqtyrmegyedkfpsqISGGMRQRVALMRTMITDPQIILM 160
Cdd:cd03246 79 GYLPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495091093 161 DESYKALDYPLKIALeSELLSIVKKERKTVVFITHDIeEAVTMSDRVYVM 210
Cdd:cd03246 121 DEPNSHLDVEGERAL-NQAIAALKAAGATRIVIAHRP-ETLASADRILVL 168
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-210 |
9.30e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.67 E-value: 9.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYE-------GAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS 77
Cdd:COG4608 8 LEVRDLKKHFPvrgglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 78 -------PKIGYVLQKDL--LFPWRTVIDNVVLGLEIAGV-SKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVA 146
Cdd:COG4608 88 relrplrRRMQMVFQDPYasLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 147 LMRTMITDPQIILMDESYKALDYplkialesellSI----------VKKERK-TVVFITHDIeeAVT--MSDRVYVM 210
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDV-----------SIqaqvlnlledLQDELGlTYLFISHDL--SVVrhISDRVAVM 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-211 |
1.20e-29 |
|
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: 109.06 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHtspkigyvl 84
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 qkdllfpwrtvidnvvlgleiagvSKREARERAKALLqtyrmegyedkfpSQISGGMRQRVALMRTMITDPQIILMDESY 164
Cdd:cd03216 68 ------------------------SPRDARRAGIAMV-------------YQLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495091093 165 KALDyplkiALESE-LLSIVKKERK---TVVFITHDIEEAVTMSDRVYVMK 211
Cdd:cd03216 111 AALT-----PAEVErLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLR 156
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-218 |
2.75e-29 |
|
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: 110.27 E-value: 2.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 13 FYEGAAGPVqILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRE----TTGHTSPKIGYVLQKDL 88
Cdd:cd03252 8 FRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlalaDPAWLRRQVGVVLQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 89 LFPwRTVIDNVVLGLEiaGVSKREARERAK-ALLQTYRM---EGYEDKFPSQ---ISGGMRQRVALMRTMITDPQIILMD 161
Cdd:cd03252 87 LFN-RSIRDNIALADP--GMSMERVIEAAKlAGAHDFISelpEGYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 162 ESYKALDYPLKIALESELLSIVKKerKTVVFITHDIeEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAG--RTVIIIAHRL-STVKNADRIIVMEK--GRIV 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
40-218 |
4.35e-29 |
|
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: 109.20 E-value: 4.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP---KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARER 116
Cdd:cd03264 31 LGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrrRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 117 AKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALeSELLSIVKKERkTVVFITHD 196
Cdd:cd03264 111 VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRF-RNLLSELGEDR-IVILSTHI 188
|
170 180
....*....|....*....|..
gi 495091093 197 IEEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03264 189 VEDVESLCNQVAVLNK--GKLV 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
29-220 |
4.55e-29 |
|
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: 109.38 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILV---DNRETTGHTSPKIGYVLQKDLLFPWRTVIDNVVLGLEI 105
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghDVVREPREVRRRIGIVFQDLSVDDELTGWENLYIHARL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 106 AGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKK 185
Cdd:cd03265 101 YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEE 180
|
170 180 190
....*....|....*....|....*....|....*
gi 495091093 186 ERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINE 220
Cdd:cd03265 181 FGMTILLTTHYMEEAEQLCDRVAII--DHGRIIAE 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-249 |
5.63e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 114.82 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILV--------DNRET 72
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVagqdvatlDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 73 TGHTSPKIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMI 152
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 153 TDPQIILMDESYKALDYplkiALESELLSIVKKERK---TVVFITHDIEEAvTMSDRvyVMKAHPGEII---------NE 220
Cdd:PRK10535 161 NGGQVILADEPTGALDS----HSGEEVMAILHQLRDrghTVIIVTHDPQVA-AQAER--VIEIRDGEIVrnppaqekvNV 233
|
250 260
....*....|....*....|....*....
gi 495091093 221 IKIDLETDSPLIPERRMSRRFNDYYEMIW 249
Cdd:PRK10535 234 AGGTEPVVNTASGWRQFVSGFREALTMAW 262
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 |
7.56e-29 |
|
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: 113.92 E-value: 7.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 2 SHTLEAIDISKFYEG---AAGPVQilhkmkFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP 78
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGrrpALRPVS------FTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA-DADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 K-----IGYVLQKDLLFPwRTVIDNVVLGLEIAGVSK-REARERAKA--LLQTyRMEGYE---DKFPSQISGGMRQRVAL 147
Cdd:TIGR02857 392 DswrdqIAWVPQHPFLFA-GTIAENIRLARPDASDAEiREALERAGLdeFVAA-LPQGLDtpiGEGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 148 MRTMITDPQIILMDESYKALDyplkIALESELLSIVKK--ERKTVVFITHDIEEAVTMsDRVYVM 210
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLD----AETEAEVLEALRAlaQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-220 |
1.14e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 109.29 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDN------RETTGHTS- 77
Cdd:PRK10619 6 LNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvRDKDGQLKv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 78 ----------PKIGYVLQKDLLFPWRTVIDNVVLG-LEIAGVSKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRV 145
Cdd:PRK10619 82 adknqlrllrTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 146 ALMRTMITDPQIILMDESYKALDyPlkiALESELLSIVKK---ERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINE 220
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALD-P---ELVGEVLRIMQQlaeEGKTMVVVTHEMGFARHVSSHVIFL--HQGKIEEE 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-220 |
6.42e-28 |
|
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: 106.54 E-value: 6.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNREttGHTSP------KIGYVLQKDLLFPwRTV 95
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID--IRDISrkslrsMIGVVLQDTFLFS-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 96 IDNVVLGLEIAgvsKREARERAKALLQTYRM-----EGYEDKFPSQ---ISGGMRQRVALMRTMITDPQIILMDESYKAL 167
Cdd:cd03254 94 MENIRLGRPNA---TDEEVIEAAKEAGAHDFimklpNGYDTVLGENggnLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 168 DYPLKIALESELLSIVKKerKTVVFITH---DIEEAvtmsDRVYVMkaHPGEIINE 220
Cdd:cd03254 171 DTETEKLIQEALEKLMKG--RTSIIIAHrlsTIKNA----DKILVL--DDGKIIEE 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-218 |
7.03e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.41 E-value: 7.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP----KIGYVLQKDLLFPwRTVID 97
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEslrrQIGVVPQDTFLFS-GTIRE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 98 NVVLGLEiaGVSKREARERAKALlqtyRMEGYEDKFP-----------SQISGGMRQRVALMRTMITDPQIILMDESYKA 166
Cdd:COG1132 433 NIRYGRP--DATDEEVEEAAKAA----QAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSA 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 167 LDYplkialESELL---SIVK-KERKTVVFITHDIeEAVTMSDRVYVMKAhpGEII 218
Cdd:COG1132 507 LDT------ETEALiqeALERlMKGRTTIVIAHRL-STIRNADRILVLDD--GRIV 553
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-220 |
7.06e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 109.15 E-value: 7.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAgpvqILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS---PKIG 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARlarARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 162 ESYKALDyPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA-------HPGEIINE 220
Cdd:PRK13536 198 EPTTGLD-PHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAgrkiaegRPHALIDE 262
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-210 |
7.88e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 7.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 20 PVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPD---NGSILVD----NRETTGHTSPKIGYVLQK-DLLFP 91
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDgitlTAKTVWDIREKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 92 WRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPL 171
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 495091093 172 KIALESELLSIVKKERKTVVFITHDIEEAVtMSDRVYVM 210
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVL 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-218 |
1.14e-27 |
|
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: 111.01 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 2 SHTLEAIDISKFYEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP--- 78
Cdd:COG4987 331 GPSLELEDVSFRYPGAGRPV--LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdlr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 -KIGYVLQKDLLFPwRTVIDNVVLGLEIAGvskreaRERAKALLQTYRMEGYEDKFP-----------SQISGGMRQRVA 146
Cdd:COG4987 409 rRIAVVPQRPHLFD-TTLRENLRLARPDAT------DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 147 LMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKkeRKTVVFITHDIEEAVTMsDRVYVMKAhpGEII 218
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLED--GRIV 548
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-218 |
1.75e-27 |
|
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: 105.39 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 14 YEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP----KIGYVLQKDLL 89
Cdd:cd03251 10 YPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAslrrQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 90 FPwRTVIDNVVLGLEiaGVSKREARERAK-ALLQTYRM---EGYEDKFP---SQISGGMRQRVALMRTMITDPQIILMDE 162
Cdd:cd03251 88 FN-DTVAENIAYGRP--GATREEVEEAARaANAHEFIMelpEGYDTVIGergVKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495091093 163 SYKALDyplkiaLESELL---SIVK-KERKTVVFITH---DIEEAvtmsDRVYVMkaHPGEII 218
Cdd:cd03251 165 ATSALD------TESERLvqaALERlMKNRTTFVIAHrlsTIENA----DRIVVL--EDGKIV 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-220 |
2.84e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.33 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGAAGpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHT---- 76
Cdd:PRK13642 1 MNKILEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 77 SPKIGYVLQK-DLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDP 155
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 156 QIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTmSDRVYVMKAhpGEIINE 220
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKA--GEIIKE 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
18-216 |
4.29e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.71 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 18 AGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGhTSP-----KIGYVLQKDLLFPw 92
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST-LKPeiyrqQVSYCAQTPTLFG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 93 RTVIDNVVLGLEIAGvsKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPL 171
Cdd:PRK10247 95 DTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495091093 172 KIALESELLSIVKKERKTVVFITHDIEEaVTMSDRVYVMKAHPGE 216
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGE 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-218 |
6.81e-26 |
|
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: 101.46 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 21 VQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG----HTSPKIGYVLQKDLLFPwRTVI 96
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnlrWLRSQIGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 97 DNVVLGLEIAgvsKREARERAKALLQTYR-----MEGYE----DKfPSQISGGMRQRVALMRTMITDPQIILMDESYKAL 167
Cdd:cd03249 95 ENIRYGKPDA---TDEEVEEAAKKANIHDfimslPDGYDtlvgER-GSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 168 DYplkialESEL-----LSIVKKERKTVVfITHDIeEAVTMSDRVYVMkaHPGEII 218
Cdd:cd03249 171 DA------ESEKlvqeaLDRAMKGRTTIV-IAHRL-STIRNADLIAVL--QNGQVV 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-220 |
7.08e-26 |
|
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: 101.54 E-value: 7.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP----KIGYVLQKDLLFPwRTVID 97
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslrrAIGVVPQDTVLFN-DTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 98 NVVLGLEiaGVSKREARERAKALLQTYRMEGYEDKFPSQ-------ISGGMRQRVALMRTMITDPQIILMDESYKALDYP 170
Cdd:cd03253 94 NIRYGRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495091093 171 LKIALESELLSIVKkeRKTVVFITHDIEEAVTmSDRVYVMKAhpGEIINE 220
Cdd:cd03253 172 TEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKD--GRIVER 216
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
33-211 |
1.74e-25 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 104.82 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 33 ANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETtGHTSP-----KIGYVLQKDLLFPwRTVIDNVVLGLEIAG 107
Cdd:TIGR01846 482 PGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL-AIADPawlrrQMGVVLQENVLFS-RSIRDNIALCNPGAP 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 108 VSK-REARERAKALLQTYRM-EGYEDKFPSQ---ISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSI 182
Cdd:TIGR01846 560 FEHvIHAAKLAGAHDFISELpQGYNTEVGEKganLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREI 639
|
170 180
....*....|....*....|....*....
gi 495091093 183 VKKerKTVVFITHDIeEAVTMSDRVYVMK 211
Cdd:TIGR01846 640 CRG--RTVIIIAHRL-STVRACDRIIVLE 665
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
1.93e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.97 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGAAgpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS--- 77
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 78 -PKIGYVLQK--DLLFPwRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITD 154
Cdd:PRK13647 78 rSKVGLVFQDpdDQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 155 PQIILMDESYKALDyPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:PRK13647 157 PDVIVLDEPMAYLD-PRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKE 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-218 |
2.05e-25 |
|
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: 99.16 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKFYEGAAGPV--QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKP--DNGSILVDNRETTGHTSPK 79
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 -IGYVLQKDLLFPWRTVidnvvlgleiagvskREARERAkALLQtyrmegyedkfpsQISGGMRQRVALMRTMITDPQII 158
Cdd:cd03213 83 iIGYVPQDDILHPTLTV---------------RETLMFA-AKLR-------------GLSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495091093 159 LMDESYKALDYplkiALESELLSIVKKER---KTVVFITHDI-EEAVTMSDRVYVMkaHPGEII 218
Cdd:cd03213 134 FLDEPTSGLDS----SSALQVMSLLRRLAdtgRTIICSIHQPsSEIFELFDKLLLL--SQGRVI 191
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
2.53e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.50 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYegaaGPVQILHK--MKFHAdaNEFVSFVGPSGCGKSTL---FNIITGLLkPDN---GSILVDNRET 72
Cdd:COG1117 8 LEPKIEVRNLNVYY----GDKQALKDinLDIPE--NKVTALIGPSGCGKSTLlrcLNRMNDLI-PGArveGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 73 TGHTSP------KIGYVLQKDLLFPWrTVIDNVVLGLEIAGV-SKREARERA-KALLQTY-------RMegyeDKFPSQI 137
Cdd:COG1117 81 YDPDVDvvelrrRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIkSKSELDEIVeESLRKAAlwdevkdRL----KKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 138 SGGMRQRVALMRTMITDPQIILMDESYKALDyP---LKI-ALESELlsivkKERKTVVFITHDIEEAVTMSDRVYVMkaH 213
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALD-PistAKIeELILEL-----KKDYTIVIVTHNMQQAARVSDYTAFF--Y 227
|
....*
gi 495091093 214 PGEII 218
Cdd:COG1117 228 LGELV 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-223 |
3.44e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 100.26 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYE-----GAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK 79
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLY-QLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQKD--LLF--------PWRTVIDNVVLGLE-IAGVSKREARERAKALLQTYRMEG-YEDKFPSQISGGMRQRVAL 147
Cdd:TIGR02769 82 QRRAFRRDvqLVFqdspsavnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 148 MRTMITDPQIILMDESYKALDyplkIALESELLSIVKKERK----TVVFITHDIEEAVTMSDRVYVMkaHPGEIINEIKI 223
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKLQQafgtAYLFITHDLRLVQSFCQRVAVM--DKGQIVEECDV 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-206 |
3.71e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIIT--GLLKPD---------NGSILVDNRETT 73
Cdd:PRK14239 6 LQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtitgsivyNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 74 GHTSPKIGYVLQKDLLFPWrTVIDNVVLGLEIAGVSKREARERA--KALLQTYRMEGYEDKFPSQ---ISGGMRQRVALM 148
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAveKSLKGASIWDEVKDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 149 RTMITDPQIILMDESYKALDyPLKIA-LESELLSIvkKERKTVVFITHDIEEAVTMSDR 206
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALD-PISAGkIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-212 |
3.86e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 101.04 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 27 MKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG---HTSPKIGYVLQKDLLFPWRTVIDNVVLGL 103
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSrarHARQRVGVVPQFDNLDPDFTVRENLLVFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 104 EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLKIALESELLSIV 183
Cdd:PRK13537 106 RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD-PQARHLMWERLRSL 184
|
170 180
....*....|....*....|....*....
