|
Name |
Accession |
Description |
Interval |
E-value |
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-232 |
3.20e-169 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 465.21 E-value: 3.20e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQEN 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 81 NLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK10771 81 NLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLGIKS 232
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGIKS 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-230 |
4.92e-146 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 406.45 E-value: 4.92e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQEN 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 81 NLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:COG3840 81 NLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA--SALLGI 230
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPalAAYLGI 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-212 |
6.02e-122 |
|
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: 344.86 E-value: 6.02e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 2 LKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENN 81
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 82 LFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:cd03298 81 LFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 162 PALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
2-214 |
1.26e-120 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 341.84 E-value: 1.26e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 2 LKLIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENN 81
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 82 LFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:TIGR01277 81 LFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 877977460 162 PALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKT 214
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-212 |
1.67e-87 |
|
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: 257.83 E-value: 1.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 2 LKLIDITWLYH--HLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQE 79
Cdd:cd03259 1 LELKGLSKTYGsvRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 80 NNLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 877977460 160 LDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
18-217 |
4.74e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 228.44 E-value: 4.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLN 97
Cdd:COG3842 24 VSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQDYALFPHLTVAENVAFGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 pGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:COG3842 104 -MRGVPKAEIRARvAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG3842 183 RELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-217 |
1.59e-67 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 211.47 E-value: 1.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGL- 96
Cdd:COG3839 22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQSYALYPHMTVYENIAFPLk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLtlNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:COG3839 102 LRKV--PKAEIDRRvREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 877977460 176 CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG3839 180 HRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-207 |
2.34e-67 |
|
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: 205.50 E-value: 2.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 2 LKLIDITWLYHH--LPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT----LTPPSRRPVSM 75
Cdd:cd03229 1 LELKNVSKRYGQktVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 76 LFQENNLFSHLNVQQNIGLGLnpgltlnasqrekrdaiarqmgieslmarlpgelSGGQRQRVALARCLVREQPVLLLDE 155
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 156 PFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
18-209 |
4.60e-67 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 207.63 E-value: 4.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhTLTPPSRRpVSMLFQENNLFSHLNVQQNIGLGLn 97
Cdd:COG1116 30 VSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK--PVTGPGPD-RGVVFQEPALLPWLTVLDNVALGL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:COG1116 106 ELRGVPKAERRERaRELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLW 185
|
170 180 190
....*....|....*....|....*....|....*
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVAD--GRIA 209
Cdd:COG1116 186 QETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
17-207 |
5.19e-64 |
|
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: 198.46 E-value: 5.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPSRRpVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:cd03293 22 DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP--VTGPGPD-RGYVFQQDALLPWLTVLDNVALGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:cd03293 99 ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIW 178
|
170 180 190
....*....|....*....|....*....|.
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRsIVVADGR 207
Cdd:cd03293 179 RETGKTVLLVTHDIDEAVFLADR-VVVLSAR 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
19-231 |
4.52e-63 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 199.99 E-value: 4.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLN 97
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRERRVGFVFQHYALFPHMTVAENIAFGLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICR 177
Cdd:COG1118 102 VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASA--LLGIK 231
Cdd:COG1118 182 ELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVarFLGCV 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-219 |
6.09e-61 |
|
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: 191.01 E-value: 6.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPG 99
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 LTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRER 179
Cdd:cd03299 100 KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEF 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 877977460 180 QLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:cd03299 180 GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
17-208 |
1.88e-60 |
|
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: 189.76 E-value: 1.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYALFPHLTVFENIAFGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:cd03300 98 RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQ 177
|
170 180 190
....*....|....*....|....*....|..
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03300 178 KELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-218 |
4.46e-59 |
|
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: 186.34 E-value: 4.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPV----SMLFQENNLFSHLNVQQNI 92
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDiTGLSEKELYELrrriGMLFQGGALFDSLTVFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGLTLnaSQREKRDAIA---RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:COG1127 104 AFPLREHTDL--SEAEIRELVLeklELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVID 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 877977460 170 TLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:COG1127 182 ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-219 |
6.88e-59 |
|
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: 186.40 E-value: 6.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPM--RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSR-RPVSML 76
Cdd:COG1120 1 MLEAENLSVGYGGRPVldDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlASLSRRELaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 77 FQENNLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQ----MGIESLMARLPGELSGGQRQRVALARCLVREQPVLL 152
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEalerTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 153 LDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-208 |
1.15e-58 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 184.86 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-----RRPVSMLFQENNLFSHLNVQQNI 92
Cdd:COG1136 28 SLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDiSSLSERElarlrRRHIGFVFQFFNLLPELTALENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGlTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:COG1136 108 ALPLLLA-GVSRKERRERaRELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 877977460 172 VSDICRERQLTLLMVSHSvEDAARIAPRSIVVADGRI 208
Cdd:COG1136 187 LRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-219 |
2.19e-58 |
|
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: 184.46 E-value: 2.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQ--ENNLFShLNVQQNIGL 94
Cdd:COG1122 21 SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelRRKVGLVFQnpDDQLFA-PTVEEDVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 GL-NPGLTlnASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG1122 100 GPeNLGLP--REEIRERvEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 877977460 173 SDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1122 178 KRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-208 |
3.31e-58 |
|
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: 183.46 E-value: 3.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDisklseKELAAFRRRHIGFVFQSFNLLPDLTALENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03255 104 ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELL 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 877977460 173 SDICRERQLTLLMVSHSvEDAARIAPRSIVVADGRI 208
Cdd:cd03255 184 RELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
19-217 |
1.55e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 182.95 E-value: 1.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQENNLFSHLNVQQNI- 92
Cdd:COG3638 23 SLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrlRRRIGMIFQQFNLVPRLSVLTNVl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 --GLGLNP---GLTLNASQREKRDAIA--RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:COG3638 103 agRLGRTStwrSLLGLFPPEDRERALEalERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 166 QEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG3638 183 RQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-229 |
4.20e-57 |
|
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: 184.92 E-value: 4.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKlIDITWLYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLTPPSRRPVS 74
Cdd:COG4148 2 MLE-VDFRLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsarGIFLPPHRRRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 75 MLFQENNLFSHLNVQQNIGLGLNPglTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLD 154
Cdd:COG4148 81 YVFQEARLFPHLSVRGNLLYGRKR--APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 155 EPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLG 229
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGG 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-217 |
1.40e-56 |
|
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: 180.01 E-value: 1.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTP----PSRRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:cd03261 20 DLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDiSGLSEaelyRLRRRMGMLFQSGALFDSLTVFENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLNPGLTLNASQREKRDAIARQM-GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03261 100 FPLREHTRLSEEEIREIVLEKLEAvGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:cd03261 180 RSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-220 |
3.03e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.10 E-value: 3.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLFQENNLFSHLNVQQNIGL--G 95
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQEPALYPDLTVRENLRFfaR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPgltLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:COG1131 100 LYG---LPRKEARERiDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 877977460 175 IcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSG 220
Cdd:COG1131 177 L-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-208 |
9.03e-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: 177.06 E-value: 9.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQNYALYPHMTVYDNIAFGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NpgltlnaSQREKRDAI-------ARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:cd03301 98 K-------LRKVPKDEIdervrevAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMR 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 877977460 170 TLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03301 171 AELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-194 |
2.55e-55 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 175.75 E-value: 2.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPM--RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAP---ASGTLLIAGEDHTLTPPSRRPVSM 75
Cdd:COG4136 1 MLSLENLTITLGGRPLlaPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 76 LFQENNLFSHLNVQQNIGLGLNPGLTlnasqREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVL 151
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPPTIG-----RAQRRARVEQAleeaGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 877977460 152 LLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAA 194
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
12-212 |
1.51e-54 |
|
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: 174.02 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 12 HHLPMRFTLaveRGEQVAILGPSGAGKSTLLNLIAGFLAPASG------TLLIAGEDHTLTPPSRRPVSMLFQENNLFSH 85
Cdd:cd03297 13 FTLKIDFDL---NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlngTVLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 86 LNVQQNIGLGLNpgLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 877977460 166 QEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-223 |
2.98e-54 |
|
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: 174.41 E-value: 2.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 2 LKLIDITWLYHHLPM---RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSML 76
Cdd:cd03295 1 IEFENVTKRYGGGKKavnNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 77 FQENNLFSHLNVQQNIGLGLnpglTLNASQREKRDAIARQ------MGIESLMARLPGELSGGQRQRVALARCLVREQPV 150
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVP----KLLKWPKEKIRERADEllalvgLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 151 LLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQAS 223
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-217 |
1.13e-52 |
|
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: 170.06 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlRRQIGMIFQQFNLIERLSVLENVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLNP------GLTLNASQREKRDAIA--RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03256 101 SGRLGrrstwrSLFGLFPKEEKQRALAalERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 166 QEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:cd03256 181 RQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-224 |
1.25e-52 |
|
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: 170.37 E-value: 1.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPMRFT------LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED--HTLTPPSRRP 72
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPvlkdvsLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 73 VSMLFQennlfshlnvqqNIGLGLNPGLTLNAS-----------QREKR-DAIARQMGI-ESLMARLPGELSGGQRQRVA 139
Cdd:COG1124 81 VQMVFQ------------DPYASLHPRHTVDRIlaeplrihglpDREERiAELLEQVGLpPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 140 LARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
....*
gi 877977460 220 GQASA 224
Cdd:COG1124 229 GPKHP 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-224 |
3.55e-52 |
|
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: 168.67 E-value: 3.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNpg 99
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFRHMTVFDNVAFGLR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 lTLNASQREKRDAIARQ-------MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:cd03296 101 -VKPRSERPPEAEIRAKvhellklVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA 224
Cdd:cd03296 180 RRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-207 |
6.23e-52 |
|
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: 167.26 E-value: 6.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQE-NNLFSHLNVQQNIGLG 95
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelRRKVGLVFQNpDDQFFGPTVEEEVAFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNpGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:cd03225 101 LE-NLGLPEEEIEERvEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK 179
|
170 180 190
....*....|....*....|....*....|...