gi 495091093 184 KKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:PRK13537 185 LARGKTILLTTHFMEEAERLCDRLCVIEE 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-207 |
7.41e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 98.73 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP------ 78
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 --KIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQ 156
Cdd:PRK11629 86 nqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495091093 157 IILMDESYKALDYPLKIALeSELLSIVKKERKTV-VFITHDIEEAVTMSDRV 207
Cdd:PRK11629 166 LVLADEPTGNLDARNADSI-FQLLGELNRLQGTAfLVVTHDLQLAKRMSRQL 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-210 |
8.27e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 100.72 E-value: 8.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 41 GPSGCGKSTLFNIITGLLKPDNGSILVDNR-----ETTGHTSP---KIGYVLQKDLLFPWRTVIDNVVLGLeiagvsKRE 112
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaEKGICLPPekrRIGYVFQDARLFPHYKVRGNLRYGM------AKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 113 ARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKialeSELLSIVKKERKTV-- 190
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK----RELLPYLERLAREIni 180
|
170 180
....*....|....*....|..
gi 495091093 191 --VFITHDIEEAVTMSDRVYVM 210
Cdd:PRK11144 181 piLYVSHSLDEILRLADRVVVL 202
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
1.31e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 97.89 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISK-FYEGAAGPVQI--LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDN-------- 69
Cdd:COG4778 1 MTTLLEVENLSKtFTLHLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwvdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 70 ----------RETTghtspkIGYVLQkdllF----PWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRM-EGYEDKFP 134
Cdd:COG4778 81 qaspreilalRRRT------IGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 135 SQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALeSELLSIVKKERKTVVFITHDIE--EAVtmSDRVYVMKA 212
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVV-VELIEEAKARGTAIIGIFHDEEvrEAV--ADRVVDVTP 227
|
.
gi 495091093 213 H 213
Cdd:COG4778 228 F 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-218 |
1.56e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.26 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISkfYegAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHtSP----KI 80
Cdd:COG4559 2 LEAENLS--V--RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAW-SPwelaRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVL--QKDLLFPWrTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMI------ 152
Cdd:COG4559 77 RAVLpqHSSLAFPF-TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 153 -TDPQIILMDESYKALDyplkIALESELLSIVKK---ERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG4559 156 dGGPRWLFLDEPTSALD----LAHQHAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQ--GRLV 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-196 |
8.52e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 8.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNREttghtspKIGYVLQKDL 88
Cdd:COG0488 3 NLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-------RIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 89 LFPWRTVIDNVVLGL-EIAGVSKREARERAK-----------ALLQTY--RMEGYE-------------------DKFPS 135
Cdd:COG0488 72 LDDDLTVLDTVLDGDaELRALEAELEELEAKlaepdedlerlAELQEEfeALGGWEaearaeeilsglgfpeedlDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 136 QISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELlsivKKERKTVVFITHD 196
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-197 |
1.05e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.33 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 10 ISKFYEGAAgpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIL--------VDNRETTgHTSPKIG 81
Cdd:PRK10908 7 VSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghditrLKNREVP-FLRRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMD 161
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 495091093 162 ESYKALDYplkiALESELLSIVKKERK---TVVFITHDI 197
Cdd:PRK10908 163 EPTGNLDD----ALSEGILRLFEEFNRvgvTVLMATHDI 197
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-233 |
1.51e-23 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 95.67 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKIGYVL 84
Cdd:TIGR02323 4 LQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QKDLL-FPWRTVIDNVVLGLEI-----AGVSKR----------EARERAKALLQTYRME-GYEDKFPSQISGGMRQRVAL 147
Cdd:TIGR02323 80 RRRLMrTEWGFVHQNPRDGLRMrvsagANIGERlmaigarhygNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 148 MRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEIINEIKIDLET 227
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQ--GRVVESGLTDQVL 237
|
....*.
gi 495091093 228 DSPLIP 233
Cdd:TIGR02323 238 DDPQHP 243
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-210 |
1.92e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.03 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 3 HTLEAIDISKFYEGAagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKI-- 80
Cdd:PRK13652 2 HLIETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 --GYVLQK--DLLFPwRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQ 156
Cdd:PRK13652 79 fvGLVFQNpdDQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 157 IILMDESYKALDyPLKIA-LESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVM 210
Cdd:PRK13652 158 VLVLDEPTAGLD-PQGVKeLIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-220 |
1.95e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.96 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKFYEGAagpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG---HTSPK- 79
Cdd:PRK10895 3 TLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplHARARr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 -IGYVLQKDLLFPWRTVIDNVVLGLEI-AGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:PRK10895 79 gIGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 158 ILMDESYKALDyPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK-----AH--PGEIINE 220
Cdd:PRK10895 159 ILLDEPFAGVD-PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSqghliAHgtPTEILQD 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
28-210 |
2.42e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.06 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 28 KFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKI---GYV--LQKDLLFPWRTVIDNVVL- 101
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIarmGVVrtFQHVRLFREMTVIENLLVa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 102 -------GLeIAGV--------SKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKA 166
Cdd:PRK11300 105 qhqqlktGL-FSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495091093 167 LDYPLKIALeSELLSIVKKERK-TVVFITHDIEEAVTMSDRVYVM 210
Cdd:PRK11300 184 LNPKETKEL-DELIAELRNEHNvTVLLIEHDMKLVMGISDRIYVV 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-210 |
2.53e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.20 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK----IGYVLQK-DLLFPWRTVIDN 98
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrkhIGIVFQNpDNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 99 VVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKialeSE 178
Cdd:PRK13648 105 VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR----QN 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 495091093 179 LLSIVK--KERK--TVVFITHDIEEAVTmSDRVYVM 210
Cdd:PRK13648 181 LLDLVRkvKSEHniTIISITHDLSEAME-ADHVIVM 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-218 |
3.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.11 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG------HTSPKIGYVLQ--KDLLFPwRTV 95
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvklsDIRKKVGLVFQypEYQLFE-ETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 96 IDNVVLGLEIAGVSKREARERAKALLQTYRM--EGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKI 173
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495091093 174 ALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM--NKGKCE 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-196 |
3.61e-23 |
|
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: 97.82 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKFYEGAAgpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT----GHTSPK 79
Cdd:TIGR02868 334 TLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSsldqDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQKDLLFPwRTVIDNVVLGL-EIAGVSKREARERAK------AL---LQTYRMEGyedkfPSQISGGMRQRVALMR 149
Cdd:TIGR02868 411 VSVCAQDAHLFD-TTVRENLRLARpDATDEELWAALERVGladwlrALpdgLDTVLGEG-----GARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495091093 150 TMITDPQIILMDESYKALDyplkIALESELLSIVKK--ERKTVVFITHD 196
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLD----AETADELLEDLLAalSGRTVVLITHH 529
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-210 |
6.58e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.42 E-value: 6.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYE------GAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG 74
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 75 HTSP-------KIGYVLQKDL--LFPWRTVIDNVVLGLEI-AGVSKREARERAKALLQT--YRMEGYeDKFPSQISGGMR 142
Cdd:PRK11308 82 ADPEaqkllrqKIQIVFQNPYgsLNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKvgLRPEHY-DRYPHMFSGGQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 143 QRVALMRTMITDPQIILMDESYKALDyplkIALESELLSI---VKKERKTV-VFITHDIEEAVTMSDRVYVM 210
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALD----VSVQAQVLNLmmdLQQELGLSyVFISHDLSVVEHIADEVMVM 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-221 |
8.06e-23 |
|
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: 96.80 E-value: 8.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGAA-GPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILV--------------DNRett 73
Cdd:TIGR03269 284 NVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpDGR--- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 74 GHTSPKIGYVLQKDLLFPWRTVIDNVV--LGLEIAgvsKREARERAkalLQTYRMEGYE--------DKFPSQISGGMRQ 143
Cdd:TIGR03269 361 GRAKRYIGILHQEYDLYPHRTVLDNLTeaIGLELP---DELARMKA---VITLKMVGFDeekaeeilDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 144 RVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK-------AHPGE 216
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRdgkivkiGDPEE 514
|
....*
gi 495091093 217 IINEI 221
Cdd:TIGR03269 515 IVEEL 519
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-223 |
1.10e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.60 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYE-----GAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVD-------NRET 72
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplaklNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 73 TGHTSPKIGYVLQKDL--LFPWRTVIDNVVLGLE-IAGVSKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVALM 148
Cdd:PRK10419 84 RKAFRRDIQMVFQDSIsaVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 149 RTMITDPQIILMDESYKALDyplkIALESELLSIVKKERK----TVVFITHDIEEAVTMSDRVYVMkaHPGEIINEIKI 223
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLD----LVLQAGVIRLLKKLQQqfgtACLFITHDLRLVERFCQRVMVM--DNGQIVETQPV 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-218 |
1.19e-22 |
|
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: 96.29 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAI-DISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLkPDN-----GSILVDNRETTG 74
Cdd:COG4172 2 MSMPLLSVeDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDPaahpsGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 75 HTSP--------KIGYVLQKDL--LFPWRTVIDNVVLGLEI-AGVSKREARERAKALLQ-------TYRMegyeDKFPSQ 136
Cdd:COG4172 81 LSERelrrirgnRIAMIFQEPMtsLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLErvgipdpERRL----DAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 137 ISGGMRQRValmrtMI-----TDPQIILMDESYKALDYPL--KIaLesELLSIVKKERKT-VVFITHDIeeAVT--MSDR 206
Cdd:COG4172 157 LSGGQRQRV-----MIamalaNEPDLLIADEPTTALDVTVqaQI-L--DLLKDLQRELGMaLLLITHDL--GVVrrFADR 226
|
250
....*....|..
gi 495091093 207 VYVMKAhpGEII 218
Cdd:COG4172 227 VAVMRQ--GEIV 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-211 |
1.62e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.74 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK--------IGYVLQ--KDLLFPwR 93
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrkkVSLVFQfpEAQLFE-N 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 94 TVIDNVVLGLEIAGVSKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLK 172
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD-PEG 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 495091093 173 IALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLE 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-218 |
1.82e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.91 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKFYEGAagpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP----K 79
Cdd:PRK13548 2 MLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-DWSPaelaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVL--QKDLLFPWrTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMI----- 152
Cdd:PRK13548 77 RRAVLpqHSSLSFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 153 -TDPQIILMDESYKALDyplkIALESELLSIVK----KERKTVVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:PRK13548 156 dGPPRWLLLDEPTSALD----LAHQHHVLRLARqlahERGLAVIVVLHDLNLAARYADRIVLL--HQGRLV 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-218 |
2.35e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.68 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKIGyvl 84
Cdd:PRK11701 7 LSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QKDLLFPWRT----VIDNVVLGLEI---AG--VSKR----------EARERAKALLQtyRME---GYEDKFPSQISGGMR 142
Cdd:PRK11701 80 EAERRRLLRTewgfVHQHPRDGLRMqvsAGgnIGERlmavgarhygDIRATAGDWLE--RVEidaARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 143 QRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ--GRVV 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
22-211 |
3.04e-22 |
|
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: 90.06 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT---GHTSPKIGYVLQKDLLFPwRTVIDN 98
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdleKALSSLISVLNQRPYLFD-TTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 99 vvLGLeiagvskrearerakallqtyrmegyedkfpsQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLKialESE 178
Cdd:cd03247 95 --LGR--------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLD-PIT---ERQ 136
|
170 180 190
....*....|....*....|....*....|....*
gi 495091093 179 LLSIVKK--ERKTVVFITHDIeEAVTMSDRVYVMK 211
Cdd:cd03247 137 LLSLIFEvlKDKTLIWITHHL-TGIEHMDKILFLE 170
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
35-200 |
3.78e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 91.38 E-value: 3.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 35 EFVSFVGPSGCGKSTLFNIITGLlkpDNGS-----IL------VDNRETTGHTSPKIGYVLQKDLLFPWRTVIDNVVLGL 103
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGL---DDGSsgevsLVgqplhqMDEEARAKLRAKHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 104 EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIV 183
Cdd:PRK10584 114 LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLN 193
|
170
....*....|....*..
gi 495091093 184 KKERKTVVFITHDIEEA 200
Cdd:PRK10584 194 REHGTTLILVTHDLQLA 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-200 |
4.54e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.99 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 14 YEGAagPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIlvdnretTGHTSPKIGYVLQK---DLLF 90
Cdd:NF040873 2 YGGR--PV--LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------RRAGGARVAYVPQRsevPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 91 PwRTVIDNVVLGL----EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKA 166
Cdd:NF040873 71 P-LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 495091093 167 LDYplkiALESELLSIVKKER---KTVVFITHDIEEA 200
Cdd:NF040873 150 LDA----ESRERIIALLAEEHargATVVVVTHDLELV 182
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-210 |
7.74e-22 |
|
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: 90.61 E-value: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 21 VQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS----PKIGYVLQKDLLFPwRTVI 96
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHkylhSKVSLVGQEPVLFA-RSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 97 DNVVLGLeiAGVSKrearERAKALLQTYRMEGYEDKFP-----------SQISGGMRQRVALMRTMITDPQIILMDESYK 165
Cdd:cd03248 106 DNIAYGL--QSCSF----ECVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495091093 166 ALDYPLKIALESELLSivKKERKTVVFITHDIeEAVTMSDRVYVM 210
Cdd:cd03248 180 ALDAESEQQVQQALYD--WPERRTVLVIAHRL-STVERADQILVL 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
22-218 |
1.08e-21 |
|
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: 90.53 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNG---SILvdnRETTGHTS-----PKIGYV---LQKDllF 90
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF---GERRGGEDvwelrKRIGLVspaLQLR--F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 91 PWRTVIDNVVL-GLE-IAGVSKR---EARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYK 165
Cdd:COG1119 92 PRDETVLDVVLsGFFdSIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495091093 166 ALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKahPGEII 218
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLK--DGRVV 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
36-218 |
1.17e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.23 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 36 FVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK--------IGYVLQkdllFP-----WRTVIDNVVLG 102
Cdd:PRK13634 35 YVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkplrkkVGIVFQ----FPehqlfEETVEKDICFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 103 LEIAGVSKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLKIALESELLS 181
Cdd:PRK13634 111 PMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD-PKGRKEMMEMFY 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 495091093 182 IVKKERK-TVVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:PRK13634 190 KLHKEKGlTTVLVTHSMEDAARYADQIVVM--HKGTVF 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-218 |
1.37e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.45 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 12 KFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDN----------RETTGHTSPKI- 80
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhELITNPYSKKIk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 ---------GYVLQkdllFPW-----RTVIDNVVLGLEIAGVSKREARERAKALLQtyRM---EGYEDKFPSQISGGMRQ 143
Cdd:PRK13631 110 nfkelrrrvSMVFQ----FPEyqlfkDTIEKDIMFGPVALGVKKSEAKKLAKFYLN--KMgldDSYLERSPFGLSGGQKR 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 144 RVALMRTMITDPQIILMDESYKALDyPlkiALESELLSIV---KKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLD-P---KGEHEMMQLIldaKANNKTVFVITHTMEHVLEVADEVIVMDK--GKIL 255
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-218 |
1.58e-21 |
|
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: 89.57 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDN--------RETTGHtspkIGYVLQKDLLFpWRTV 95
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpADLRRN----IGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 96 IDNVVLG------------LEIAGVSK----------REARERAKALlqtyrmegyedkfpsqiSGGMRQRVALMRTMIT 153
Cdd:cd03245 95 RDNITLGapladderilraAELAGVTDfvnkhpngldLQIGERGRGL-----------------SGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 154 DPQIILMDESYKALDYplkiALESELLSIVKKER--KTVVFITHDIeEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03245 158 DPPILLLDEPTSAMDM----NSEERLKERLRQLLgdKTLIIITHRP-SLLDLVDRIIVMDS--GRIV 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-196 |
3.16e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGaagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIlvdnreTTGHTSpKIGYVL 84
Cdd:COG0488 316 LELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------KLGETV-KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QK-DLLFPWRTVIDNVVLGLEiaGVSKREARERAKALLQTYRMegyEDKFPSQISGGMRQRVALMRTMITDPQIILMDES 163
Cdd:COG0488 385 QHqEELDPDKTVLDELRDGAP--GGTEQEVRGYLGRFLFSGDD---AFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
170 180 190
....*....|....*....|....*....|....
gi 495091093 164 YKALDYPLKIALEsELLsivkKERK-TVVFITHD 196
Cdd:COG0488 460 TNHLDIETLEALE-EAL----DDFPgTVLLVSHD 488
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-218 |
3.68e-21 |
|
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: 92.09 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHT----SPKI 80
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPA--LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlaslRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQKDLLFPwRTVIDNVVLGlEIAGVSKREARErakALLQTYRMEgYEDKFP-----------SQISGGMRQRVALMR 149
Cdd:TIGR02203 409 ALVSQDVVLFN-DTIANNIAYG-RTEQADRAEIER---ALAAAYAQD-FVDKLPlgldtpigengVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 150 TMITDPQIILMDESYKALDYplkialESE-----LLSIVKKERKTVVfITH---DIEEAvtmsDRVYVMKAhpGEII 218
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDN------ESErlvqaALERLMQGRTTLV-IAHrlsTIEKA----DRIVVMDD--GRIV 546
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
33-205 |
3.97e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 33 ANEFVSFVGPSGCGKSTL---FNIITGLLKP--DNGSILVDNRET-TGHTSP-----KIGYVLQKDLLFPwRTVIDNVVL 101
Cdd:PRK14243 35 KNQITAFIGPSGCGKSTIlrcFNRLNDLIPGfrVEGKVTFHGKNLyAPDVDPvevrrRIGMVFQKPNPFP-KSIYDNIAY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 102 GLEIAG--VSKREARERAkaLLQTYRMEGYEDKFP---SQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLKIALE 176
Cdd:PRK14243 114 GARINGykGDMDELVERS--LRQAALWDEVKDKLKqsgLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD-PISTLRI 190
|
170 180
....*....|....*....|....*....
gi 495091093 177 SELLSIVkKERKTVVFITHDIEEAVTMSD 205
Cdd:PRK14243 191 EELMHEL-KEQYTIIIVTHNMQQAARVSD 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-217 |
4.84e-21 |
|
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: 87.10 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGhTSP------KIGYVL---QKDLLFPWRTVIDNV 99
Cdd:cd03215 21 FEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR-RSPrdairaGIAYVPedrKREGLVLDLSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 VLgleiagvskrearerakallqtyrmegyedkfPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyplkIALESEL 179
Cdd:cd03215 100 AL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VGAKAEI 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495091093 180 LSIVKKER---KTVVFITHDIEEAVTMSDRVYVMKAhpGEI 217
Cdd:cd03215 144 YRLIRELAdagKAVLLISSELDELLGLCDRILVMYE--GRI 182
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-218 |
5.15e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 88.75 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHT--SP 78
Cdd:PRK14267 1 MKFAIETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNiySP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 ---------KIGYVLQKDLLFPWRTVIDNVVLGLEIAGV--SKREARERAK-ALLQTYRMEGYEDK---FPSQISGGMRQ 143
Cdd:PRK14267 77 dvdpievrrEVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEwALKKAALWDEVKDRlndYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 144 RVALMRTMITDPQIILMDESYKALDyPLKIALESELLSIVKKERkTVVFITHDIEEAVTMSDrvYVMKAHPGEII 218
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANID-PVGTAKIEELLFELKKEY-TIVLVTHSPAQAARVSD--YVAFLYLGKLI 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-218 |
7.20e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.18 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 18 AGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVD-------NRETTGHTspkIGYVLQKDLLF 90
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdirtvTRASLRRN---IAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 91 PwRTVIDNVVLGLEIAGVSK-REARERAKALlqtYRMEGYEDKFP-------SQISGGMRQRVALMRTMITDPQIILMDE 162
Cdd:PRK13657 422 N-RSIEDNIRVGRPDATDEEmRAAAERAQAH---DFIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495091093 163 SYKALDYP----LKIALESellsiVKKERKTVVfITH---DIEEAvtmsDRVYVMkaHPGEII 218
Cdd:PRK13657 498 ATSALDVEteakVKAALDE-----LMKGRTTFI-IAHrlsTVRNA----DRILVF--DNGRVV 548
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-220 |
8.69e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.68 E-value: 8.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYE-GAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK-------- 79
Cdd:PRK13646 7 NVSYTYQkGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrkr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 IGYVLQ--KDLLFPwRTVIDNVVLGLEIAGVSKREARERAKALLqtyrME-GYE----DKFPSQISGGMRQRVALMRTMI 152
Cdd:PRK13646 87 IGMVFQfpESQLFE-DTVEREIIFGPKNFKMNLDEVKNYAHRLL----MDlGFSrdvmSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 153 TDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEIINE 220
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKE--GSIVSQ 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
40-218 |
1.22e-20 |
|
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: 90.51 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLkPDNGSILVDNRETTGhtspkigyvLQKDLLFPWR------------------TVIDNVVL 101
Cdd:COG4172 318 VGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDG---------LSRRALRPLRrrmqvvfqdpfgslsprmTVGQIIAE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 102 GLEI--AGVSKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLK---IAL 175
Cdd:COG4172 388 GLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQaqiLDL 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495091093 176 eseLLSIVKKERKTVVFITHDIeeAV--TMSDRVYVMKAhpGEII 218
Cdd:COG4172 468 ---LRDLQREHGLAYLFISHDL--AVvrALAHRVMVMKD--GKVV 505
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-218 |
1.27e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.60 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYE-GAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIL------VDNRETTGHTS 77
Cdd:PRK13651 3 IKVKNIVKIFNkKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 78 PKIGYVLQ----------KDL--------------LFPwRTVIDNVVLGLEIAGVSKREARERAKALLQTYRM-EGYEDK 132
Cdd:PRK13651 83 VLEKLVIQktrfkkikkiKEIrrrvgvvfqfaeyqLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 133 FPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD-PQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*.
gi 495091093 213 hpGEII 218
Cdd:PRK13651 241 --GKII 244
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-220 |
1.59e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGAAGPVQI--LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRET--TGHT 76
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEKlaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 77 ---SPKIGYVLQK-DLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMI 152
Cdd:PRK13633 81 wdiRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 153 TDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTmSDRVYVMKAhpGEIINE 220
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDS--GKVVME 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
36-218 |
2.09e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.88 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 36 FVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK--------IGYVLQ--KDLLFPwRTVIDNVVLGLEI 105
Cdd:PRK13649 35 YTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqirkkVGLVFQfpESQLFE-ETVLKDVAFGPQN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 106 AGVSKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLKialESELLSIVK 184
Cdd:PRK13649 114 FGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD-PKG---RKELMTLFK 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 495091093 185 KERK---TVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:PRK13649 190 KLHQsgmTIVLVTHLMDDVANYADFVYVLEK--GKLV 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
40-210 |
5.90e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.36 E-value: 5.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLKPDNGSILVD-------NRETTGHTSPKIGYVLQKDLLFPWRTVIDNVVLGLeiagvskRE 112
Cdd:PRK11831 39 MGPSGIGKTTLLRLIGGQIAPDHGEILFDgenipamSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPL-------RE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 113 ARERAKALLQTYRM--------EGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLKIALESELLSIVK 184
Cdd:PRK11831 112 HTQLPAPLLHSTVMmkleavglRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD-PITMGVLVKLISELN 190
|
170 180
....*....|....*....|....*..
gi 495091093 185 KERK-TVVFITHDIEEAVTMSDRVYVM 210
Cdd:PRK11831 191 SALGvTCVVVSHDVPEVLSIADHAYIV 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-218 |
6.69e-20 |
|
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: 85.46 E-value: 6.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 21 VQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSI----LVDNRETTGHTSpKIGYVL-QKDLLFpWR-T 94
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKKFLR-RIGVVFgQKTQLW-WDlP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 95 VIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIA 174
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495091093 175 LEsELLSIVKKERKTVVFIT-HDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:cd03267 192 IR-NFLKEYNRERGTTVLLTsHYMKDIEALARRVLVI--DKGRLL 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
35-210 |
7.73e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.19 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 35 EFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK-----IGYVLQK-DLLFPWRTVIDNVVLGLEIAGV 108
Cdd:PRK13644 29 EYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirklVGIVFQNpETQFVGRTVEEDLAFGPENLCL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 109 SKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKErK 188
Cdd:PRK13644 109 PPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKG-K 187
|
170 180
....*....|....*....|..
gi 495091093 189 TVVFITHDIEEaVTMSDRVYVM 210
Cdd:PRK13644 188 TIVYITHNLEE-LHDADRIIVM 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-221 |
9.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS--------PKIGYVLQ--KDLLFPwR 93
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeikpvrKKVGVVFQfpESQLFE-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 94 TVIDNVVLGLEIAGVSKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLK 172
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 173 IALeSELLSIVKKERKTVVFITHDIEEAVTMSDRVYVM-KAH------PGEIINEI 221
Cdd:PRK13643 181 IEM-MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLeKGHiiscgtPSDVFQEV 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-211 |
1.36e-19 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 87.50 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 16 GAAGPvqILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVD-------NRETTGhtsPKIGYVLQKDL 88
Cdd:COG4618 342 GSKRP--ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDgadlsqwDREELG---RHIGYLPQDVE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 89 LFPwRTVIDN-----------VVLGLEIAGVskrearerakallqtYRM-----EGYEdkfpSQI-------SGGMRQRV 145
Cdd:COG4618 417 LFD-GTIAENiarfgdadpekVVAAAKLAGV---------------HEMilrlpDGYD----TRIgeggarlSGGQRQRI 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 146 ALMRTMITDPQIILMDESYKALDYPLKIALeSELLSIVKKERKTVVFITHDIeEAVTMSDRVYVMK 211
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAAL-AAAIRALKARGATVVVITHRP-SLLAAVDKLLVLR 540
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-218 |
3.28e-19 |
|
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: 83.35 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 11 SKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIlvdnrETTGHTSPKI--GYVLQKDL 88
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-----TVRGRVSSLLglGGGFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 89 lfpwrTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:cd03220 100 -----TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495091093 169 YPLKIALESELLSIVKKERkTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEK--GKIR 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-210 |
5.23e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 86.09 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDN--GSILVDNRETTGHTSPKIGYVLQKDLLFPWRTVIDNVV 100
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 101 ----LGLEiAGVSKREARERAKALLQTYRMEGYED-----KFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPL 171
Cdd:PLN03211 163 fcslLRLP-KSLTKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190
....*....|....*....|....*....|....*....
gi 495091093 172 KIALESELLSIVKKErKTVVFITHDieeavtMSDRVYVM 210
Cdd:PLN03211 242 AYRLVLTLGSLAQKG-KTIVTSMHQ------PSSRVYQM 273
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-211 |
5.85e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 5.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGaagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP-- 78
Cdd:PRK15439 8 APPLLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-RLTPak 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 79 --KIGYVL--QKDLLFPWRTVIDNVVLGLEiagvSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITD 154
Cdd:PRK15439 83 ahQLGIYLvpQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 155 PQIILMDESYKALdyplkIALESE-LLSIVKKERKT---VVFITHDIEEAVTMSDRVYVMK 211
Cdd:PRK15439 159 SRILILDEPTASL-----TPAETErLFSRIRELLAQgvgIVFISHKLPEIRQLADRISVMR 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-195 |
6.17e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.93 E-value: 6.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 21 VQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG------HTspKIGYVLQKDLLFPwRT 94
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhylHR--QVALVGQEPVLFS-GS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 95 VIDNVVLGL------EIAGVSKRE-ARERAKALLQTYRMEGYEDKfpSQISGGMRQRVALMRTMITDPQIILMDESYKAL 167
Cdd:TIGR00958 571 VRENIAYGLtdtpdeEIMAAAKAAnAHDFIMEFPNGYDTEVGEKG--SQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180
....*....|....*....|....*...