gi 877977460 175 ICRERQlTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:cd03225 180 LKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-219 |
4.11e-51 |
|
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: 173.17 E-value: 4.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRP----VSMLFQ--ENNLFSHLNVQQN 91
Cdd:COG1123 285 SLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDlTKLSRRSLRElrrrVQMVFQdpYSSLNPRMTVGDI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IGLGLNPGLTLNASQREKR-DAIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:COG1123 365 IAEPLRLHGLLSRAERRERvAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 170 TLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1123 445 NLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-219 |
5.86e-51 |
|
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: 165.45 E-value: 5.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPMRFT------LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----- 69
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTalkdvsLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 70 RRPVSMLFQENNLFSHLNVQQNIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQP 149
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 150 VLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-219 |
1.77e-50 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 165.70 E-value: 1.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTP-------PSRRPVSMLFQ--ENNLFShLNVQ 89
Cdd:TIGR04521 25 SLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRD--ITAkkkkklkDLRKKVGLVFQfpEHQLFE-ETVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 QNIGLG-LNPGLTLNASQREKRDAIaRQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:TIGR04521 102 KDIAFGpKNLGLSEEEAEERVKEAL-ELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR04521 181 ILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-208 |
2.59e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.06 E-value: 2.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 2 LKLIDITWLYHHLPM--RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLF 77
Cdd:COG4619 1 LELEGLSFRVGGKPIlsPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlSAMPPPEwRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 78 QENNLFSHlNVQQNIGLGLNpgLTLNASQREKRDAIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEP 156
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQ--LRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 157 FSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-219 |
4.48e-50 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 163.24 E-value: 4.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPS------RRPVSMLFQENNLFSHLNVQQNI 92
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGED--LTDSKkdinklRRKVGMVFQQFNLFPHLTVLENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLnpgltLNASQREKRDAIAR------QMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:COG1126 99 TLAP-----IKVKKMSKAEAEERamelleRVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 877977460 167 EMLTLVSDICRERqLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1126 174 EVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
18-212 |
1.52e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 165.89 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLN 97
Cdd:PRK09452 33 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYALFPHMTVFENVAFGLR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGLTLNASQREK-RDAIaRQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:PRK09452 113 MQKTPAAEITPRvMEAL-RMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQ 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:PRK09452 192 RKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-225 |
2.74e-49 |
|
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: 161.56 E-value: 2.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPM--RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLF 77
Cdd:COG4555 1 MIEVENLSKKYGKVPAlkDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 78 QENNLFSHLNVQQNIGLgLNPGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEP 156
Cdd:COG4555 81 DERGLYDRLTVRENIRY-FAELYGLFDEELKKRiEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 157 FSALDPALRQEMLTLVSDiCRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASAS 225
Cdd:COG4555 160 TNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
30-219 |
2.84e-49 |
|
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: 164.20 E-value: 2.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 30 ILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPGLTLNASQREK 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 110 RDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHS 189
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190
....*....|....*....|....*....|
gi 877977460 190 VEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-218 |
9.62e-49 |
|
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: 160.89 E-value: 9.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT------LTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsrkeLRELRRKKISMVFQSFALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLN-PGLTLNASQREKRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:cd03294 124 AFGLEvQGVPRAEREERAAEALE-LVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-222 |
2.83e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 159.10 E-value: 2.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP------PSRRPVSMLFQennlfshLNVQQNI 92
Cdd:COG1121 26 SLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvPQRAEVDWDFP-------ITVRDVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGL----TLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:COG1121 99 LMGRYGRRglfrRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEAL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 169 LTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWqGKTDELLSGQA 222
Cdd:COG1121 179 YELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-217 |
1.06e-47 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 161.16 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNP 98
Cdd:PRK11607 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 GltlNASQREKRDAIARQMGI---ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:PRK11607 119 D---KLPKAEIASRVNEMLGLvhmQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 877977460 176 CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK11607 196 LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-208 |
2.06e-47 |
|
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: 155.77 E-value: 2.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGMVFQQFNLFPHLTVLENITLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LnpgltLNASQREKRDAIARQM------GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:cd03262 101 P-----IKVKGMSKAEAEERALellekvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVL 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 877977460 170 TLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03262 176 DVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-212 |
2.39e-47 |
|
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: 156.13 E-value: 2.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQenNLFSHLN----VQQ 90
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkirRKEIQMVFQ--DPMSSLNprmtIGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 91 NIGLGLNPGLTLNASQREKRDAIARQMGI---ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:cd03257 104 QIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03257 184 ILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-217 |
4.90e-47 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 159.42 E-value: 4.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPG 99
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLKLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 LTlNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRE 178
Cdd:PRK11000 104 GA-KKEEINQRvNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 877977460 179 RQLTLLMVSHSVEDAARIAPRsIVVAD-GRIAWQGKTDEL 217
Cdd:PRK11000 183 LGRTMIYVTHDQVEAMTLADK-IVVLDaGRVAQVGKPLEL 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-209 |
1.48e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 155.02 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTlTPPSRRPVsmLFQENNLFSHLNVQQNIGLGL 96
Cdd:COG4525 25 DVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-GPGADRGV--VFQKDALLPWLNVLDNVAFGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 npglTLNASQREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG4525 102 ----RLRGVPKAERRARAEELlalvGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVAD--GRIA 209
Cdd:COG4525 178 LDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-219 |
2.27e-46 |
|
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: 157.20 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 28 VAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE------DHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNpgLT 101
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMK--RA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 102 LNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQL 181
Cdd:TIGR02142 104 RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGI 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 877977460 182 TLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR02142 184 PILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-219 |
2.75e-46 |
|
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: 153.75 E-value: 2.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQIPRLFPELTVLENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGLTLNASQ----------REKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03219 100 AQARTGSGLLLararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEET 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 166 QEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:cd03219 180 EELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-216 |
1.75e-45 |
|
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: 152.12 E-value: 1.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 12 HHLPMRF---------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQE 79
Cdd:COG0411 8 RGLTKRFgglvavddvSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgIARTFQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 80 NNLFSHLNVQQNIGLG---------LNPGLTLNASQREKRDAIAR------QMGIESLMARLPGELSGGQRQRVALARCL 144
Cdd:COG0411 88 PRLFPELTVLENVLVAaharlgrglLAALLRLPRARREEREARERaeelleRVGLADRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 145 VREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-219 |
3.18e-45 |
|
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: 150.28 E-value: 3.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYVPEGRRIFPELTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGltlnaSQREKRDAIARQMGI----ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:cd03224 100 AYAR-----RRAKRKARLERVYELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 877977460 172 VSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:cd03224 175 IREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-227 |
3.62e-45 |
|
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: 157.37 E-value: 3.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPA---SGTLLIAGEDHTLTPPSRRP--VSMLFQE-NNLFSHLNVQQNI 92
Cdd:COG1123 26 SLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrrIGMVFQDpMTQLNPVTVGDQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG1123 106 AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASAL 227
Cdd:COG1123 186 RELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-219 |
3.83e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 151.01 E-value: 3.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPS------RRPVSMLFQENNLFSHLNVQQNI 92
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK--VNDPKvderliRQEAGMVFQQFYLFPHLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGlnPGLTLNASQREKRD---AIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK09493 99 MFG--PLRVRGASKEEAEKqarELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 170 TLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK09493 177 KVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-208 |
3.92e-45 |
|
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: 148.70 E-value: 3.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLFQENNLFSHLNVQQNIglgln 97
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPEEPSLYENLTVRENL----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 pgltlnasqrekrdaiarqmgieslmarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcR 177
Cdd:cd03230 95 -------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL-K 142
|
170 180 190
....*....|....*....|....*....|.