gi 495091093 168 DyplkIALESELLSIVKKERKTVVFITH 195
Cdd:TIGR00958 649 D----AECEQLLQESRSRASRTVLLIAH 672
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-220 |
6.88e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.14 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKIGY---VLQKDLLFPWR-TVIDN 98
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARrlaLLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 99 VVLG----LEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIA 174
Cdd:PRK11231 97 VAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495091093 175 LESeLLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA-------HPGEIINE 220
Cdd:PRK11231 177 LMR-LMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANghvmaqgTPEEVMTP 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-210 |
7.86e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.99 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAID-IS-KFYEGaagpvqilhkmkfhadanEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG------- 74
Cdd:PRK15079 33 TLKAVDgVTlRLYEG------------------ETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddewr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 75 HTSPKIGYVLQKDL--LFPWRTVIDNVVLGLEI--AGVSKREARERAKA-LLQTYRMEGYEDKFPSQISGGMRQRVALMR 149
Cdd:PRK15079 95 AVRSDIQMIFQDPLasLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAmMLKVGLLPNLINRYPHEFSGGQCQRIGIAR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 150 TMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVM 210
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-218 |
8.21e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.44 E-value: 8.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFY------------------EGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDN 62
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 63 GSILVDnrettGHTSPKIGY--VLQKDLlfpwrTVIDNVVLGLEIAGVSKREARERAKAL-------------LQTYrme 127
Cdd:COG1134 81 GRVEVN-----GRVSALLELgaGFHPEL-----TGRENIYLNGRLLGLSRKEIDEKFDEIvefaelgdfidqpVKTY--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 128 gyedkfpsqiSGGMRQRVALMRTMITDPQIILMDESY---------KALDyplkiALESellsiVKKERKTVVFITHDIE 198
Cdd:COG1134 148 ----------SSGMRARLAFAVATAVDPDILLVDEVLavgdaafqkKCLA-----RIRE-----LRESGRTVIFVSHSMG 207
|
250 260
....*....|....*....|
gi 495091093 199 EAVTMSDRVYVMKAhpGEII 218
Cdd:COG1134 208 AVRRLCDRAIWLEK--GRLV 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-220 |
1.16e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.44 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP----KIGYVL 84
Cdd:COG4604 6 NVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSrelaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QKDLLFPWR-TVIDNVVLG--------LeiaGVSKREARERAKALLQtyrMEGYEDKFPSQISGGMRQRVALMRTMITDP 155
Cdd:COG4604 81 RQENHINSRlTVRELVAFGrfpyskgrL---TAEDREIIDEAIAYLD---LEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495091093 156 QIILMDESYKALDypLKIALE--SELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAH-------PGEIINE 220
Cdd:COG4604 155 DYVLLDEPLNNLD--MKHSVQmmKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGrvvaqgtPEEIITP 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-218 |
1.44e-18 |
|
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: 84.79 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIL--------VDNRETTGHtspkIGYVLQKDLLFPwRT 94
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILlngfslkdIDRHTLRQF----INYLPQEPYIFS-GS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 95 VIDNVVLGLE--------IAGVSKREARERAKALLQTYRMEGYEDKfpSQISGGMRQRVALMRTMITDPQIILMDESYKA 166
Cdd:TIGR01193 564 ILENLLLGAKenvsqdeiWAACEIAEIKDDIENMPLGYQTELSEEG--SSISGGQKQRIALARALLTDSKVLILDESTSN 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495091093 167 LDYPLKIALESELLSIvkkERKTVVFITHDIEEAvTMSDRVYVMKAhpGEII 218
Cdd:TIGR01193 642 LDTITEKKIVNNLLNL---QDKTIIFVAHRLSVA-KQSDKIIVLDH--GKII 687
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-196 |
1.89e-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: 79.03 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAagpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNREttghtspKIGYVl 84
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------KIGYF- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 qkdllfpwrtvidnvvlgleiagvskrearerakallqtyrmegyedkfpSQISGGMRQRVALMRTMITDPQIILMDESY 164
Cdd:cd03221 69 --------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|..
gi 495091093 165 KALDYPLKIALESELlsivKKERKTVVFITHD 196
Cdd:cd03221 99 NHLDLESIEALEEAL----KEYPGTVILVSHD 126
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-211 |
2.07e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDN----------------GSILVDNRETTGHTspkiGYVLQ 85
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellgrtvqreGRLARDIRKSRANT----GYIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 86 KDLLFPWRTVIDNVVLGleIAGVS----------KREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDP 155
Cdd:PRK09984 94 QFNLVNRLSVLENVLIG--ALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 156 QIILMDESYKALD-YPLKIALESeLLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:PRK09984 172 KVILADEPIASLDpESARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALR 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-218 |
2.75e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 83.74 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKF-YEGA--AGPVQilhkmkFHADANEFVSFVGPSGCGKSTLFNIITGLLkPDNGSILVDNRETT----GHT 76
Cdd:PRK11174 349 TIEAEDLEILsPDGKtlAGPLN------FTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELReldpESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 77 SPKIGYVLQKDLLFPwRTVIDNVVLGLEIAGVSK-REARERAKALLQTYRME-GYEDKFPSQ---ISGGMRQRVALMRTM 151
Cdd:PRK11174 422 RKHLSWVGQNPQLPH-GTLRDNVLLGNPDASDEQlQQALENAWVSEFLPLLPqGLDTPIGDQaagLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 152 ITDPQIILMDESYKALDyplkiaLESE--LLSIVKK--ERKTVVFITHDIEEAVTMsDRVYVMKAhpGEII 218
Cdd:PRK11174 501 LQPCQLLLLDEPTASLD------AHSEqlVMQALNAasRRQTTLMVTHQLEDLAQW-DQIWVMQD--GQIV 562
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-196 |
3.96e-18 |
|
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: 83.45 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYegaaGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIlvdnreTTGHTSpKIGYVL 84
Cdd:TIGR03719 323 IEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI------EIGETV-KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 Q-KDLLFPWRTVIDNVVLGLEIAGVSKREARERakALLQTYRMEGYE-DKFPSQISGGMRQRVALMRTMITDPQIILMDE 162
Cdd:TIGR03719 392 QsRDALDPNKTVWEEISGGLDIIKLGKREIPSR--AYVGRFNFKGSDqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180 190
....*....|....*....|....*....|....
gi 495091093 163 SYKALDYPLKIALESELLSIVkkerKTVVFITHD 196
Cdd:TIGR03719 470 PTNDLDVETLRALEEALLNFA----GCAVVISHD 499
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-210 |
5.98e-18 |
|
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: 83.14 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 34 NEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGH---TSPKIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSK 110
Cdd:TIGR01257 956 NQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNldaVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 111 REARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIvkKERKTV 190
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTI 1113
|
170 180
....*....|....*....|
gi 495091093 191 VFITHDIEEAVTMSDRVYVM 210
Cdd:TIGR01257 1114 IMSTHHMDEADLLGDRIAII 1133
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
30-218 |
7.52e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.60 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 30 HADANEFVSF----------VGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT----GHTSPKIGYVLQ--KDLLFPwR 93
Cdd:PRK15112 25 TVEAVKPLSFtlregqtlaiIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRIRMIFQdpSTSLNP-R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 94 TVIDNVvLGLEIAGVSKREARERAKALLQTYRMEG----YEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDY 169
Cdd:PRK15112 104 QRISQI-LDFPLRLNTDLEPEQREKQIIETLRQVGllpdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495091093 170 PLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM--HQGEVV 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-168 |
9.95e-18 |
|
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: 79.24 E-value: 9.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 21 VQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPD---NGSILVDNRETTGHTSPK-IGYVLQKDLLFPWRTVI 96
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKcVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 97 DNVVLGLEIAG--------VSKREARERAKALLQT----YRMEGyedkfpsqISGGMRQRVALMRTMITDPQIILMDESY 164
Cdd:cd03234 100 ETLTYTAILRLprkssdaiRKKRVEDVLLRDLALTriggNLVKG--------ISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
....
gi 495091093 165 KALD 168
Cdd:cd03234 172 SGLD 175
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-220 |
1.28e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.57 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGL--LKPD---NGSILVDNRET----TGHTSPKIGYVLQKDLL 89
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIfkmdVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 90 FPWRTVIDNVVLGLEIAGV--SKREARERAKALLQTYRM-EGYEDKFPS---QISGGMRQRVALMRTMITDPQIILMDES 163
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 164 YKALDyPLKIALESELLSIVKKErKTVVFITHDIEEAVTMSDrvYVMKAHPGEIINE 220
Cdd:PRK14247 174 TANLD-PENTAKIESLFLELKKD-MTIVLVTHFPQQAARISD--YVAFLYKGQIVEW 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-211 |
2.44e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPKIGYVLQKDLLFPWRTVIDN 98
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN-KLDHKLAAQLGIGIIYQELSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 99 V---------------VLGLEIagVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDES 163
Cdd:PRK09700 95 LtvlenlyigrhltkkVCGVNI--IDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495091093 164 YKAL-----DYPLKIaleselLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:PRK09700 173 TSSLtnkevDYLFLI------MNQLRKEGTAIVYISHKLAEIRRICDRYTVMK 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
29-224 |
4.07e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHtSPK------IGYV---LQKDLLFPWRTVIDNV 99
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR-SPRdairagIAYVpedRKGEGLVLDLSIRENI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 VLG----LEIAG-VSKREARERAKALLQTYRMegyedKFPS------QISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:COG1129 352 TLAsldrLSRGGlLDRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 169 yplkIALESELLSIVK---KERKTVVFITHDIEEAVTMSDRVYVMKAhpGEIINEIKID 224
Cdd:COG1129 427 ----VGAKAEIYRLIRelaAEGKAVIVISSELPELLGLSDRILVMRE--GRIVGELDRE 479
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-211 |
8.91e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.84 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKI-----GYVLQKDLLFPWR 93
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKImreavAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 94 TVIDNVVLGLEIAgvSKREARERAKALLQTY-RMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALdYPLK 172
Cdd:PRK11614 96 TVEENLAMGGFFA--ERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL-APII 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 495091093 173 IALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLE 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
35-211 |
9.43e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.58 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 35 EFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDN------RETTGHTSPKIGYVLQK--DLLFPwRTVIDNVVLGLEIA 106
Cdd:PRK13636 33 EVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysRKGLMKLRESVGMVFQDpdNQLFS-ASVYQDVSFGAVNL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 107 GVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLKIaleSELLSIVKKE 186
Cdd:PRK13636 112 KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD-PMGV---SEIMKLLVEM 187
|
170 180
....*....|....*....|....*....
gi 495091093 187 RK----TVVFITHDIEEAVTMSDRVYVMK 211
Cdd:PRK13636 188 QKelglTIIIATHDIDIVPLYCDNVFVMK 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-212 |
2.67e-16 |
|
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: 74.81 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVdnrettghtSPKIGYVLQKdllfPW---RTVIDNV 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV---------PGSIAYVSQE----PWiqnGTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 VLGLEIagvSKREARE--RAKALLQTYRMegyedkFPSQI-----------SGGMRQRVALMRTMITDPQIILMDESYKA 166
Cdd:cd03250 87 LFGKPF---DEERYEKviKACALEPDLEI------LPDGDlteigekginlSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495091093 167 LD-----YPLKIALESELlsivkKERKTVVFITHDIeEAVTMSDRVYVMKA 212
Cdd:cd03250 158 VDahvgrHIFENCILGLL-----LNNKTRILVTHQL-QLLPHADQIVVLDN 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-181 |
5.36e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.50 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRE-TTGHTSPKIGYV-----LQKDLlfpwrTVI 96
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTaTRGDRSRFMAYLghlpgLKADL-----STL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 97 DNVVLgleIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPLKIALE 176
Cdd:PRK13543 101 ENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLV 176
|
....*
gi 495091093 177 SELLS 181
Cdd:PRK13543 177 NRMIS 181
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-212 |
6.18e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.92 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKS-TLFNIItGLLKPD---NGSILVDNRETTGHT--------SPKIGYVLQK 86
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANgriGGSATFNGREILNLPekelnklrAEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 87 DL--LFPWRTVIDNV--VLGLEiAGVSKREARERAKALLQTYRMEGYEDK---FPSQISGGMRQRVALMRTMITDPQIIL 159
Cdd:PRK09473 106 PMtsLNPYMRVGEQLmeVLMLH-KGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495091093 160 MDESYKALDYPLKiALESELLSIVKKERKT-VVFITHDIEEAVTMSDRVYVMKA 212
Cdd:PRK09473 185 ADEPTTALDVTVQ-AQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYA 237
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-218 |
6.55e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.89 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDN----RETTGHTSpKIGYVL-QK-----DLlfpwrTVIDN 98
Cdd:COG4586 43 FTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKRRKEFAR-RIGVVFgQRsqlwwDL-----PAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 99 VVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESE 178
Cdd:COG4586 117 FRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREF 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495091093 179 LLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:COG4586 197 LKEYNRERGTTILLTSHDMDDIEALCDRVIVI--DHGRII 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-210 |
1.16e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKIG----YVLQKDLL---FP 91
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASrrvaSVPQDTSLsfeFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 92 WRTVIDnvvLG-------LEIAGVSKREARERAKALLQTYRmegYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESY 164
Cdd:PRK09536 94 VRQVVE---MGrtphrsrFDTWTETDRAAVERAMERTGVAQ---FADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495091093 165 KALDYPLKIAlESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVM 210
Cdd:PRK09536 168 ASLDINHQVR-TLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
23-218 |
1.26e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNR--ETTGHTSPKIGYVL-QKDLLFPWRTVIDNV 99
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplSSLSHSVLRQGVAMvQQDPVVLADTFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 VLGLEIAGVSKREARERAK-ALLQTYRMEGYEDKFPSQ---ISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIAL 175
Cdd:PRK10790 436 TLGRDISEEQVWQALETVQlAELARSLPDGLYTPLGEQgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAI 515
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495091093 176 ESELLSIvkKERKTVVFITHDIEEAVTmSDRVYVMkaHPGEII 218
Cdd:PRK10790 516 QQALAAV--REHTTLVVIAHRLSTIVE-ADTILVL--HRGQAV 553
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-218 |
1.51e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.93 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDN----------RETTGHTSPKIGYVLQKDLLFPW 92
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfgkdifQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 93 RTVIDNVVLGLEIAGVskREARERAKALLQTYRMEGY----EDKF---PSQISGGMRQRVALMRTMITDPQIILMDESYK 165
Cdd:PRK14246 105 LSIYDNIAYPLKSHGI--KEKREIKKIVEECLRKVGLwkevYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495091093 166 ALDYPLKIALEsELLSIVKKErKTVVFITHDIEEAVTMSDrvYVMKAHPGEII 218
Cdd:PRK14246 183 MIDIVNSQAIE-KLITELKNE-IAIVIVSHNPQQVARVAD--YVAFLYNGELV 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-216 |
1.84e-15 |
|
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: 73.60 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 34 NEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNrettghtsPKIGYVLQK----------DLLFpwrTVIDNVvlgl 103
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL--------DTVSYKPQYikadyegtvrDLLS---SITKDF---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 104 eiaGVSKREARERAKALlqtyRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIV 183
Cdd:cd03237 90 ---YTHPYFKTEIAKPL----QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180 190
....*....|....*....|....*....|...
gi 495091093 184 KKERKTVVFITHDIEEAVTMSDRVYVMKAHPGE 216
Cdd:cd03237 163 ENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSV 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-218 |
1.93e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.66 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 21 VQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKIgYVLQKDLLF---------- 90
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKL-QALRRDIQFifqdpyasld 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 91 PWRTVIDNVVLGLEIAGV-SKREARERAKALLQTYRME-GYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495091093 169 YPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM--YLGQIV 543
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-218 |
2.32e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.06 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP----KIGYVL 84
Cdd:PRK11176 346 NVTFTYPGKEVPA--LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAslrnQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QKDLLFPwRTVIDNVVLGLEiaGVSKREARERAKALlqTYRME---GYEDKFPSQI-------SGGMRQRVALMRTMITD 154
Cdd:PRK11176 424 QNVHLFN-DTIANNIAYART--EQYSREQIEEAARM--AYAMDfinKMDNGLDTVIgengvllSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 155 PQIILMDESYKALDYPLKIALESElLSIVKKERkTVVFITH---DIEEAvtmsDRVYVMKAhpGEII 218
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAA-LDELQKNR-TSLVIAHrlsTIEKA----DEILVVED--GEIV 557
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-217 |
2.70e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVD----NRETTGHTS--PKIGYVLQKDLLFPWRTV 95
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkplDYSKRGLLAlrQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 96 ID-NVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPlkiA 174
Cdd:PRK13638 95 IDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD-P---A 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495091093 175 LESELLSIVKK---ERKTVVFITHDIEEAVTMSDRVYVMK-------AHPGEI 217
Cdd:PRK13638 171 GRTQMIAIIRRivaQGNHVIISSHDIDLIYEISDAVYVLRqgqilthGAPGEV 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-206 |
5.42e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.82 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 16 GAAGPVqILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKP-----DNGSILVDNRETTGHTS-----PKIGYVLQ 85
Cdd:PRK14271 30 GFAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDvlefrRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 86 KDLLFPwRTVIDNVVLGLEIAG-VSKREARERAKALLQTYRM-EGYEDKF---PSQISGGMRQRVALMRTMITDPQIILM 160
Cdd:PRK14271 109 RPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495091093 161 DESYKALDYPLKIALESELLSIVkkERKTVVFITHDIEEAVTMSDR 206
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDR 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
34-219 |
7.38e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.35 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 34 NEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP---------KIGYVLQkdllFP-----WRTVIDNV 99
Cdd:PRK13645 37 NKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevkrlrkEIGLVFQ----FPeyqlfQETIEKDI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 VLGLEIAGVSKREARERAKALLQTYRM-EGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESE 178
Cdd:PRK13645 113 AFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495091093 179 LLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIIN 219
Cdd:PRK13645 193 FERLNKEYKKRIIMVTHNMDQVLRIADEVIVM--HEGKVIS 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-168 |
8.50e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.54 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPD---NGSILVDNRETTGHTSPKI-GYVLQKDLLFPWRTVID 97
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIsAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 98 NVVLGLEI---AGVSKREARERAKALLQTYRME-------GYEDKFPSqISGGMRQRVALMRTMITDPQIILMDESYKAL 167
Cdd:TIGR00955 119 HLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
.
gi 495091093 168 D 168
Cdd:TIGR00955 198 D 198
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-241 |
1.08e-14 |
|
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: 73.30 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGaagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGL--LKPDNGSIL-----------VDNRE 71
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 72 TTGHTSPKIGYVLQKDLLFPW---------------------------RTVIDNVVLGLEIAGVSKREARERAKALLQTY 124
Cdd:TIGR03269 77 KVGEPCPVCGGTLEPEEVDFWnlsdklrrrirkriaimlqrtfalygdDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 125 RMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITH------DI- 197
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevieDLs 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 495091093 198 EEAVTMSDRVYVMKAHPGEIIN---------EIKIDLETDSPLIPERRMSRRF 241
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAvfmegvsevEKECEVEVGEPIIKVRNVSKRY 289
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-217 |
1.33e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.61 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKF---YEGAagpvQILHKMKFHADANEFVSFVGPSGCGKSTLF------NIITGLLKPDN-----GSIL 66
Cdd:PRK14258 1 MSKLIPAIKVNNLsfyYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESEVRVEGrveffNQNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 67 VDNRETTGHTSPKIGYVLQKDLLFPwRTVIDNVVLGLEIAGVSKR-------EARERAKALLQTYRMEGYEDKFpsQISG 139
Cdd:PRK14258 77 YERRVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDEIKHKIHKSAL--DLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 140 GMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAHPGEI 217
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-218 |
1.49e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 72.93 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDN---RETTgHTSPK--IGYVLQKDLLFpwrtvi 96
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVT-QASLRaaIGIVPQDTVLF------ 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 97 dNVVLGLEIA----GVSKREARERAKAlLQTYRM-----EGYEdkfpSQI-------SGGMRQRVALMRTMITDPQIILM 160
Cdd:COG5265 445 -NDTIAYNIAygrpDASEEEVEAAARA-AQIHDFieslpDGYD----TRVgerglklSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 161 DESYKALDYPLKIALESELLSiVKKERKTVVfITH---DIEEAvtmsDRVYVMKAhpGEII 218
Cdd:COG5265 519 DEATSALDSRTERAIQAALRE-VARGRTTLV-IAHrlsTIVDA----DEILVLEA--GRIV 571
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-196 |
1.56e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.84 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 37 VSFVGPSGCGKSTLFNIITGLLKPDNGSILVdnrettGHTSpKIGYVLQ-KDLLFPWRTVIDNVVLGLEIAGVSKREARE 115
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETV-KLAYVDQsRDALDPNKTVWEEISGGLDIIKVGNREIPS 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 116 RAkallqtyrmegY----------EDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVkk 185
Cdd:PRK11819 426 RA-----------YvgrfnfkggdQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFP-- 492
|
170
....*....|.
gi 495091093 186 erKTVVFITHD 196
Cdd:PRK11819 493 --GCAVVISHD 501
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
40-253 |
1.63e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK------IGYVLQKDLLFPWRTVIDNVVLGLEI----AGVS 109
Cdd:PRK10762 36 VGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNGPKssqeagIGIIHQELNLIPQLTIAENIFLGREFvnrfGRID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 110 KREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALdyplkIALESELLSIVKKERKT 189
Cdd:PRK10762 115 WKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL-----TDTETESLFRVIRELKS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 190 ----VVFITHDIEEAVTMSDRVYVMKahPGEIINEIKI-DLETDSpLIpERRMSRRFNDYYEMIWHNIG 253
Cdd:PRK10762 190 qgrgIVYISHRLKEIFEICDDVTVFR--DGQFIAEREVaDLTEDS-LI-EMMVGRKLEDQYPRLDKAPG 254
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-230 |
1.66e-14 |
|
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: 70.22 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTghTSP------KIGY 82
Cdd:cd03244 7 NVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS--KIGlhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 83 VLQKDLLFPwRTVIDN-----------VVLGLEIAGVskREARERAKALLQTYRMEGyedkfPSQISGGMRQRVALMRTM 151
Cdd:cd03244 83 IPQDPVLFS-GTIRSNldpfgeysdeeLWQALERVGL--KEFVESLPGGLDTVVEEG-----GENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 152 ITDPQIILMDESYKALDYplkiALESELLSIVKKERK--TVVFITHDIeEAVTMSDRVYVMKAhpGEIIneikidlETDS 229
Cdd:cd03244 155 LRKSKILVLDEATASVDP----ETDALIQKTIREAFKdcTVLTIAHRL-DTIIDSDRILVLDK--GRVV-------EFDS 220
|
.
gi 495091093 230 P 230
Cdd:cd03244 221 P 221
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
37-168 |
2.27e-14 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 72.28 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 37 VSFVGPSGCGKSTLFNIITGLLKPDNGSILVDN--RETTGHT--SPKIGYVLQKDLLFPwRTVIDNVVL---GLEIAGVS 109
Cdd:TIGR03796 508 VALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGipREEIPREvlANSVAMVDQDIFLFE-GTVRDNLTLwdpTIPDADLV 586
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 110 kREARERAKALLQTYRMEGYEDKFP---SQISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:TIGR03796 587 -RACKDAAIHDVITSRPGGYDAELAeggANLSGGQRQRLEIARALVRNPSILILDEATSALD 647
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-230 |
7.38e-14 |
|
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: 68.21 E-value: 7.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT----GHTSPKIGYVLQKDLLFPwRTVID 97
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiplEDLRSSLTIIPQDPTLFS-GTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 98 NVVLGLEIAGVSKREARERAkallqtyrmEGYEDkfpsqISGGMRQRVALMRTMITDPQIILMDESYKALDYplkiALES 177
Cdd:cd03369 101 NLDPFDEYSDEEIYGALRVS---------EGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASIDY----ATDA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 178 ELLSIVKKERK--TVVFITHDIeEAVTMSDRVYVMKAhpGEIIneikidlETDSP 230
Cdd:cd03369 163 LIQKTIREEFTnsTILTIAHRL-RTIIDYDKILVMDA--GEVK-------EYDHP 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
29-168 |
7.59e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT-------------GHtSPKIgyvlqKDLLFPWrtv 95
Cdd:PRK13538 22 FTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeyhqdllylGH-QPGI-----KTELTAL--- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495091093 96 iDNVVLGLEIAGVSKREARERAkalLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:PRK13538 93 -ENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-211 |
9.58e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 9.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGaagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRE-----TTGH 75
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasTTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 76 TSPKIGYVLQKDLLFPWRTVIDNVVLG-LEIAG--VSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRV----ALM 148
Cdd:PRK11288 77 LAAGVAIIYQELHLVPEMTVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVeiakALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 149 RtmitDPQIILMDESYKALDyplkiALESE-LLSIV---KKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:PRK11288 157 R----NARVIAFDEPTSSLS-----AREIEqLFRVIrelRAEGRVILYVSHRMEEIFALCDAITVFK 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-213 |
1.22e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNREttghtspKIGYVLQKDLLFPWRTVIDN 98
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-------RIGYVPQKLYLDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 99 VVLGLEiAGVSKRE---ARERAKA--LLQtyrmegyedkFPSQ-ISGGMRQRVALMRTMITDPQIILMDESYKALDYPLK 172
Cdd:PRK09544 88 RFLRLR-PGTKKEDilpALKRVQAghLID----------APMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495091093 173 IALeSELLSIVKKERK-TVVFITHDIEEAVTMSDRVYVMKAH 213
Cdd:PRK09544 157 VAL-YDLIDQLRRELDcAVLMVSHDLHLVMAKTDEVLCLNHH 197
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-168 |
1.26e-13 |
|
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: 67.52 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNR---ETTGHTSPKIGYVLQKDLLFPWRTVIDNV 99
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 100 VLGLEIAGvskREARERAkalLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:cd03231 95 RFWHADHS---DEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-218 |
1.29e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKSTlfniiTGL----LKPDNGSILVD-------NRETTGHTSPKIGYVLQ-- 85
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKST-----TGLallrLINSQGEIWFDgqplhnlNRRQLLPVRHRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 86 KDLLFPWRTVIDNVVLGLEI--AGVSKREARERAKALLQTYRME-GYEDKFPSQISGGMRQRVALMRTMITDPQIILMDE 162
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 163 SYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ--GEVV 505
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-220 |
2.49e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.61 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 20 PVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLK-PdnGSILVDNRETTGHTSPKIGYVLQKDL---------- 88
Cdd:PRK11022 19 PFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMAEKLEFNGQDLQRISEKERRNLvgaevamifq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 89 -----LFPWRTVIDNVVLGLEI-AGVSKREARERAKALLQTYRM---EGYEDKFPSQISGGMRQRVALMRTMITDPQIIL 159
Cdd:PRK11022 97 dpmtsLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 160 MDESYKALDYPLKIALESELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEIINE 220
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA--GQVVET 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-218 |
2.65e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 14 YEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVD-------NR---ETTGHTSPKIGYV 83
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRqviELSEQSAAQMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 84 LQKDLLF----PWRTVIDNVVLGLEIA-------GVSKREARERAKALLQTYRMEGYE---DKFPSQISGGMRQRVALMR 149
Cdd:PRK10261 102 RGADMAMifqePMTSLNPVFTVGEQIAesirlhqGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495091093 150 TMITDPQIILMDESYKALDyplkIALESELLSIVKKERKT----VVFITHDIEEAVTMSDRVYVMkaHPGEII 218
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALD----VTIQAQILQLIKVLQKEmsmgVIFITHDMGVVAEIADRVLVM--YQGEAV 248
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-219 |
4.93e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK----I 80
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrqaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 81 GYVLQKDLLFPwRTVIDNVVLGLEIAGvskreaRERAKALLQTYRMEGYEDKFPS----------QISGGMRQRVALMRT 150
Cdd:PRK11160 417 SVVSQRVHLFS-ATLRDNLLLAAPNAS------DEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495091093 151 MITDPQIILMDESYKALDYplkiALESELLSIVKK--ERKTVVFITHDIEEAVTMsDRVYVMKAhpGEIIN 219
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDA----ETERQILELLAEhaQNKTVLMITHRLTGLEQF-DRICVMDN--GQIIE 553
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-210 |
5.15e-13 |
|
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: 68.50 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS---PKIGYVLQ 85
Cdd:TIGR01257 1942 ELTKVYSGTSSPA--VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISdvhQNMGYCPQ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 86 KDLLFPWRTVIDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYK 165
Cdd:TIGR01257 2020 FDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495091093 166 ALDYPLKIALESELLSIVKKERkTVVFITHDIEEAVTMSDRVYVM 210
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIM 2143
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
40-211 |
2.63e-12 |
|
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: 64.27 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLKPDNGSILVDNR--------ETTGHTSPKIGYVLQKdllfPW---RTVIDNVVLGLEIAgv 108
Cdd:cd03290 33 VGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesepsfeATRSRNRYSVAYAAQK----PWllnATVEENITFGSPFN-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 109 skreaRERAKALLQTYRMEGYEDKFP----SQI-------SGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALES 177
Cdd:cd03290 107 -----KQRYKAVTDACSLQPDIDLLPfgdqTEIgerginlSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQ 181
|
170 180 190
....*....|....*....|....*....|....*
gi 495091093 178 E-LLSIVKKERKTVVFITHDIeEAVTMSDRVYVMK 211
Cdd:cd03290 182 EgILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMK 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
36-218 |
4.02e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 36 FVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP----KIGYVLQKDLLFPWRTVIDNVVLG-LEIAGVSK 110
Cdd:PRK10253 35 FTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevarRIGLLAQNATTPGDITVQELVARGrYPHQPLFT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 111 REARERAKALLQTYRMEGYED---KFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALeSELLSIVKKER 187
Cdd:PRK10253 115 RWRKEDEEAVTKAMQATGITHladQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL-LELLSELNREK 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 495091093 188 K-TVVFITHDIEEA-------VTMSDRVYVMKAHPGEII 218
Cdd:PRK10253 194 GyTLAAVLHDLNQAcryashlIALREGKIVAQGAPKEIV 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-211 |
4.48e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.52 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK-IGYVLQK---DLLFPwRTVIDNV 99
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNlVAYVPQSeevDWSFP-VLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 VLG----LEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIAL 175
Cdd:PRK15056 102 MMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 495091093 176 ESeLLSIVKKERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:PRK15056 182 IS-LLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-168 |
6.00e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISkfyeGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRE-TTGHTSPKIGY 82
Cdd:PRK13539 2 MLEGEDLA----CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiDDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 83 VLQKDLLFPWRTVIDNVVLGLEIAGVSKREARERAKAL-LQ--TYRMEGYedkfpsqISGGMRQRVALMRTMITDPQIIL 159
Cdd:PRK13539 78 LGHRNAMKPALTVAENLEFWAAFLGGEELDIAAALEAVgLAplAHLPFGY-------LSAGQKRRVALARLLVSNRPIWI 150
|
....*....