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03230 143 KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-158 |
7.47e-45 |
|
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: 147.02 E-value: 7.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLT--PPSRRPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRKEIGYVFQDPQLFPRLTVRENLRLGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 97 NPGLTLNASQREKRDAIARQMGIESLMARL----PGELSGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:pfam00005 85 LLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-217 |
1.80e-44 |
|
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: 148.48 E-value: 1.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFL-----APASGTLLIAGED--HTLTPPS--RRPVSMLFQENNLFsHLNVQ 89
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiyDLDVDVLelRRRVGMVFQKPNPF-PGSIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 QNIGLGLNPGLTLNASQREKRDAIA-RQMGI-ESLMARL-PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:cd03260 99 DNVAYGLRLHGIKLKEELDERVEEAlRKAALwDEVKDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 167 EMLTLVSDICRErqLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:cd03260 179 KIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-212 |
5.10e-44 |
|
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: 146.04 E-value: 5.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedhtltppsrRPVSmlfqennlfshlnvqqniglglnp 98
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG----------KDLA------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 glTLNASQREKRDAIARQ----MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:cd03214 65 --SLSPKELARKIAYVPQalelLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRR 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 877977460 175 ICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03214 143 LARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
19-221 |
5.86e-44 |
|
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: 154.92 E-value: 5.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFsHLNVQQNIGLGl 96
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlSDLDPASwRRQIAWVPQNPYLF-AGTIRENLRLG- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPgltlNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:COG4988 435 RP----DASDEELEAA-LEAAGLDEFVAALPdgldtplGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 166 QEMLTLVSDICRERqlTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:COG4988 510 AEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-228 |
1.47e-43 |
|
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: 154.15 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFSHlNVQQNIGLG 95
Cdd:COG4987 354 LSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlRDLDEDDlRRRIAVVPQRPHLFDT-TLRENLRLA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 lNPgltlNASQREKRDAIaRQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG4987 433 -RP----DATDEELWAAL-ERVGLGDWLAALPdgldtwlGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAAT 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 165 RQEMLTLVSDICRERqlTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:COG4987 507 EQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-219 |
5.63e-43 |
|
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: 153.84 E-value: 5.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFSHlNVQQNIGLG 95
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlRQIDPASlRRQIGVVLQDVFLFSG-TIRENITLG 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 lNPGLTLnasqrEKRDAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG2274 573 -DPDATD-----EEIIEAARLAGLHDFIEALPmgydtvvGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 165 RQEMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:COG2274 647 EAIILENLRRLLKGR--TVIIIAHrlsTIRLADRI----IVLDKGRIVEDGTHEELLA 698
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-216 |
8.03e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 146.35 E-value: 8.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRPVSMLFQ--ENNLFSHlNVQQNI 92
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdiRKKVGLVFQypEYQLFEE-TIEKDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGL-NPGLtlnaSQREKRDAIARQMGI-----ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:PRK13637 106 AFGPiNLGL----SEEEIENRVKRAMNIvgldyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 167 EMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-218 |
3.03e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 150.70 E-value: 3.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFsHLNVQQNIGLG 95
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDiRDLTLESlRRQIGVVPQDTFLF-SGTIRENIRYG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 lNPgltlNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDP-- 162
Cdd:COG1132 438 -RP----DATDEEVEEA-AKAAQAHEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTet 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 163 --ALRQEMLTLVsdicreRQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:COG1132 512 eaLIQEALERLM------KGRTTIVIAHrlsTIRNADRI----LVLDDGRIVEQGTHEELL 562
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-223 |
5.77e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 145.61 E-value: 5.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNp 98
Cdd:PRK10851 22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGLT- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 glTLNASQREKRDAIARQ-------MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10851 101 --VLPRRERPNAAAIKAKvtqllemVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRW 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQAS 223
Cdd:PRK10851 179 LRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-230 |
6.73e-42 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 142.43 E-value: 6.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGYVPEGRRIFPSLTVEENLLLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 lnpgltlnASQREKRDAIARQMgiESLMARLP----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:COG0410 103 --------AYARRDRAEVRADL--ERVYELFPrlkerrrqraGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 166 QEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLGI 230
Cdd:COG0410 173 EEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-219 |
9.10e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 143.62 E-value: 9.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIagEDHTLTP--------PSRRPVSMLFQ--ENNLFSHlNVQ 89
Cdd:PRK13634 28 VSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI--GERVITAgkknkklkPLRKKVGIVFQfpEHQLFEE-TVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 QNIGLG-LNPGLTlnasqREKRDAIARQM----GI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK13634 105 KDICFGpMNFGVS-----EEDAKQKAREMielvGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-208 |
9.14e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.34 E-value: 9.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLT----PPSRRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:COG2884 22 SLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlSRLKrreiPYLRRRIGVVFQDFRLLPDRTVYENVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLnpgLTLNASQREKRDAIA---RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:COG2884 102 LPL---RVTGKSRKEIRRRVRevlDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIME 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 877977460 171 LVSDICReRQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:COG2884 179 LLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-218 |
2.29e-41 |
|
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: 140.76 E-value: 2.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYLPQEASIFRKLTVEENILAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:cd03218 100 LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 877977460 176 cRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:cd03218 180 -KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
18-207 |
4.15e-41 |
|
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: 137.76 E-value: 4.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQennlfshlnvqqniglg 95
Cdd:cd00267 18 VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelRRRIGYVPQ----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 lnpgltlnasqrekrdaiarqmgieslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:cd00267 81 ----------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL 126
|
170 180 190
....*....|....*....|....*....|..
gi 877977460 176 CrERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:cd00267 127 A-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-217 |
1.55e-40 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 141.78 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPg 99
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKM- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 LTLNASQREKRDAIARQM----GIESlmaRLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:PRK11432 106 LGVPKEERKQRVKEALELvdlaGFED---RYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIREL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 877977460 176 CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK11432 183 QQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-210 |
2.10e-40 |
|
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: 137.66 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP------PSRRPVSMLFQennlfshLNVQQNI 92
Cdd:cd03235 19 SFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQRRSIDRDFP-------ISVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNP--GLTLNASQREKRDAIA--RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:cd03235 92 LMGLYGhkGLFRRLSKADKAKVDEalERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 877977460 169 LTLVSDICRERqLTLLMVSHSVEDAARIAPRSIVVADGRIAW 210
Cdd:cd03235 172 YELLRELRREG-MTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-215 |
2.63e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 138.61 E-value: 2.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTL---LNLIAGflaPASGTLLIAGEDHTL-TPPS-------RRPVSMLFQENNLFSHLN 87
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLlrvLNLLEM---PRSGTLNIAGNHFDFsKTPSdkairelRRNVGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 88 VQQNI------GLGLNpgltlnasqreKRDAIARQMGI------ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDE 155
Cdd:PRK11124 99 VQQNLieapcrVLGLS-----------KDQALARAEKLlerlrlKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 156 PFSALDPalrqEMLTLVSDICRERQ---LTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTD 215
Cdd:PRK11124 168 PTAALDP----EITAQIVSIIRELAetgITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-217 |
3.67e-40 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 138.20 E-value: 3.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP-----PSRRPVSMLFQENNLFSHLNVQQNI-- 92
Cdd:TIGR02315 23 LNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrKLRRRIGMIFQHYNLIERLTVLENVlh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 -GLGLNPGL-----TLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:TIGR02315 103 gRLGYKPTWrsllgRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 167 EMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:TIGR02315 183 QVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-207 |
5.05e-40 |
|
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: 135.59 E-value: 5.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFShLNVQQNIglg 95
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAYVPQDPFLFS-GTIRENI--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 lnpgltlnasqrekrdaiarqmgieslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:cd03228 97 ----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL 142
|
170 180 190
....*....|....*....|....*....|....*
gi 877977460 176 CRERqlTLLMVSH---SVEDAARIaprsIVVADGR 207
Cdd:cd03228 143 AKGK--TVIVIAHrlsTIRDADRI----IVLDDGR 171
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-219 |
9.70e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 137.21 E-value: 9.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRpvSMLFQENNL-FShLNVQQNIG 93
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarRR--AVLPQHSSLsFP-FTVEEVVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLNPgltLNASQREKRDAIARQM---GIESLMARLPGELSGGQRQRVALARCLVR------EQPVLLLDEPFSALDPAL 164
Cdd:PRK13548 99 MGRAP---HGLSRAEDDALVAAALaqvDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAH 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 165 RQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGK-----TDELLS 219
Cdd:PRK13548 176 QHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTpaevlTPETLR 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-219 |
9.84e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.84 E-value: 9.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhTLTPPS----RRPVSMLFQE-NNLFSHLNVQQNIG 93
Cdd:PRK13635 27 SFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM--VLSEETvwdvRRQVGMVFQNpDNQFVGATVQDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGL-NPGLTLNASQREKRDAIaRQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK13635 105 FGLeNIGVPREEMVERVDQAL-RQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13635 184 RQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-217 |
1.69e-39 |
|
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: 135.71 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGL- 94
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSiRTDRKAARQSLGYCPQFDALFDELTVREHLRFy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 ----GLNpgltlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:cd03263 100 arlkGLP-----KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 877977460 171 LVSDICRERqlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:cd03263 175 LILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-219 |
2.77e-39 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 138.29 E-value: 2.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS----RRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDlTALSERElraaRRKIGMIFQHFNLLSSRTVAENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LglnPgLTLNASQREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:COG1135 105 L---P-LEIAGVPKAEIRKRVAELlelvGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSIL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 170 TLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1135 181 DLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-207 |
4.47e-39 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 134.30 E-value: 4.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HTLTPPSRRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:TIGR02673 22 SLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDvnrlrGRQLPLLRRRIGVVFQDFRLLPDRTVYENVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLN-PGLTLNASQREKRdAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:TIGR02673 102 LPLEvRGKKEREIQRRVG-AALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLL 180
|
170 180 190
....*....|....*....|....*....|....*
gi 877977460 173 SDICReRQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:TIGR02673 181 KRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-212 |
4.99e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 135.14 E-value: 4.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 2 LKLIDITWLYHHLPMRF--TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLT-PPS-------RR 71
Cdd:COG4161 3 IQLKNINCFYGSHQALFdiNLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSqKPSekairllRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 72 PVSMLFQENNLFSHLNVQQNIG------LGLNpgltlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLV 145
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIeapckvLGLS-----KEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 146 REQPVLLLDEPFSALDPALRQEmltlVSDICRERQ---LTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQ----VVEIIRELSqtgITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-208 |
5.41e-39 |
|
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: 134.07 E-value: 5.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HTLTPPSRRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrGRAIPYLRRKIGVVFQDFRLLPDRNVYENVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVS 173
Cdd:cd03292 101 FALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLK 180
|
170 180 190
....*....|....*....|....*....|....*
gi 877977460 174 DIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03292 181 KI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-219 |
6.49e-39 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 138.31 E-value: 6.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS------RRPVSMLFQENNLFSHLNVQQNI 92
Cdd:COG4175 47 SFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKelrelrRKKMSMVFQHFALLPHRTVLENV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLN----PgltlnasqREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG4175 127 AFGLEiqgvP--------KAERRERAREAlelvGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLI 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 165 RQEM----LTLVsdicRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4175 199 RREMqdelLELQ----AKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILT 253
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-219 |
6.86e-39 |
|
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: 135.64 E-value: 6.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhTLTPPS----RRPVSMLFQ--ENNLFSHLnVQQNIG 93
Cdd:TIGR04520 23 LSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENlweiRKKVGMVFQnpDNQFVGAT-VEDDVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGL-NPGLtlNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR04520 101 FGLeNLGV--PREEMRKRvDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLET 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR04520 179 IRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-218 |
7.16e-39 |
|
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: 134.83 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASG-TLLIAGEDHTLTPPSR-RP----VSMLFQENnLFSHLNVQQ-- 90
Cdd:COG1119 23 SWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElRKriglVSPALQLR-FPRDETVLDvv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 91 ------NIGLGLNPGltlnASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG1119 102 lsgffdSIGLYREPT----DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 165 RQEMLTLVSDICRERQLTLLMVSHSVEDaarIAP---RSIVVADGRIAWQGKTDELL 218
Cdd:COG1119 178 RELLLALLDKLAAEGAPTLVLVTHHVEE---IPPgitHVLLLKDGRVVAAGPKEEVL 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-219 |
1.42e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.47 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPP----SRRPVsmLFQENNLFSHLNVQQNIGLG 95
Cdd:COG4559 22 LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPwelaRRRAV--LPQHSSLAFPFTVEEVVALG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGltlnASQREKRDAIARQ----MGIESLMARLPGELSGGQRQRVALARCL------VREQP-VLLLDEPFSALDPAL 164
Cdd:COG4559 100 RAPH----GSSAAQDRQIVREalalVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPrWLFLDEPTSALDLAH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 165 RQEMLTLVSDICReRQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4559 176 QHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-206 |
1.65e-38 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 134.06 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTlTPPSRRPVsmLFQENNLFSHLNVQQNIGLGLNpg 99
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAERGV--VFQNEGLLPWRNVQDNVAFGLQ-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 ltLNASQREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:PRK11248 97 --LAGVEKMQRLEIAHQMlkkvGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
170 180 190
....*....|....*....|....*....|.
gi 877977460 176 CRERQLTLLMVSHSVEDAARIAPRSIVVADG 206
Cdd:PRK11248 175 WQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-206 |
2.34e-38 |
|
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: 132.97 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVsmlFQENNLFSHLNVQQNIGLGLNPG 99
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVV---FQNYSLLPWLTVRENIALAVDRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 L-TLNASQREK--RDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:TIGR01184 83 LpDLSKSERRAivEEHIA-LVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIW 161
|
170 180 190
....*....|....*....|....*....|
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADG 206
Cdd:TIGR01184 162 EEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-219 |
4.81e-38 |
|
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: 132.35 E-value: 4.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 6 DITWLYHhlPMRFTL-----AVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQ 78
Cdd:cd03253 5 NVTFAYD--PGRPVLkdvsfTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDiREVTLDSlRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 79 ENNLFsHLNVQQNIGLGlnpglTLNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVRE 147
Cdd:cd03253 83 DTVLF-NDTIGYNIRYG-----RPDATDEEVIEA-AKAAQIHDKIMRFPdgydtivGErglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 148 QPVLLLDEPFSALDPALRQEMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHrlsTIVNADKI----IVLKDGRIVERGTHEELLA 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-208 |
7.82e-38 |
|
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: 131.79 E-value: 7.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPS--------RRPVSMLFQENNLFSHLNVQQ 90
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--LFALDedararlrARHVGFVFQSFQLLPTLTALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 91 NIGLglnPgLTLnasqREKRDAIAR------QMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG4181 110 NVML---P-LEL----AGRRDARARaralleRVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 877977460 165 RQEMLTLVSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRI 208
Cdd:COG4181 182 GEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
18-195 |
8.41e-38 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 130.81 E-value: 8.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhTLTPPSRRPVSM-------LFQENNLFSHLNVQQ 90
Cdd:TIGR03608 17 LNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQE-TPPLNSKKASKFrreklgyLFQNFALIENETVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 91 NIGLGLnpgLTLNASQREKRDAIAR---QMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:TIGR03608 96 NLDLGL---KYKKLSKKEKREKKKEaleKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDE 172
|
170 180
....*....|....*....|....*...
gi 877977460 168 MLTLVSDICRERQlTLLMVSHSVEDAAR 195
Cdd:TIGR03608 173 VLDLLLELNDEGK-TIIIVTHDPEVAKQ 199
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-208 |
1.90e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 133.82 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGL-N 97
Cdd:PRK11650 24 DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQNYALYPHMSVRENMAYGLkI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGLTlnASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:PRK11650 104 RGMP--KAEIEERvAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLH 181
|
170 180 190
....*....|....*....|....*....|..
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:PRK11650 182 RRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-223 |
1.34e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 132.85 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAG------EDHTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakiSDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQAS 223
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-208 |
2.39e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 128.66 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP--VSMLFQENNL--FSHLNVQQNIG 93
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAkyIGRVFQDPMMgtAPSMTIEENLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 L--------GLNPGltLNASQREK-RDAIAR-QMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:COG1101 105 LayrrgkrrGLRRG--LTKKRRELfRELLATlGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:COG1101 183 TAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-207 |
2.88e-36 |
|
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: 126.82 E-value: 2.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDIT------WLYHHLpmrfTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPV 73
Cdd:COG4133 2 MLEAENLScrrgerLLFSGL----SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPiRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 74 SMLFQENNLFSHLNVQQNIGL--GLNPgltLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVL 151
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFwaALYG---LRADREAIDEALEA-VGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 152 LLDEPFSALDPALRQEMLTLVSDiCRERQLTLLMVSHSVEDAAriAPRSIVVADGR 207
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-222 |
3.87e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 130.38 E-value: 3.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 29 AILGPSGAGKSTLLNLIAGFLAPASGtlLIAGEDHTLT--------PPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPgl 100
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKG--RIVLNGRVLFdaekgiclPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAK-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 101 tlnaSQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQ 180
Cdd:PRK11144 104 ----SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 877977460 181 LTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQA 222
Cdd:PRK11144 180 IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
19-218 |
7.08e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 127.12 E-value: 7.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSR--RPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:COG4604 21 SLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQENHINSRLTVRELVAFGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NP---GlTLNASQREK-RDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG4604 101 FPyskG-RLTAEDREIiDEAIAY-LDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:COG4604 179 RRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-219 |
8.02e-36 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 129.54 E-value: 8.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPMRFT------LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----- 69
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHalnnvsLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 70 RRPVSMLFQENNLFSHLNVQQNIGLglnPgLTLNASQREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLV 145
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL---P-LELAGTPKAEIKARVTELlelvGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 146 REQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-219 |
2.03e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 125.53 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRArlgIGYLPQEASIFRKLTVEDNILAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPgLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDP-AlrqemltlVSD 174
Cdd:COG1137 104 EL-RKLSKKEREERlEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPiA--------VAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 175 I------CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG1137 175 IqkiirhLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-219 |
3.18e-35 |
|
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: 124.96 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFShLNVQQNIGLG 95
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDiRDLNLRWlRSQIGLVSQEPVLFD-GTIAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGltlnasQREKRDAIARQMGIESLMARLP-----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALD--- 161
Cdd:cd03249 101 KPDA------TDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDaes 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 162 PALRQEMLtlvSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:cd03249 175 EKLVQEAL---DRAMKGR--TTIVIAHrlsTIRNADLI----AVLQNGQVVEQGTHDELMA 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-219 |
5.40e-35 |
|
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: 130.19 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTL----LNLIagflaPASGTLLIAGED-HTLTP----PSRRPVSMLFQenNLFSHLN-- 87
Cdd:COG4172 306 SLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDlDGLSRralrPLRRRMQVVFQ--DPFGSLSpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 88 --VQQNIGLGL---NPGLTlnASQREKR-DAIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:COG4172 379 mtVGQIIAEGLrvhGPGLS--AAERRARvAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSH--SVEDAarIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4172 457 DVSVQAQILDLLRDLQREHGLAYLFISHdlAVVRA--LAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-219 |
6.77e-35 |
|
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: 124.27 E-value: 6.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFSHlNVQQNIGLG 95
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvRDYTLASlRRQIGLVSQDVFLFND-TVAENIAYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 lnpglTLNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDpaL 164
Cdd:cd03251 100 -----RPGATREEVEEA-ARAANAHEFIMELPegydtviGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALD--T 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 165 RQEMltLVSDICRE--RQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:cd03251 172 ESER--LVQAALERlmKNRTTFVIAHrlsTIENADRI----VVLEDGKIVERGTHEELLA 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-208 |
8.04e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 124.79 E-value: 8.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLiAGEdhtlTPPS--RRPVSMLFQENNLFSHLNVQQNIGLGLN 97
Cdd:PRK11247 33 LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGT----APLAeaREDTRLMFQDARLLPWKKVIDNVGLGLK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGLTLNAsqrekRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICR 177
Cdd:PRK11247 108 GQWRDAA-----LQALA-AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQ 181
|
170 180 190
....*....|....*....|....*....|.