gi 495091093 160 MDESYKALD 168
Cdd:PRK13539 151 LDEPTAALD 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
32-209 |
1.29e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 32 DANEFVSFVGPSGCGKSTLFNiitgllkpDNGSILVDNRETTGHTSPKI----GYVLQKDLLFPwRTVIDNVVLGLEIAg 107
Cdd:PTZ00265 1254 NVNEFSLTKEGGSGEDSTVFK--------NSGKILLDGVDICDYNLKDLrnlfSIVSQEPMLFN-MSIYENIKFGKEDA- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 108 vskreARERAKALLQTYRMEGYEDKFPSQ-----------ISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALE 176
Cdd:PTZ00265 1324 -----TREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
170 180 190
....*....|....*....|....*....|...
gi 495091093 177 SELLSIVKKERKTVVFITHDIeEAVTMSDRVYV 209
Cdd:PTZ00265 1399 KTIVDIKDKADKTIITIAHRI-ASIKRSDKIVV 1430
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-218 |
1.51e-11 |
|
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: 61.89 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPD---NGSIL---VDNRETTGHTS 77
Cdd:cd03233 3 TLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHyngIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 78 PKIGYVLQKDLLFPWRTVidnvvlgleiagvskREARERAKallqtyRMEGyeDKFPSQISGGMRQRVALMRTMITDPQI 157
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTV---------------RETLDFAL------RCKG--NEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495091093 158 ILMDESYKALDYplKIALE--SELLSIVKKERKTVVF-ITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:cd03233 140 LCWDNSTRGLDS--STALEilKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYE--GRQI 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
40-196 |
1.89e-11 |
|
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: 63.42 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLKPDNGsilvdnrETTGHTSPKIGYVLQKDLLFPWRTVIDNVVLGL-EIAGVSKR------- 111
Cdd:TIGR03719 37 LGLNGAGKSTLLRIMAGVDKDFNG-------EARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVaEIKDALDRfneisak 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 112 --EARERAKALLQtyRMEGYEDKFPSQ---------------------------ISGGMRQRVALMRTMITDPQIILMDE 162
Cdd:TIGR03719 110 yaEPDADFDKLAA--EQAELQEIIDAAdawdldsqleiamdalrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDE 187
|
170 180 190
....*....|....*....|....*....|....
gi 495091093 163 SYKALDYPLKIALESELlsivKKERKTVVFITHD 196
Cdd:TIGR03719 188 PTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
39-230 |
2.22e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.61 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 39 FVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGH---TSPKIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREARE 115
Cdd:NF033858 297 FLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGdiaTRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAA 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 116 RAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDyPlkIALES--ELLSIVKKERKTVVFI 193
Cdd:NF033858 377 RVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD-P--VARDMfwRLLIELSREDGVTIFI 453
|
170 180 190
....*....|....*....|....*....|....*...
gi 495091093 194 -THDIEEAvTMSDRVYVMkaHPGEIineikidLETDSP 230
Cdd:NF033858 454 sTHFMNEA-ERCDRISLM--HAGRV-------LASDTP 481
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-195 |
2.54e-11 |
|
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: 60.63 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVdnrettgHTSPKIGYVLQK----------DLLFPW 92
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-------PEGEDLLFLPQRpylplgtlreQLIYPW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 93 RTVIdnvvlgleiagvskrearerakallqtyrmegyedkfpsqiSGGMRQRVALMRTMITDPQIILMDESYKALDyplk 172
Cdd:cd03223 89 DDVL-----------------------------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALD---- 123
|
170 180
....*....|....*....|...
gi 495091093 173 IALESELLSIVKKERKTVVFITH 195
Cdd:cd03223 124 EESEDRLYQLLKELGITVISVGH 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
37-204 |
6.53e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 37 VSFVGPSGCGKSTLFNIITGLLKPDNGSILVDnrettghTSPKIGYVLQ-KDLLFPWRTVIDNVVLG---LEIAGVS--- 109
Cdd:PRK11147 348 IALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------TKLEVAYFDQhRAELDPEKTVMDNLAEGkqeVMVNGRPrhv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 110 -----------KReARERAKALlqtyrmegyedkfpsqiSGGMRQRVALMRTMITDPQIILMDESYKALDyplkiaLES- 177
Cdd:PRK11147 421 lgylqdflfhpKR-AMTPVKAL-----------------SGGERNRLLLARLFLKPSNLLILDEPTNDLD------VETl 476
|
170 180 190
....*....|....*....|....*....|.
gi 495091093 178 ELL-SIVKKERKTVVFITHD---IEEAVTMS 204
Cdd:PRK11147 477 ELLeELLDSYQGTVLLVSHDrqfVDNTVTEC 507
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-212 |
6.58e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 6.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAI-DISKFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKS-TLFNIITGLLKPD----NGSIL-------- 66
Cdd:PRK15134 1 MTQPLLAIeNLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRfhgesllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 67 VDNRETTGHTSPKIGYVLQKDL--LFPWRTVIDNV--VLGLEiAGVSKREARERAKALLQTYRMEGYEDK---FPSQISG 139
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMvsLNPLHTLEKQLyeVLSLH-RGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 140 GMRQRVALMRTMITDPQIILMDESYKALDyplkIALESELLSIVKKERK----TVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALD----VSVQAQILQLLRELQQelnmGLLFITHNLSIVRKLADRVAVMQN 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
33-228 |
8.61e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.58 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 33 ANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPK------IGYVL---QKDLLFPWRTVIDNVVLGL 103
Cdd:COG3845 283 AGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT-GLSPRerrrlgVAYIPedrLGRGLVPDMSVAENLILGR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 104 EIAG-------VSKREARERAKALLQTY--RMEGYEDKFpSQISGGMRQRVALMRTMITDPQIILMDESYKALDyplkI- 173
Cdd:COG3845 362 YRRPpfsrggfLDRKAIRAFAEELIEEFdvRTPGPDTPA-RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD----Vg 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 174 ALE---SELLSiVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINEIKIDlETD 228
Cdd:COG3845 437 AIEfihQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVM--YEGRIVGEVPAA-EAT 490
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-217 |
1.07e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSPKI----GYVL-----QKDLLFPWRTVIDNV 99
Cdd:PRK15439 284 LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEIN-ALSTAQrlarGLVYlpedrQSSGLYLDAPLAWNV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 V-LGLEIAGVSKREARERAkALLQTYRMEGYEDKFPSQ----ISGGMRQRVALMRTMITDPQIILMDESYKALDyplkIA 174
Cdd:PRK15439 363 CaLTHNRRGFWIKPARENA-VLERYRRALNIKFNHAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD----VS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495091093 175 LESELLSIVK---KERKTVVFITHDIEEAVTMSDRVYVMkaHPGEI 217
Cdd:PRK15439 438 ARNDIYQLIRsiaAQNVAVLFISSDLEEIEQMADRVLVM--HQGEI 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-211 |
1.13e-10 |
|
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: 61.38 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 19 GPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPD--NGSILVDNRETTGH----TSPK-IGYVLQKDLLFP 91
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASnirdTERAgIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 92 WRTVIDNVVLGLEIAGVSKREARE----RAKALLQTYRMEGYEDKFP-SQISGGMRQRVALMRTMITDPQIILMDESYKA 166
Cdd:TIGR02633 92 ELSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495091093 167 LdyplkIALESE-LLSIVKK-ERKTV--VFITHDIEEAVTMSDRVYVMK 211
Cdd:TIGR02633 172 L-----TEKETEiLLDIIRDlKAHGVacVYISHKLNEVKAVCDTICVIR 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-220 |
1.30e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.19 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSP----KIGYVLQKDLLFPWRTVIDN 98
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafarKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 99 VVLG-------LEIAGVSKREARERAKALLQtyrMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDypl 171
Cdd:PRK10575 106 VAIGrypwhgaLGRFGAADREKVEEAISLVG---LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495091093 172 kIALESELLSIVKK---ERK-TVVFITHDIEEAVTMSDrvYVMKAHPGEIINE 220
Cdd:PRK10575 180 -IAHQVDVLALVHRlsqERGlTVIAVLHDINMAARYCD--YLVALRGGEMIAQ 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-196 |
3.36e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSI-----LVDNRettghtspkigyvLQKDllfPWR---- 93
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdLIVAR-------------LQQD---PPRnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 94 TVIDNVVLGL-EIAGVSKR--------EARERAKALLQTYRMEGYED-----KFPSQI------------------SGGM 141
Cdd:PRK11147 82 TVYDFVAEGIeEQAEYLKRyhdishlvETDPSEKNLNELAKLQEQLDhhnlwQLENRInevlaqlgldpdaalsslSGGW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 142 RQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIvkkeRKTVVFITHD 196
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF----QGSIIFISHD 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-185 |
4.12e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDnrettGHTSPKIGYVLQKDLLF--------PWRT 94
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE-----RQSIKKDLCTYQKQLCFvghrsginPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 95 VIDNVVLGLEIAGvSKREARErakaLLQTYRMEGYEDkFP-SQISGGMRQRVALMRTMITDPQIILMDESYKALDyplki 173
Cdd:PRK13540 91 LRENCLYDIHFSP-GAVGITE----LCRLFSLEHLID-YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD----- 159
|
170
....*....|..
gi 495091093 174 alESELLSIVKK 185
Cdd:PRK13540 160 --ELSLLTIITK 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-230 |
5.14e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 12 KFYEGAAGPVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTS-----PKIGYVLQK 86
Cdd:PTZ00265 389 RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINlkwwrSKIGVVSQD 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 87 DLLFPwRTVIDNVVLGL-------------EIAGVSKREARE-----RAKA------LLQTYRMEG-------YE----- 130
Cdd:PTZ00265 469 PLLFS-NSIKNNIKYSLyslkdlealsnyyNEDGNDSQENKNkrnscRAKCagdlndMSNTTDSNEliemrknYQtikds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 131 -------------------DKF-------PSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVK 184
Cdd:PTZ00265 548 evvdvskkvlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495091093 185 KERKTVVFITHDIeEAVTMSDRVYVMKAHpgEIINEIKIDLETDSP 230
Cdd:PTZ00265 628 NENRITIIIAHRL-STIRYANTIFVLSNR--ERGSTVDVDIIGEDP 670
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-224 |
6.63e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHtSPK------IGYVLQ---KDLLFPWRT 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR-SPQdglangIVYISEdrkRDGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 95 VIDNVVLG----LEIAGVSKREARERAkALLQTYRMegYEDKFPSQ------ISGGMRQRVALMRTMITDPQIILMDESY 164
Cdd:PRK10762 347 VKENMSLTalryFSRAGGSLKHADEQQ-AVSDFIRL--FNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 165 KALDYPLKIALeSELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGEIINEIKID 224
Cdd:PRK10762 424 RGVDVGAKKEI-YQLINQFKAEGLSIILVSSEMPEVLGMSDRILVM--HEGRISGEFTRE 480
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
108-224 |
6.71e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.59 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 108 VSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVkKER 187
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDG 194
|
90 100 110
....*....|....*....|....*....|....*..
gi 495091093 188 KTVVFITHDIEEAVTMSDRVYVMKAhpGEIINEIKID 224
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDR--GRVIADGKVD 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
40-196 |
6.73e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.04 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPkiGYvlqKDL---------LFPwrtvidnvvlglEIAGVSK 110
Cdd:COG4615 364 VGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNRE--AY---RQLfsavfsdfhLFD------------RLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 111 REARERAKALLQTYRMEG---YED-KFPS-QISGGMRQRVALMRTMITDPQIILMDE-------SYKALDYplkialeSE 178
Cdd:COG4615 427 EADPARARELLERLELDHkvsVEDgRFSTtDLSQGQRKRLALLVALLEDRPILVFDEwaadqdpEFRRVFY-------TE 499
|
170
....*....|....*...