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:PRK11247 182 QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
20-224 |
8.09e-35 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 124.53 E-value: 8.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIaGFL-APASGTLLIAGE--------DHTLTPPSRRPV-------SMLFQENNLF 83
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCI-NLLeTPDSGEIRVGGEeirlkpdrDGELVPADRRQLqrirtrlGMVFQSFNLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 84 SHLNVQQNIGLGlnPgltLNASQREKRDAIARQM------GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPF 157
Cdd:COG4598 108 SHMTVLENVIEA--P---VHVLGRPKAEAIERAEallakvGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 158 SALDPALRQEMLTLVSDICRE-RqlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA 224
Cdd:COG4598 183 SALDPELVGEVLKVMRDLAEEgR--TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSE 248
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-219 |
9.89e-35 |
|
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: 123.75 E-value: 9.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIGLGl 96
Cdd:cd03252 22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLFNR-SIRDNIALA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTlnasqREKRDAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03252 100 DPGMS-----MERVIEAAKLAGAHDFISELPegydtivGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 166 QEMLTLVSDICRERqlTLLMVSHSVEdAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:cd03252 175 HAIMRNMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-219 |
1.02e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.09 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIA----------GEDHTLTPPSRRPVSMLFQENNLFSHLNVQ 89
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslSQQKGLIRQLRQHVGFVFQNFNLFPHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 QNIGLGlnpGLTLNASQREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:PRK11264 104 ENIIEG---PVIVKGEPKEEATARARELlakvGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 166 QEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK11264 181 GEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-217 |
5.44e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.06 E-value: 5.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqAAGIAIIHQELNLVPNLSVAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNP--GLTLN-ASQREKRDAIARQMGIE-SLMARLpGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:COG1129 104 REPrrGGLIDwRAMRRRARELLARLGLDiDPDTPV-GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 877977460 172 VSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG1129 183 IRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-224 |
1.41e-33 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 127.29 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFsHLNVQQNIGLGl 96
Cdd:TIGR03375 485 SLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDNIALG- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTLNASQRekrdaIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:TIGR03375 563 APYADDEEILR-----AAELAGVTEFVRRHPdgldmqiGErgrsLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 166 QEMLTLVSDICRERqlTLLMVSH--SVEDaarIAPRSIVVADGRIAWQGKTDELLSGQASA 224
Cdd:TIGR03375 638 ERFKDRLKRWLAGK--TLVLVTHrtSLLD---LVDRIIVMDNGRIVADGPKDQVLEALRKG 693
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-212 |
6.12e-33 |
|
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: 118.85 E-value: 6.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIGLGL 96
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLFYG-TLRDNITLGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 npgltLNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03245 103 -----PLADDERILRA-AELAGVTDFVNKHPngldlqiGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 877977460 166 QEMLTLVSDICRERqlTLLMVSHSVEdAARIAPRSIVVADGRIAWQG 212
Cdd:cd03245 177 ERLKERLRQLLGDK--TLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-219 |
7.55e-33 |
|
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: 120.93 E-value: 7.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAP---ASGTLLIAGED-HTLTPPSRRP-----VSMLFQENnlFSHLN-- 87
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDlLKLSEKELRKirgreIQMIFQDP--MTSLNpv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 88 --VQQNIGLGLNPGLTLNASQREKRdAIA--RQMGI---ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:COG0444 103 mtVGDQIAEPLRIHGGLSKAEARER-AIEllERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTAL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRsIVV--AdGRIAWQGKTDELLS 219
Cdd:COG0444 182 DVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADR-VAVmyA-GRIVEEGPVEELFE 240
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-217 |
1.68e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 119.10 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HTLTPPSRRPVSMLFQENNLFSHLNVQQNIG 93
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamsRSRLYTVRKRMSMLFQSGALFTDMNVFDNVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLN-----PGLTLNASQREKRDAIARQmGIESLMarlPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:PRK11831 107 YPLRehtqlPAPLLHSTVMMKLEAVGLR-GAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 877977460 169 LTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-212 |
2.87e-32 |
|
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: 115.87 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFShLNVQQNIGLgl 96
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvSDLEKALSSLISVLNQRPYLFD-TTLRNNLGR-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 npgltlnasqrekrdaiarqmgieslmarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:cd03247 98 --------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 877977460 177 RERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQG 212
Cdd:cd03247 146 KDK--TLIWITHhltGIEHMDKI----LFLENGKIIMQG 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
3.03e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.17 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYhhlPMRFTLA-------VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE---DHTLTPpSR 70
Cdd:PRK13632 7 MIKVENVSFSY---PNSENNAlknvsfeINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItisKENLKE-IR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 71 RPVSMLFQE-NNLFSHLNVQQNIGLGL-NPGLTlnasqREKRDAI----ARQMGIESLMARLPGELSGGQRQRVALARCL 144
Cdd:PRK13632 83 KKIGIIFQNpDNQFIGATVEDDIAFGLeNKKVP-----PKKMKDIiddlAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 145 VREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAArIAPRSIVVADGRIAWQGKTDELL 218
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
29-212 |
7.71e-32 |
|
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: 115.75 E-value: 7.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 29 AILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLFQENNLFSHLNVQQNIG-LGLNPGLtlNASQ 106
Cdd:cd03264 29 GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGYLPQEFGVYPNFTVREFLDyIAWLKGI--PSKE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 107 REKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERqlTLLM 185
Cdd:cd03264 107 VKARvDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVIL 184
|
170 180
....*....|....*....|....*..
gi 877977460 186 VSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03264 185 STHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-211 |
9.63e-32 |
|
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: 113.68 E-value: 9.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRrpvsmlfqennlfshlnvqqniglglnp 98
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD---------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 gltlnasqrekrdaiARQMGIESLMarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcRE 178
Cdd:cd03216 72 ---------------ARRAGIAMVY-----QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL-RA 130
|
170 180 190
....*....|....*....|....*....|...
gi 877977460 179 RQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQ 211
Cdd:cd03216 131 QGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-218 |
1.06e-31 |
|
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: 115.79 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFSHlNVQQNIGLG 95
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDiRDISRKSlRSMIGVVLQDTFLFSG-TIMENIRLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 lnpgltLNASQREKRDAIARQMGIESLMARLP-----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDP-- 162
Cdd:cd03254 101 ------RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTet 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 163 -ALRQEMLTLVSDicrerQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:cd03254 175 eKLIQEALEKLMK-----GRTSIIIAHrlsTIKNADKI----LVLDDGKIIEEGTHDELL 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-219 |
1.15e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 118.14 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQenNLFSHLNVQQNI 92
Cdd:PRK11308 36 FTL--ERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQ--NPYGSLNPRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGLTLN-----ASQREKRDAIARQMGIESLMA-RLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:PRK11308 112 GQILEEPLLINtslsaAERREKALAMMAKVGLRPEHYdRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 877977460 167 EMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK11308 192 QVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-199 |
1.19e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 114.64 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQennlfshLNVQQNIGLGL-- 96
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLP-------LTVRDLVAMGRwa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 --NPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:NF040873 85 rrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAE 164
|
170 180
....*....|....*....|....*
gi 877977460 175 IcRERQLTLLMVSHSVEDAARIAPR 199
Cdd:NF040873 165 E-HARGATVVVVTHDLELVRRADPC 188
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
19-221 |
1.43e-31 |
|
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: 121.77 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIGLGl 96
Cdd:TIGR01846 477 NLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRDNIALC- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTLnasqrEKRDAIARQMGIESLMARLP-----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:TIGR01846 555 NPGAPF-----EHVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESE 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 166 QEMLTLVSDICRERqlTLLMVSHSVeDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:TIGR01846 630 ALIMRNMREICRGR--TVIIIAHRL-STVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-219 |
1.67e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 119.18 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTL--TPPSRRpVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:PRK09536 24 LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvEALsaRAASRR-VASVPQDTSLSFEFDVRQVVEMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTLNASQREKRDAIARQ----MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK09536 103 TPHRSRFDTWTETDRAAVERamerTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 877977460 173 SDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK09536 183 RRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-221 |
2.09e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 116.47 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 22 VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS------RRPVSMLFQ--ENNLFSHlNVQQNIG 93
Cdd:PRK13641 30 LEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkklRKKVSLVFQfpEAQLFEN-TVLKDVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LG-LNPGLTlnaSQREKRDAIA--RQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK13641 109 FGpKNFGFS---EDEAKEKALKwlKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 170 TLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK13641 186 QLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-224 |
2.35e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.84 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS---------------RRPVSMLFQENNLF 83
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrllRTRLTMVFQHFNLW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 84 SHLNVQQNIGLGlnPGLTLNASQREKRDAIAR---QMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:PRK10619 105 SHMTVLENVMEA--PIQVLGLSKQEARERAVKylaKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 160 LDPALRQEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA 224
Cdd:PRK10619 183 LDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-203 |
2.99e-31 |
|
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: 120.08 E-value: 2.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIGLG 95
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAG-TIAENIRLA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LnPGLTLNASQREKRDAIARQM------GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:TIGR02857 420 R-PDASDAEIREALERAGLDEFvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
170 180 190
....*....|....*....|....*....|....
gi 877977460 170 TLVSDICRERqlTLLMVSHSVEDAARiAPRSIVV 203
Cdd:TIGR02857 499 EALRALAQGR--TVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-212 |
3.23e-31 |
|
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: 114.39 E-value: 3.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhTLTPP--SRRPVSMLFQENNLFSHLNVQQNIGL-- 94
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPaeARRRLGFVSDSTGLYDRLTARENLEYfa 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 ---GLNPgltlnASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:cd03266 104 glyGLKG-----DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 877977460 172 VSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03266 179 IRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-193 |
3.67e-31 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 113.29 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE--DHT---LTPpSRRPVSMLFQ--ENNLFSHlNVQQNI 92
Cdd:TIGR01166 13 FAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSrkgLLE-RRQRVGLVFQdpDDQLFAA-DVDQDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLG-LNPGLTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR01166 91 AFGpLNLGLSEAEVERRVREALTA-VGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAI 169
|
170 180
....*....|....*....|..
gi 877977460 172 VSDIcRERQLTLLMVSHSVEDA 193
Cdd:TIGR01166 170 LRRL-RAEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-219 |
4.19e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 115.67 E-value: 4.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 23 ERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLT--PPSRRPVSMLFQ--ENNLFSHlNVQQNIGLG-LN 97
Cdd:PRK13652 28 PRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEniREVRKFVGLVFQnpDDQIFSP-TVEQDIAFGpIN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGLTlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICR 177
Cdd:PRK13652 107 LGLD-EETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13652 186 TYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-219 |
5.63e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 115.33 E-value: 5.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRPVSMLFQ--ENNLFShLNVQQNIG 93
Cdd:PRK13636 27 INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESVGMVFQdpDNQLFS-ASVYQDVS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LG-LNPGLTLNASQREKRDAIARQmGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK13636 106 FGaVNLKLPEDEVRKRVDNALKRT-GIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13636 185 VEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-217 |
1.18e-30 |
|
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: 112.85 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLFQENNLFSHLNVQQNIGL-GL 96
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDLSVDDELTGWENLYIhAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIC 176
Cdd:cd03265 100 LYGVP-GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 877977460 177 RERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:cd03265 179 EEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-219 |
1.30e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.02 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRPVSMLFQ--ENNLFSHlNVQQNIG 93
Cdd:PRK13639 23 FKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevRKTVGIVFQnpDDQLFAP-TVEEDVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LG-LNPGLTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK13639 102 FGpLNLGLSKEEVEKRVKEALKA-VGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 877977460 173 SDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13639 181 YDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-217 |
1.38e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 115.21 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRP----VSMLFQenNLFSHLNVQQNIG 93
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDiTGLSGRELRPlrrrMQMVFQ--DPYASLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLNPGLTLN--ASQREKRDAIA---RQMGIESLMA-RLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:COG4608 116 DIIAEPLRIHglASKAERRERVAellELVGLRPEHAdRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 877977460 168 MLTLVSDICRERQLTLLMVSH--SVedaAR-IAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG4608 196 VLNLLEDLQDELGLTYLFISHdlSV---VRhISDRVAVMYLGKIVEIAPRDEL 245
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-218 |
1.68e-30 |
|
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: 118.38 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 22 VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFshlN--VQQNIGLGlN 97
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDiRDVTQASlRAAIGIVPQDTVLF---NdtIAYNIAYG-R 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGltlnASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:COG5265 457 PD----ASEEEVEAA-ARAAQIHDFIESLPdgydtrvGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTER 531
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 167 EMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:COG5265 532 AIQAALREVARGR--TTLVIAHrlsTIVDADEI----LVLEAGRIVERGTHAELL 580
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
2.33e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.67 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDI---TWLYHHLPMRFTLA-----VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhTLTPPS--- 69
Cdd:PRK13650 1 MSNIIEVknlTFKYKEDQEKYTLNdvsfhVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD--LLTEENvwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 70 -RRPVSMLFQE-NNLFSHLNVQQNIGLGL-NPGLTLNaSQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVR 146
Cdd:PRK13650 79 iRHKIGMVFQNpDNQFVGATVEDDVAFGLeNKGIPHE-EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 147 EQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAArIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-228 |
2.87e-30 |
|
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: 112.98 E-value: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQENnlFSHLN----VQ 89
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafRRDVQLVFQDS--PSAVNprmtVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 QNIGLGLNPGLTLNASQREKR-DAIARQMGIES-LMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:TIGR02769 109 QIIGEPLRHLTSLDESEQKARiAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAV 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:TIGR02769 189 ILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNL 249
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-217 |
4.49e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 111.46 E-value: 4.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRP---VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:TIGR03410 20 SLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYVPQGREIFPRLTVEENLLTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNpgltlnASQREKRDAIARQMGI----ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:TIGR03410 100 LA------ALPRRSRKIPDEIYELfpvlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:TIGR03410 174 IRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-217 |
4.93e-30 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 113.25 E-value: 4.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-RRPVSMLFQENNLFSHLNVQQNIGLgln 97
Cdd:TIGR01188 13 NFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKvRRSIGIVPQYASVDEDLTGRENLEM--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGLTLNASQREKRDAIARQMGIESLMA---RLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:TIGR01188 90 MGRLYGLPKDEAEERAEELLELFELGEaadRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 877977460 175 IcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:TIGR01188 170 L-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-221 |
8.27e-30 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 112.00 E-value: 8.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE--DHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGLTLNASQR-EKRDAIARQM---GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10253 106 RYPHQPLFTRWRkEDEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-229 |
1.01e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 111.14 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP---PSRRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK10895 23 SLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGIGYLPQEASIFRRLSVYDNLMAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:PRK10895 103 LQIRDDLSAEQREDRaNELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 175 IcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLG 229
Cdd:PRK10895 183 L-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-228 |
1.82e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.93 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQENnlFSHLNVQQNIG 93
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkafRRDIQMVFQDS--ISAVNPRKTVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLNPGL----TLNASQREKR-DAIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:PRK10419 110 EIIREPLrhllSLDKAERLARaSEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:PRK10419 190 VIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVL 250
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
20-209 |
6.87e-29 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 108.21 E-value: 6.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSR-----RPVSMLFQENNLFSHLNVQQNIG 93
Cdd:TIGR02211 26 LSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSlSKLSSNERaklrnKKLGFIYQFHHLLPDFTALENVA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LglnPGLTLNASQREKRD---AIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:TIGR02211 106 M---PLLIGKKSVKEAKErayEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFD 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 877977460 171 LVSDICRERQLTLLMVSHSVEDAARIaPRSIVVADGRIA 209
Cdd:TIGR02211 183 LMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-229 |
9.93e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 108.54 E-value: 9.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 14 LPMRF---------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPP---SRRPVSMLFQENN 81
Cdd:PRK11300 11 LMMRFggllavnnvNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVRTFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 82 LFSHLNVQQN--------IGLGLNPGL-TLNASQREKRDAIAR------QMGIESLMARLPGELSGGQRQRVALARCLVR 146
Cdd:PRK11300 91 LFREMTVIENllvaqhqqLKTGLFSGLlKTPAFRRAESEALDRaatwleRVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 147 EQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASA 226
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKA 250
|
...
gi 877977460 227 LLG 229
Cdd:PRK11300 251 YLG 253
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-213 |
2.85e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.91 E-value: 2.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP------PSRRPVSMLFQ--ENNLFSHlNVQQ 90
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikQIRKKVGLVFQfpESQLFEE-TVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 91 NIGLG-LNPGLTlnasqREKRDAIARQ----MGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:PRK13649 106 DVAFGpQNFGVS-----QEEAEALAREklalVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 877977460 165 RQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGK 213
Cdd:PRK13649 181 RKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-212 |
3.45e-28 |
|
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: 106.65 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtltPPSRRP-----VSMLF-QENNLFSHLNVQQNI 92
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV----PWKRRKkflrrIGVVFgQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GL-----GLNPgltlnASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:cd03267 117 YLlaaiyDLPP-----ARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-189 |
4.64e-28 |
|
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: 110.91 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFsHLNVQQNIGLGl 96
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAHLF-DTTVRENLRLA- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPgltlNASQREKRDAiARQMGIESLMARLPG-----------ELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:TIGR02868 433 RP----DATDEELWAA-LERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
170 180
....*....|....*....|....