gi 495091093 179 LLSIVKKERKTVVFITHD 196
Cdd:COG4615 500 LLPELKARGKTVIAISHD 517
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-216 |
7.00e-10 |
|
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: 57.94 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIlvdnrettgHTSPKIGYVLQKDLLFPwRTVIDNVvlg 102
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---------KHSGRISFSSQFSWIMP-GTIKENI--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 103 leIAGVSKREARerAKALLQTYRMEGYEDKFPSQ-----------ISGGMRQRVALMRTMITDPQIILMDESYKALDypl 171
Cdd:cd03291 119 --IFGVSYDEYR--YKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD--- 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495091093 172 kIALESELL-SIVKK--ERKTVVFITHDIEEaVTMSDRVYVMkaHPGE 216
Cdd:cd03291 192 -VFTEKEIFeSCVCKlmANKTRILVTSKMEH-LKKADKILIL--HEGS 235
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
41-168 |
1.39e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.03 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 41 GPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPKIGYVLQKDLLFPWRTVIDNVVLGLEIagvskREARERAKAL 120
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEI-----YNSAETLYAA 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 495091093 121 LQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-212 |
1.47e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.86 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLkPDNGSILVDNRETTGHTSPKI----GYVLQKDllfpwRTVIDNVVLG-L 103
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELarhrAYLSQQQ-----TPPFAMPVFQyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 104 EIAGVSKREARERAKALLQTYRMEGYEDKFP---SQISGGMRQRVALM-------RTMITDPQIILMDESYKALDYPLKI 173
Cdd:PRK03695 91 TLHQPDKTRTEAVASALNEVAEALGLDDKLGrsvNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQA 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 495091093 174 ALESeLLSIVKKERKTVVFITHDIEEAVTMSDRVYVMKA 212
Cdd:PRK03695 171 ALDR-LLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-211 |
3.26e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.03 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 7 AIDISKF-YEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT----GHTSPKIG 81
Cdd:PRK10789 315 DVNIRQFtYPQTDHPA--LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklqlDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 82 YVLQKDLLFPwRTVIDNVVLGLEIAgvsKREARERAKALLQTY----RM-EGYEDKFPSQ---ISGGMRQRVALMRTMIT 153
Cdd:PRK10789 393 VVSQTPFLFS-DTVANNIALGRPDA---TQQEIEHVARLASVHddilRLpQGYDTEVGERgvmLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 154 DPQIILMDESYKALDYplkiALESELLSIVKK--ERKTVVFITHDIeEAVTMSDRVYVMK 211
Cdd:PRK10789 469 NAEILILDDALSAVDG----RTEHQILHNLRQwgEGRTVIISAHRL-SALTEASEILVMQ 523
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
40-195 |
3.38e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 56.74 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLKPDNGSILVdnrettghtsPKigyvlQKDLLF-PWR------TVIDNVVLGLEIAGVSkre 112
Cdd:COG4178 395 TGPSGSGKSTLLRAIAGLWPYGSGRIAR----------PA-----GARVLFlPQRpylplgTLREALLYPATAEAFS--- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 113 aRERAKALLQTYRMEGYEDKFP-----SQI-SGGMRQRVALMRTMITDPQIILMDESYKALDyplkIALESELLSIVKKE 186
Cdd:COG4178 457 -DAELREALEAVGLGHLAERLDeeadwDQVlSLGEQQRLAFARLLLHKPDWLFLDEATSALD----EENEAALYQLLREE 531
|
170
....*....|.
gi 495091093 187 RK--TVVFITH 195
Cdd:COG4178 532 LPgtTVISVGH 542
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
35-218 |
3.82e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 35 EFVSFVGPSGCGKSTLFNIITGLLKPD----NGSILVDNRETTGHTSP--KIGYVLQ--KDLLFPWRTVIDNVVLGLEIA 106
Cdd:PRK10418 30 RVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALRgrKIATIMQnpRSAFNPLHTMHTHARETCLAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 107 GVSKREARerakaLLQTYRMEGYEDK------FPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELL 180
Cdd:PRK10418 110 GKPADDAT-----LTAALEAVGLENAarvlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLE 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 495091093 181 SIVKKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:PRK10418 185 SIVQKRALGMLLVTHDMGVVARLADDVAVMSH--GRIV 220
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
40-196 |
3.97e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLKPDNGsilvdnrETTGHTSPKIGYVLQKDLLFPWRTVIDNVVLGL-EIAGVSKR------- 111
Cdd:PRK11819 39 LGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVaEVKAALDRfneiyaa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 112 --EARERAKALLQtyRMEGYEDKFPSQ---------------------------ISGGMRQRVALMRTMITDPQIILMDE 162
Cdd:PRK11819 112 yaEPDADFDALAA--EQGELQEIIDAAdawdldsqleiamdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDE 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 495091093 163 SYKALDyplkiA-----LESELlsivKKERKTVVFITHD 196
Cdd:PRK11819 190 PTNHLD-----AesvawLEQFL----HDYPGTVVAVTHD 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-215 |
5.42e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 34 NEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILvdnrettghTSPKIGYVLQ----------KDLLFPWRTVIDNVVLGL 103
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---------PELKISYKPQyikpdydgtvEDLLRSITDDLGSSYYKS 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 104 EIAgvsKRearerakalLQTYRMegyEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIV 183
Cdd:PRK13409 436 EII---KP---------LQLERL---LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIA 500
|
170 180 190
....*....|....*....|....*....|..
gi 495091093 184 KKERKTVVFITHDIEEAVTMSDRVYVMKAHPG 215
Cdd:PRK13409 501 EEREATALVVDHDIYMIDYISDRLMVFEGEPG 532
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-218 |
5.91e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.23 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLkPDNGSILVDNRETTGHTSPKI----GYVLQKDLLFPWRTVIDnvVLGLE 104
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELarhrAYLSQQQSPPFAMPVFQ--YLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 105 IAGVSKREAREraKALLQTYRMEGYEDKFP---SQISGGMRQRVALMRTMIT-------DPQIILMDESYKALDyplkIA 174
Cdd:COG4138 94 QPAGASSEAVE--QLLAQLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD----VA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495091093 175 LESELLSIVKK---ERKTVVFITHDIEEAVTMSDRVYVMKAhpGEII 218
Cdd:COG4138 168 QQAALDRLLRElcqQGITVVMSSHDLNHTLRHADRVWLLKQ--GKLV 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
37-196 |
1.13e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 37 VSFVGPSGCGKSTLFNIITGLLKPDNGSILVD--------NRETTGHTSPKIGYVLQKDLLFpwRTVIDNVVL------G 102
Cdd:PRK10636 30 VGLVGKNGCGKSTLLALLKNEISADGGSYTFPgnwqlawvNQETPALPQPALEYVIDGDREY--RQLEAQLHDanerndG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 103 LEIAGV-SKREA------RERAKALLQTYRMEGYEDKFP-SQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIA 174
Cdd:PRK10636 108 HAIATIhGKLDAidawtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIW 187
|
170 180
....*....|....*....|..
gi 495091093 175 LESELlsivKKERKTVVFITHD 196
Cdd:PRK10636 188 LEKWL----KSYQGTLILISHD 205
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-217 |
1.15e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 4 TLEAIDISKFYEG---AAGPVQI-LHKmkfhadaNEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTspk 79
Cdd:PRK10522 322 TLELRNVTFAYQDngfSVGPINLtIKR-------GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 80 igyvlqkdlLFPWRTVIDNV---------VLGLEiagvSKREARERAKALLQTYRMEG---YEDKFPS--QISGGMRQRV 145
Cdd:PRK10522 392 ---------PEDYRKLFSAVftdfhlfdqLLGPE----GKPANPALVEKWLERLKMAHkleLEDGRISnlKLSKGQKKRL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 146 ALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFITHDiEEAVTMSDRVYVMKAhpGEI 217
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRN--GQL 527
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-222 |
1.44e-08 |
|
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: 53.30 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 22 QILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGL--LKPDNGSILVDNRETTghtspkigyvlqkDLlfpwrTVIDNV 99
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT-------------DL-----PPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 VLGL--------EIAGVSKREarerakaLLQtYRMEGYedkfpsqiSGGMRQRVALMRTMITDPQIILMDESYKALDY-P 170
Cdd:cd03217 76 RLGIflafqyppEIPGVKNAD-------FLR-YVNEGF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 171 LKIAleSELLSIVKKERKTVVFITH--DIEEAVTmSDRVYVM------KAHPGEIINEIK 222
Cdd:cd03217 140 LRLV--AEVINKLREEGKSVLIITHyqRLLDYIK-PDRVHVLydgrivKSGDKELALEIE 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-221 |
1.98e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHtSPK----IGYVL-----QKDLLFPWRTVIDNv 99
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR-SPRdairAGIMLcpedrKAEGIIPVHSVADN- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 vlgLEI--------AGVSKREARERAKALLQTYRMEgyeDKFPS------QISGGMRQRVALMRTMITDPQIILMDESYK 165
Cdd:PRK11288 352 ---INIsarrhhlrAGCLINNRWEAENADRFIRSLN---IKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495091093 166 ALDyplkIALESELLSIV---KKERKTVVFITHDIEEAVTMSDRVYVMKAhpGEIINEI 221
Cdd:PRK11288 426 GID----VGAKHEIYNVIyelAAQGVAVLFVSSDLPEVLGVADRIVVMRE--GRIAGEL 478
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-198 |
2.61e-08 |
|
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: 54.53 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIlvdnrettgHTSPKIGYVLQkdllFPW---RTVIDNV 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---------KHSGRISFSPQ----TSWimpGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 VLGLeiagvSKREARERakALLQTYRMEGYEDKFPSQ-----------ISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:TIGR01271 508 IFGL-----SYDEYRYT--SVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190
....*....|....*....|....*....|...
gi 495091093 169 yplkIALESELL-SIVKK--ERKTVVFITHDIE 198
Cdd:TIGR01271 581 ----VVTEKEIFeSCLCKlmSNKTRILVTSKLE 609
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-219 |
3.66e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 5 LEAIDISKFYEGAagpvQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSI-LVDNrettghtsPKIGYV 83
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSEN--------ANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 84 LQ-------KDL-LFPW----RTVIDN--VVLGleIAG---VSKREARERAKALlqtyrmegyedkfpsqiSGGMRQRVA 146
Cdd:PRK15064 388 AQdhaydfeNDLtLFDWmsqwRQEGDDeqAVRG--TLGrllFSQDDIKKSVKVL-----------------SGGEKGRML 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495091093 147 LMRTMITDPQIILMDESYKALDY----PLKIALEsellsivkKERKTVVFITHDIEEAVTMSDRVYVMKahPGEIIN 219
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMDMesieSLNMALE--------KYEGTLIFVSHDREFVSSLATRIIEIT--PDGVVD 515
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-211 |
3.77e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 1 MSHTLEAIDISKFYEGaagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLkPD---NGSILVDNRETTGHT- 76
Cdd:PRK13549 2 MEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 77 --SPKIGYVL--QKDLLFPWRTVIDNVVLGLEI--AGVSKREA-RERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMR 149
Cdd:PRK13549 77 rdTERAGIAIihQELALVKELSVLENIFLGNEItpGGIMDYDAmYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495091093 150 TMITDPQIILMDESYKALDyplkialESE---LLSIVKKERK---TVVFITHDIEEAVTMSDRVYVMK 211
Cdd:PRK13549 157 ALNKQARLLILDEPTASLT-------ESEtavLLDIIRDLKAhgiACIYISHKLNEVKAISDTICVIR 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-253 |
4.12e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT--GHTSPK--IGYVLQKDLLFPwRTVIDN 98
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDLRrvLSIIPQSPVLFS-GTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 99 VVLGLEIAGVSKREARERAKAL---------LQTYRMEGYEDkfpsqISGGMRQRVALMRTMITDPQIILMDESYKALDy 169
Cdd:PLN03232 1330 IDPFSEHNDADLWEALERAHIKdvidrnpfgLDAEVSEGGEN-----FSVGQRQLLSLARALLRRSKILVLDEATASVD- 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 170 plkIALESELLSIVKKERK--TVVFITHDIEEAVTmSDRVYVMKAhpGEIineikidLETDSpliPERRMSRRFNDYYEM 247
Cdd:PLN03232 1404 ---VRTDSLIQRTIREEFKscTMLVIAHRLNTIID-CDKILVLSS--GQV-------LEYDS---PQELLSRDTSAFFRM 1467
|
....*.
gi 495091093 248 IwHNIG 253
Cdd:PLN03232 1468 V-HSTG 1472
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-196 |
7.90e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNIITGLLKPDNGSILVDNREttghtspKIGYVLQKDLLFPWRTVIDNVVLGLEIAGVSKREaRERAKA 119
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-------RLGKLRQDQFAFEEFTVLDTVIMGHTELWEVKQE-RDRIYA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 120 LLQTYRMEGY-----EDKFP-----------------------------SQISGGMRQRVALMRTMITDPQIILMDESYK 165
Cdd:PRK15064 105 LPEMSEEDGMkvadlEVKFAemdgytaearagelllgvgipeeqhyglmSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
|
170 180 190
....*....|....*....|....*....|..
gi 495091093 166 ALDYPLKIALESELlsivkKERK-TVVFITHD 196
Cdd:PRK15064 185 NLDINTIRWLEDVL-----NERNsTMIIISHD 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-199 |
1.20e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTghtsPKIGYVLQKDLlfpwrTVIDNVVLGL 103
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL----IAISSGLNGQL-----TGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 104 EIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPL-KIALESelLSI 182
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFtKKCLDK--MNE 188
|
170
....*....|....*..
gi 495091093 183 VKKERKTVVFITHDIEE 199
Cdd:PRK13545 189 FKEQGKTIFFISHSLSQ 205
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
35-215 |
1.66e-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: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 35 EFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDnRETTGHTSPKIgyvlqkdllfpwrtvidnvvlgleiagvskrear 114
Cdd:cd03222 26 EVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-GITPVYKPQYI---------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 115 erakallqtyrmegyedkfpsQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKERKTVVFIT 194
Cdd:cd03222 71 ---------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVE 129
|
170 180
....*....|....*....|.
gi 495091093 195 HDIEEAVTMSDRVYVMKAHPG 215
Cdd:cd03222 130 HDLAVLDYLSDRIHVFEGEPG 150
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-200 |
1.81e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.34 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLK--PDNGSILVDNREttghtspkigyvlqkdlLFPWRTVIDNVV 100
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ-----------------FGREASLIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 101 LGLEIAgvskreareRAKALLQtyrMEGYEDKF-----PSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIAL 175
Cdd:COG2401 108 RKGDFK---------DAVELLN---AVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|....*..
gi 495091093 176 ESELLSIVKKERKTVVFITH--DIEEA 200
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHhyDVIDD 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-197 |
1.89e-07 |
|
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: 51.87 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIlvdnrettgHTSPKIGYVLQKdllfPW---RTVIDNVV 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV---------HMKGSVAYVPQQ----AWiqnDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 101 LGLEIAGVSKREARErAKALLQTYRMEGYEDKFP-----SQISGGMRQRVALMRTMITDPQIILMDESYKALDYPL-KIA 174
Cdd:TIGR00957 721 FGKALNEKYYQQVLE-ACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHI 799
|
170 180
....*....|....*....|...