gi 877977460 166 QEMLTLVSDICRERqlTLLMVSHS 189
Cdd:TIGR02868 508 DELLEDLLAALSGR--TVVLITHH 529
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-212 |
6.44e-28 |
|
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: 105.44 E-value: 6.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedHTLTPPSRRPVSMLFQENNLFSHLNVQ-QNIGLGLN 97
Cdd:cd03269 20 SFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--KPLDIAARNRIGYLPEERGLYPKMKVIdQLVYLAQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGLTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcR 177
Cdd:cd03269 98 KGLKKEEARRRIDEWLER-LELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-A 175
|
170 180 190
....*....|....*....|....*....|....*
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03269 176 RAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-219 |
7.97e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.81 E-value: 7.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAP-ASGTLLIAGEDHTLTPPS----RRPVSMLFQE-NNLFSHLNVQQNI 92
Cdd:PRK13640 27 SFSIPRGSWTALIGHNGSGKSTISKLINGLLLPdDNPNSKITVDGITLTAKTvwdiREKVGIVFQNpDNQFVGATVGDDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGL-NPGLTLNASQREKRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK13640 107 AFGLeNRAVPRPEMIKIVRDVLA-DVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAArIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13640 186 IRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-228 |
9.25e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 110.32 E-value: 9.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 15 PMRFTLavERGEQVAILGPSGAGKSTLLNLIAGFLaPASGTLLIAG-EDHTLTPPS-RRPVSMLFQENNLFsHLNVQQNI 92
Cdd:PRK11174 368 PLNFTL--PAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGiELRELDPESwRKHLSWVGQNPQLP-HGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGlNPgltlNASQREKRDAIArQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK11174 444 LLG-NP----DASDEQLQQALE-NAWVSEFLPLLPqgldtpiGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 162 P--------ALRQEMltlvsdicreRQLTLLMVSHSVEDAARIaPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:PRK11174 518 AhseqlvmqALNAAS----------RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-219 |
1.06e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.87 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSR--RPVSMLFQENNLFSHLNVQQNIGLGL 96
Cdd:PRK11231 22 SLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEGITVRELVAYGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLT----LNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK11231 102 SPWLSlwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLM 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 173 sdicRERQL---TLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK11231 182 ----RELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-222 |
1.36e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.24 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLI---------AGEDHTLTPPS---------RRPVSMLFQ- 78
Cdd:PRK13631 45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNPYSkkiknfkelRRRVSMVFQf 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 79 -ENNLFSHlNVQQNIGLGlnPgLTLNASQREKRDAIAR---QMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLL 153
Cdd:PRK13631 125 pEYQLFKD-TIEKDIMFG--P-VALGVKKSEAKKLAKFylnKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 154 DEPFSALDPALRQEMLTLVSDiCRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQA 222
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-219 |
1.83e-27 |
|
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: 109.51 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLI-AGEDHT-LTPP-------SRRPVSMLFQENNLFSHLNVQ 89
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVdMTKPgpdgrgrAKRYIGILHQEYDLYPHRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 QN----IGLGLNPGL-------TLNASQREKRDAiarqmgiESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:TIGR03269 384 DNlteaIGLELPDELarmkaviTLKMVGFDEEKA-------EEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 159 ALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-208 |
2.65e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.43 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatldaDALAQLRREHFGFIFQRYHLLSHLTAAQNV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GL-GLNPGLTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10535 108 EVpAVYAGLERKQRLLRAQELLQR-LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAI 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 877977460 172 VSDIcRERQLTLLMVSHSVEDAARiAPRSIVVADGRI 208
Cdd:PRK10535 187 LHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-208 |
3.20e-27 |
|
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: 103.49 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 4 LIDITWLYHHLPMRF---TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtlTPPSRRPVSMLFQEN 80
Cdd:cd03226 2 IENISFSYKKGTEILddlSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 81 NLFSHL---NVQQNIGLGLNPGltlnASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPF 157
Cdd:cd03226 79 DVDYQLftdSVREELLLGLKEL----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 158 SALDPalrqEMLTLVSDICRERQL---TLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03226 155 SGLDY----KNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-219 |
6.90e-27 |
|
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: 107.88 E-value: 6.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAG---EDHTLTPpSRRPVSMLFQENNLFSHlNVQQNIGL 94
Cdd:TIGR02203 351 ISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYTLAS-LRRQVALVSQDVVLFND-TIANNIAY 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 GLNPGLTLNASQREKRDAIARQM------GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:TIGR02203 429 GRTEQADRAEIERALAAAYAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLV 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 169 LTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:TIGR02203 509 QAALERLMQGR--TTLVIAHrlsTIEKADRI----VVMDDGRIVERGTHNELLA 556
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-208 |
8.71e-27 |
|
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: 101.52 E-value: 8.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIglgl 96
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNelGDHVGYLPQDDELFSG-SIAENI---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 npgltlnasqrekrdaiarqmgieslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIc 176
Cdd:cd03246 97 ---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL- 142
|
170 180 190
....*....|....*....|....*....|..
gi 877977460 177 RERQLTLLMVSHSVEdAARIAPRSIVVADGRI 208
Cdd:cd03246 143 KAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-208 |
1.15e-26 |
|
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: 102.55 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 6 DITWLYHHLPMR-----FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE-----DHTLTppsRRPVSM 75
Cdd:cd03248 16 NVTFAYPTRPDTlvlqdVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyEHKYL---HSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 76 LFQENNLFSHlNVQQNIGLGLNP---GLTLNASQREKRDAIARQM--GIESLMARLPGELSGGQRQRVALARCLVREQPV 150
Cdd:cd03248 93 VGQEPVLFAR-SLQDNIAYGLQScsfECVKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 151 LLLDEPFSALDPALRQEMLTLVSDiCRERQlTLLMVSH---SVEDAARIaprsIVVADGRI 208
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYD-WPERR-TVLVIAHrlsTVERADQI----LVLDGGRI 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-217 |
2.03e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.42 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLL---N----LIAGflAPASGTLLIAGED---HTLTPPS-RRPVSMLFQENNLFSHlN 87
Cdd:COG1117 31 NLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPG--ARVEGEILLDGEDiydPDVDVVElRRRVGMVFQKPNPFPK-S 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 88 VQQNIGLGLNpgltLN-ASQREKRDAIARqmgiESL-MARLPGE-----------LSGGQRQRVALARCLVREQPVLLLD 154
Cdd:COG1117 108 IYDNVAYGLR----LHgIKSKSELDEIVE----ESLrKAALWDEvkdrlkksalgLSGGQQQRLCIARALAVEPEVLLMD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 155 EPFSALDP--ALRQE--MLTLvsdicRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG1117 180 EPTSALDPisTAKIEelILEL-----KK-DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-219 |
2.63e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.94 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIagEDHTLTP--------PSRRPVSMLFQ--ENNLFSHlNVQ 89
Cdd:PRK13646 28 TEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHktkdkyirPVRKRIGMVFQfpESQLFED-TVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 QNIGLG-LNPGLTLNASQREKRDAIArQMGIE-SLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:PRK13646 105 REIIFGpKNFKMNLDEVKNYAHRLLM-DLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQ 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13646 184 VMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
18-218 |
3.28e-26 |
|
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: 106.18 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSR--RPVSMLFQENNLFSHlNVQQNIGLg 95
Cdd:TIGR03796 498 FSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVlaNSVAMVDQDIFLFEG-TVRDNLTL- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGLTLNASQREKRDAiarqmGIESLMARLPGE-----------LSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:TIGR03796 576 WDPTIPDADLVRACKDA-----AIHDVITSRPGGydaelaegganLSGGQRQRLEIARALVRNPSILILDEATSALDPET 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 165 RQEmltlVSDICRERQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:TIGR03796 651 EKI----IDDNLRRRGCTCIIVAHrlsTIRDCDEI----IVLERGKVVQRGTHEELW 699
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-212 |
3.82e-26 |
|
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: 101.19 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFL---APASGTLLIAGEdhtltPPSR----RPVSMLFQENNLFSHLNVQQN 91
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQ-----PRKPdqfqKCVAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IGLGLNPGLT--LNASQREKRDAIA--RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:cd03234 102 LTYTAILRLPrkSSDAIRKKRVEDVllRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 877977460 168 MLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03234 182 LVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-218 |
4.90e-26 |
|
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: 105.59 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFSHlNVQQNI 92
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrHTL----RQFINYLPQEPYIFSG-SILENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGLTLNASQR-----EKRDAIAR-QMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:TIGR01193 569 LLGAKENVSQDEIWAaceiaEIKDDIENmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEK 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 167 EmltLVSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELL 218
Cdd:TIGR01193 649 K---IVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
4.94e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 102.47 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 2 LKLIDITWLYHH-LPMRF------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLL----------------I 58
Cdd:PRK13651 3 IKVKNIVKIFNKkLPTELkaldnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekeK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 59 AGEDHTLTPPS----------RRPVSMLFQ--ENNLFSHlNVQQNIGLG-LNPGLTLNASQREKRDAIaRQMGI-ESLMA 124
Cdd:PRK13651 83 VLEKLVIQKTRfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGpVSMGVSKEEAKKRAAKYI-ELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 125 RLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVA 204
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|....*
gi 877977460 205 DGRIAWQGKTDELLS 219
Cdd:PRK13651 240 DGKIIKDGDTYDILS 254
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-228 |
6.53e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.04 E-value: 6.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPS-RRPVSMLFQENNLFSHlNVQQNIGLGl 96
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDiRTVTRASlRRNIAVVFQDAGLFNR-SIEDNIRVG- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 npglTLNASQREKRDAIARQMGIESLMARLPG----------ELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:PRK13657 433 ----RPDATDEEMRAAAERAQAHDFIERKPDGydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 167 EMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:PRK13657 509 KVKAALDELMKGR--TTFIIAHrlsTVRNADRI----LVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-216 |
8.72e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 8.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaiALGIGMVHQHFMLVPNLTVAENIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGltlnASQREKRDAIARQmgIESLMARLP---------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:COG3845 105 LEPT----KGGRLDRKAARAR--IRELSERYGldvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 167 EMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:COG3845 179 ELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-208 |
1.02e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 100.24 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSR-----RPVSMLFQENNLFSHLNVQQNIG 93
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlHQMDEEARaklraKHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LglnPGLTLNASQREKRD---AIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK10584 111 L---PALLRGESSRQSRNgakALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 877977460 171 LVSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRI 208
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
1.46e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.14 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 2 LKLIDITWLYHHLPM----RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSM 75
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvlkGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 76 LFQENNLFSHlNVQQNIGLGLNpgltlNASQrEKRDAIARQMGIESLMARLPG----------ELSGGQRQRVALARCLV 145
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLLAAP-----NASD-EALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 146 REQPVLLLDEPFSALDPALRQEMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHrltGLEQFDRI----CVMDNGQIIEQGTHQELLAQQ 564
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
20-221 |
1.69e-25 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 99.54 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtlTPPSRRPVSMLFQENNLFSH--LNVQQN------ 91
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---PGKGWRHIGYVPQRHEFAWDfpISVAHTvmsgrt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 --IGLGLNPGLtlnASQREKRDAIaRQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:TIGR03771 78 ghIGWLRRPCV---ADFAAVRDAL-RRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 170 TLVSDICRErQLTLLMVSHSVEDAARIAPRsIVVADGRIAWQGKTDELLSGQ 221
Cdd:TIGR03771 154 ELFIELAGA-GTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQLQDPA 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-219 |
1.91e-25 |
|
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: 103.61 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKS----TLLNLIAGFLAPASGTLLIAGEDHTLTPPSR------RPVSMLFQE-----NNLFS 84
Cdd:COG4172 31 FDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQEpmtslNPLHT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 85 hlnVQQNIGLGLNPGLTLNASQREKRdAIA--RQMGI---ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:COG4172 111 ---IGKQIAEVLRLHRGLSGAAARAR-ALEllERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 160 LDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4172 187 LDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-228 |
2.17e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.03 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFSHlNVQQNI 92
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlvqydhHYL----HRQVALVGQEPVLFSG-SVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNpgltlnASQREKRDAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:TIGR00958 576 AYGLT------DTPDEEIMAAAKAANAHDFIMEFPngydtevGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 162 PALRQemlTLVSDICRErQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:TIGR00958 650 AECEQ---LLQESRSRA-SRTVLLIAHrlsTVERADQI----LVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-212 |
2.80e-25 |
|
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: 98.44 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLN-P 98
Cdd:cd03268 21 LHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPNLTARENLRLLARlL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 GLtlnasqREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcR 177
Cdd:cd03268 101 GI------RKKRiDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-R 173
|
170 180 190
....*....|....*....|....*....|....*
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03268 174 DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-208 |
3.46e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.41 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPG 99
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlkNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 LTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICREr 179
Cdd:PRK10908 108 GASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV- 186
|
170 180
....*....|....*....|....*....