gi 495091093 175 LESELLSIVKKERKTVVFITHDI 197
Cdd:TIGR00957 800 FEHVIGPEGVLKNKTRILVTHGI 822
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-200 |
1.92e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGllkpD------NGSILVDNRETTGHT----SPKIGYVlQKDLLFPW 92
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpqgysNDLTLFGRRRGSGETiwdiKKHIGYV-SSSLHLDY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 93 R--TVIDNVVL-------GLEIAgVSKREaRERAKALLQTYRMEGYEDKFPSQ-ISGGmRQRVALM-RTMITDPQIILMD 161
Cdd:PRK10938 350 RvsTSVRNVILsgffdsiGIYQA-VSDRQ-QKLAQQWLDILGIDKRTADAPFHsLSWG-QQRLALIvRALVKHPTLLILD 426
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495091093 162 ESYKALDyPLKIALESELLSIVKKERKT-VVFITHDIEEA 200
Cdd:PRK10938 427 EPLQGLD-PLNRQLVRRFVDVLISEGETqLLFVSHHAEDA 465
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
37-162 |
2.11e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 37 VSFVGPSGCGKSTLFNIITGLLKPDNGSILV------DNRETTgHTSPKIGYVLQ---KDlLFPWRTVIDNVVLGLEIAG 107
Cdd:NF033858 30 VGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggdmaDARHRR-AVCPRIAYMPQglgKN-LYPTLSVFENLDFFGRLFG 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 108 VSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDE 162
Cdd:NF033858 108 QDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-216 |
4.00e-07 |
|
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: 50.55 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 34 NEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIlvdnrettgHTSPKIGYVLQ----------KDLLFPWRTV-IDNVVLG 102
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---------DEDLKISYKPQyispdydgtvEEFLRSANTDdFGSSYYK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 103 LEIAgvsKRearerakalLQTYRMegyEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSI 182
Cdd:COG1245 437 TEII---KP---------LGLEKL---LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180 190
....*....|....*....|....*....|....
gi 495091093 183 VKKERKTVVFITHDIEEAVTMSDRVYVMKAHPGE 216
Cdd:COG1245 502 AENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGV 535
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
40-168 |
5.74e-07 |
|
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: 48.78 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLFNII-----TGLLKpdnGSILVDNRETTGHTSPKIGYVLQKDLLFPWRTVidnvvlgleiagvskREAR 114
Cdd:cd03232 39 MGESGAGKTTLLDVLagrktAGVIT---GEILINGRPLDKNFQRSTGYVEQQDVHSPNLTV---------------REAL 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 495091093 115 eRAKALLQtyrmegyedkfpsQISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:cd03232 101 -RFSALLR-------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-215 |
6.20e-07 |
|
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: 49.29 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 37 VSFVGPSGCGKSTLFNIITGLLKPDNGS---------ILVDNRETT----------GHTSP--KIGYVlqkDLlfpwrtv 95
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeILDEFRGSElqnyftklleGDVKVivKPQYV---DL------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 96 IDNVVLGLEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIAL 175
Cdd:cd03236 99 IPKAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495091093 176 ESELLSIVkKERKTVVFITHDIEEAVTMSDRVYVMKAHPG 215
Cdd:cd03236 179 ARLIRELA-EDDNYVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-243 |
7.05e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 8 IDISKFYEGaagpVQILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTGHTSPK-----IGY 82
Cdd:PRK10982 2 SNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEalengISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 83 VLQKDLLFPWRTVIDNVVLG---LEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIIL 159
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 160 MDESYKALDyplkialESE---LLSIVKKERKT---VVFITHDIEEAVTMSDRVYVMKahPGEIINEIKI-DLETDS--P 230
Cdd:PRK10982 158 MDEPTSSLT-------EKEvnhLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILR--DGQWIATQPLaGLTMDKiiA 228
|
250
....*....|...
gi 495091093 231 LIPERRMSRRFND 243
Cdd:PRK10982 229 MMVGRSLTQRFPD 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-210 |
9.43e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 21 VQILHKMKFHADANEFVSFVGPSGCGKSTLFNIIT----GLLKPDNGSILVDN---RETTGHTSPKIGYVLQKDLLFPWR 93
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpEEIKKHYRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 94 TVIDNVVL-------GLEIAGVSKRE-ARERAKALLQTY-----RMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILM 160
Cdd:TIGR00956 154 TVGETLDFaarcktpQNRPDGVSREEyAKHIADVYMATYglshtRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495091093 161 DESYKALDYplKIALE-SELLSIVKKERKTVVFIT--HDIEEAVTMSDRVYVM 210
Cdd:TIGR00956 234 DNATRGLDS--ATALEfIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVL 284
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-206 |
1.75e-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: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 34 NEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVdnrettghtspkigyvlqkdllfpwrtvidnvvlgleIAGvskrea 113
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------------------------------------IDG------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 114 rERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYP-----LKIALESELLSIVKKERK 188
Cdd:smart00382 39 -EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRLLLLLKSEKNL 117
|
170
....*....|....*...
gi 495091093 189 TVVFITHDIEEAVTMSDR 206
Cdd:smart00382 118 TVILTTNDEKDLGPALLR 135
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-199 |
6.75e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIlvdnrETTGHTSP-KIGYVLQKDLlfpwrTVIDNVVLG 102
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----DRNGEVSViAISAGLSGQL-----TGIENIEFK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 103 LEIAGVSKREARERAKALLQTYRMEGYEDKFPSQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSI 182
Cdd:PRK13546 110 MLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF 189
|
170
....*....|....*..
gi 495091093 183 vKKERKTVVFITHDIEE 199
Cdd:PRK13546 190 -KEQNKTIFFVSHNLGQ 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
137-217 |
6.87e-06 |
|
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: 46.74 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 137 ISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALeSELLSIVKKERKTVVFITHDIEEAVTMSDRVYVMkaHPGE 216
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI--GEGK 480
|
.
gi 495091093 217 I 217
Cdd:TIGR02633 481 L 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
107-224 |
8.78e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 107 GVSKR----EARERAKAllqtyrmEGYEDKF----PS------QISGGMRQRVALMRTMITDPQIILMDESYKALDYPLK 172
Cdd:NF040905 368 KVSRRgvidENEEIKVA-------EEYRKKMniktPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAK 440
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 173 IalesELLSIVKK---ERKTVVFITHDIEEAVTMSDRVYVMKAhpGEIINEIKID 224
Cdd:NF040905 441 Y----EIYTIINElaaEGKGVIVISSELPELLGMCDRIYVMNE--GRITGELPRE 489
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-168 |
1.41e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGaaGPVqILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILvdnrettghTSPKIgyvlqkdl 88
Cdd:PLN03073 513 DASFGYPG--GPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---------RSAKV-------- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 89 lfpwRTVIDNV--VLGLEIA------------GVSKREARerakALLQTYRMEGYEDKFPS-QISGGMRQRVALMRTMIT 153
Cdd:PLN03073 573 ----RMAVFSQhhVDGLDLSsnpllymmrcfpGVPEQKLR----AHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFK 644
|
170
....*....|....*
gi 495091093 154 DPQIILMDESYKALD 168
Cdd:PLN03073 645 KPHILLLDEPSNHLD 659
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-195 |
1.58e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 40 VGPSGCGKSTLF-----NIITGLlkPDNGSILVDNRETTGHTSPKIGYVL-------------------QKDLLFPWRTV 95
Cdd:PLN03073 209 VGRNGTGKTTFLrymamHAIDGI--PKNCQILHVEQEVVGDDTTALQCVLntdiertqlleeeaqlvaqQRELEFETETG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 96 ---------IDNVVLGLEIAGVSKR-------EARERAKALLQ----TYRMEGYEDKfpsQISGGMRQRVALMRTMITDP 155
Cdd:PLN03073 287 kgkgankdgVDKDAVSQRLEEIYKRlelidayTAEARAASILAglsfTPEMQVKATK---TFSGGWRMRIALARALFIEP 363
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495091093 156 QIILMDESYKALDYPLKIALESELLsivkKERKTVVFITH 195
Cdd:PLN03073 364 DLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSH 399
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
135-217 |
1.95e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 135 SQISGGMRQRVALMRTMITDPQIILMDESYKALD-------YPLKIALESELLSIvkkerktvVFITHDIEEAVTMSDRV 207
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakyeiYKLINQLVQQGVAI--------IVISSELPEVLGLSDRV 475
|
90
....*....|
gi 495091093 208 YVMkaHPGEI 217
Cdd:PRK13549 476 LVM--HEGKL 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-211 |
1.98e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 29 FHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTgHTSP------KIGYVLQ---KDLLFPWRTVIDNV 99
Cdd:PRK09700 284 FSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPldavkkGMAYITEsrrDNGFFPNFSIAQNM 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 100 VLG--LEIAGV--------SKREAR--ERAKALLQTyRMEGYEDKFpSQISGGMRQRVALMRTMITDPQIILMDESYKAL 167
Cdd:PRK09700 363 AISrsLKDGGYkgamglfhEVDEQRtaENQRELLAL-KCHSVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495091093 168 DyplkIALESELLSIVKK---ERKTVVFITHDIEEAVTMSDRVYVMK 211
Cdd:PRK09700 441 D----VGAKAEIYKVMRQladDGKVILMVSSELPEIITVCDRIAVFC 483
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-168 |
2.29e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 24 LHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSIlVDNRETtghtspkIGYVLQKDLLFPwRTVIDNVVLGl 103
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSS-VVIRGS-------VAYVPQVSWIFN-ATVRENILFG- 702
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495091093 104 eiagvSKREARERAKALLQTyRMEGYEDKFPSQ-----------ISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:PLN03232 703 -----SDFESERYWRAIDVT-ALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
132-210 |
4.70e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 132 KFPSQ------ISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELLSIVKKErKTVVFITHDIEEAVTMSD 205
Cdd:PRK10982 381 KTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKD-KGIIIISSEMPELLGITD 459
|
....*
gi 495091093 206 RVYVM 210
Cdd:PRK10982 460 RILVM 464
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
9-211 |
5.92e-05 |
|
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: 43.36 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 9 DISKFYEGAAGPVqiLHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETTG---HT-SPKIGYVL 84
Cdd:cd03288 24 DLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlplHTlRSRLSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 85 QKDLLF---------PWRTVIDNVVL-GLEIAgvskrEARERAKAL---LQTYRMEGYEDkfpsqISGGMRQRVALMRTM 151
Cdd:cd03288 102 QDPILFsgsirfnldPECKCTDDRLWeALEIA-----QLKNMVKSLpggLDAVVTEGGEN-----FSVGQRQLFCLARAF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495091093 152 ITDPQIILMDESYKALDyplkIALESELLSIVKK--ERKTVVFITHDIEEAVTmSDRVYVMK 211
Cdd:cd03288 172 VRKSSILIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVSTILD-ADLVLVLS 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-230 |
1.17e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNRETT--GHTSPK--IGYVLQKDLLFPwRTVIDN 98
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfGLMDLRkvLGIIPQAPVLFS-GTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 99 VVLGLEIAGVSKREARERAKaLLQTYR----------MEGYEDkfpsqISGGMRQRVALMRTMITDPQIILMDESYKALD 168
Cdd:PLN03130 1333 LDPFNEHNDADLWESLERAH-LKDVIRrnslgldaevSEAGEN-----FSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495091093 169 yplkIALESELLSIVKKERK--TVVFITHDIeEAVTMSDRVYVMKAhpGEIineikidLETDSP 230
Cdd:PLN03130 1407 ----VRTDALIQKTIREEFKscTMLIIAHRL-NTIIDCDRILVLDA--GRV-------VEFDTP 1456
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-217 |
3.15e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDNGSILVDNrettghtSPKIGYVLQKDLLFpWRTviDNVVLG 102
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK-------GIKLGYFAQHQLEF-LRA--DESPLQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 103 lEIAGVSKREARERAKALLQTYRMEGyeDKFP---SQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESEL 179
Cdd:PRK10636 397 -HLARLAPQELEQKLRDYLGGFGFQG--DKVTeetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
170 180 190
....*....|....*....|....*....|....*...
gi 495091093 180 LSIvkkeRKTVVFITHDIEEAVTMSDRVYVMkaHPGEI 217
Cdd:PRK10636 474 IDF----EGALVVVSHDRHLLRSTTDDLYLV--HDGKV 505
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
41-168 |
1.39e-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: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 41 GPSGCGKSTLFN---------IITGllkpdnGSILVDNRETTGHTSPKIGYVLQKDLLFPWRTVIDNVVLGLEI---AGV 108
Cdd:TIGR00956 796 GASGAGKTTLLNvlaervttgVITG------GDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqpKSV 869
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495091093 109 SKREARERAKALLQTYRMEGYEDKFPSQISGGM----RQRVALMRTMITDPQIIL-MDESYKALD 168
Cdd:TIGR00956 870 SKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-198 |
2.32e-03 |
|
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: 39.12 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 23 ILHKMKFHADANEFVSFVGPSGCGKSTLFNIITGLLKPDnGSILVD----NRETTGHTSPKIGYVLQKDLLFP--WRTVI 96
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDgvswNSVTLQTWRKAFGVIPQKVFIFSgtFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 97 DnvvlglEIAGVSKREARERAKALLQTYRMEGYEDKFPSQ-------ISGGMRQRVALMRTMITDPQIILMDESYKALDy 169
Cdd:TIGR01271 1313 D------PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLD- 1385
|
170 180 190
....*....|....*....|....*....|....*
gi 495091093 170 PLKialeselLSIVKKERK------TVVFITHDIE 198
Cdd:TIGR01271 1386 PVT-------LQIIRKTLKqsfsncTVILSEHRVE 1413
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
38-211 |
4.55e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.29 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 38 SFVGPSGCGKSTLFNIITGllKPDNGSILVDNR--------ETTGHTSpkiGYVLQKDLLFPWRTVIDNVV----LGLEI 105
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRisgfpkkqETFARIS---GYCEQNDIHSPQVTVRESLIysafLRLPK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495091093 106 AgVSKREARERAKALLQTYRMEGYEDK---FP--SQISGGMRQRVALMRTMITDPQIILMDESYKALDYPLKIALESELL 180
Cdd:PLN03140 985 E-VSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1063
|
170 180 190
....*....|....*....|....*....|....*
gi 495091093 181 SIVKKERkTVVFITH----DIEEAVtmsDRVYVMK 211
Cdd:PLN03140 1064 NTVDTGR-TVVCTIHqpsiDIFEAF---DELLLMK 1094
|
|
| |