gi 877977460 180 QLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:PRK10908 187 GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
18-189 |
4.13e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.25 E-value: 4.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNIglg 95
Cdd:PRK10247 28 FSL--RAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVSYCAQTPTLFGD-TVYDNL--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGLTLNasQREKRDAIAR---QMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10247 102 IFPWQIRN--QQPDPAIFLDdleRFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEI 179
|
170
....*....|....*...
gi 877977460 172 VSDICRERQLTLLMVSHS 189
Cdd:PRK10247 180 IHRYVREQNIAVLWVTHD 197
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-219 |
6.68e-25 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 102.34 E-value: 6.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED--HTLTPPSRRPVSMLFQENNLFSHlNVQQNIgLGLN 97
Cdd:TIGR03797 474 LQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDlaGLDVQAVRRQLGVVLQNGRLMSG-SIFENI-AGGA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PgLTLNASQREKR------DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDpalrQEMLTL 171
Cdd:TIGR03797 552 P-LTLDEAWEAARmaglaeDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRTQAI 626
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 172 VSDICRERQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:TIGR03797 627 VSESLERLKVTRIVIAHrlsTIRNADRI----YVLDAGRVVQQGTYDELMA 673
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
1.05e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.65 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPS----RRPVSMLFQ--ENNLFShLNVQQNI 92
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE--VNAENekwvRSKVGLVFQdpDDQVFS-STVWDDV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLG-LNPGLTLNASQREKRDAIaRQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAlRQEMLTL 171
Cdd:PRK13647 102 AFGpVNMGLDKDEVERRVEEAL-KAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR-GQETLME 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 172 VSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGK----TDELLSGQA 222
Cdd:PRK13647 180 ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDksllTDEDIVEQA 234
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-219 |
1.96e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.22 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPASGTLLIAGEDHTLTPPSR--RPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGLTLNASQREKrDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPV-------LLLDEPFSALDPALRQEM 168
Cdd:COG4138 94 QPAGASSEAVEQLL-AQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTinpegqlLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 169 LTLVSDICrERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4138 173 DRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-212 |
2.01e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.94 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 11 YHHLPMRFTLAVERGEQVAILGPSGAGKST----LLNLIAgflapASGTLLIAGED-HTLTP----PSRRPVSMLFQENN 81
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPlHNLNRrqllPVRHRIQVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 82 --LFSHLNVQQNIGLGL---NPglTLNASQREKR-DAIARQMGIE-SLMARLPGELSGGQRQRVALARCLVREQPVLLLD 154
Cdd:PRK15134 373 ssLNPRLNVLQIIEEGLrvhQP--TLSAAQREQQvIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 155 EPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-217 |
2.29e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.39 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLN----LIAGFLAPASGTLLI------AGEDHTLTPPSRRPVSMLFQENNLFSHLNVQ 89
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLgrtvqrEGRLARDIRKSRANTGYIFQQFNLVNRLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 QNI---GLGLNPGLT-----LNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK09984 105 ENVligALGSTPFWRtcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 162 PALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK09984 185 PESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-208 |
2.68e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTP------PSRRPVSMLFQ--ENNLFSHlNVQQN 91
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikPVRKKVGVVFQfpESQLFEE-TVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IGLG-LNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK13643 106 VAFGpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 877977460 171 LVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:PRK13643 186 LFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-219 |
2.78e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.47 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQ--ENNLFSHLnVQQNIG 93
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdiRNKAGMVFQnpDNQIVATI-VEEDVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 -----LGLNPgltlnASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:PRK13633 109 fgpenLGIPP-----EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 169 LTLVSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13633 184 VNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-208 |
2.79e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.42 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSR-----RPVSMLFQENNLFSHLNVQQNI 92
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALENV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK11629 109 AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLL 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 877977460 173 SDICRERQLTLLMVSHSVEDAARIApRSIVVADGRI 208
Cdd:PRK11629 189 GELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-221 |
4.24e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.57 E-value: 4.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGL-GL 96
Cdd:PRK13537 27 SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvPSRARHARQRVGVVPQFDNLDPDFTVRENLLVfGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT-LVSDI 175
Cdd:PRK13537 107 YFGLS-AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWErLRSLL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 877977460 176 CRERqlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK13537 186 ARGK--TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-163 |
6.71e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.56 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAveRGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRpVSMLFQENNLFSHLNVQQNIGLGLN 97
Cdd:PRK13539 23 FTLA--AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEFWAA 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 98 pglTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK13539 100 ---FLGGEELDIAAALEA-VGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-219 |
7.58e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.32 E-value: 7.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhTLTPPS----RRPVSMLFQE-NNLFSHLNVQQNIG 93
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE--LLTAENvwnlRRKIGMVFQNpDNQFVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVS 173
Cdd:PRK13642 105 FGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 877977460 174 DICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13642 185 EIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-219 |
1.09e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.36 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 29 AILGPSGAGKSTLLNLIAGFL-----APASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHLNVQQNIGLGLNPGLT 101
Cdd:PRK14247 33 ALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIelRRRVQMVFQIPNPIPNLSIFENVALGLKLNRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 102 LNAS---QREKRDAIARQMGIESLMARL---PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:PRK14247 113 VKSKkelQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 877977460 176 crERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK14247 193 --KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-218 |
1.16e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.29 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 29 AILGPSGAGKSTLLNLIAGFL-----APASGTLLIAGED---HTLTPPS-RRPVSMLFQENNLFSHLNVQQNIGLGLNpg 99
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNiysPDVDPIEvRREVGMVFQYPNPFPHLTIYDNVAIGVK-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 ltLNASQREKRD-------AIARQMGIESLMARL---PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK14267 112 --LNGLVKSKKEldervewALKKAALWDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 877977460 170 TLVSDIcrERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:PRK14267 190 ELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-210 |
1.28e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgedHTLTppsrrpVSMLFQEN-NLFSHLNVQQNIGlGL 96
Cdd:COG0488 334 LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---ETVK------IGYFDQHQeELDPDKTVLDELR-DG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTlnasQREKRDAIARqMGIESLMARLP-GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPalrqEMLTLVSDI 175
Cdd:COG0488 404 APGGT----EQEVRGYLGR-FLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEA 474
|
170 180 190
....*....|....*....|....*....|....*
gi 877977460 176 CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAW 210
Cdd:COG0488 475 LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-218 |
2.14e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.92 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedhtLTPPSRRP-----VSMLF-QENNLFSHLNVQQNi 92
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG----YVPFKRRKefarrIGVVFgQRSQLWWDLPAIDS- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 glglnpgLTLNAS--------QREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:COG4586 117 -------FRLLKAiyripdaeYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 165 RQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:COG4586 190 KEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELK 243
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-229 |
2.78e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.79 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkimREAVAIVPEGRRVFSRMTVEENLAMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 lnpGLTLNASQREKRdaIARqmgIESLMARL-------PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:PRK11614 105 ---GFFAERDQFQER--IKW---VYELFPRLherriqrAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 169 LTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASALLG 229
Cdd:PRK11614 177 FDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-219 |
3.56e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.09 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 15 PMRFTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIagEDHTLT-----PPSRRpVSMLFQENNlfSHLNVQ 89
Cdd:PRK15112 31 PLSFTL--REGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI--DDHPLHfgdysYRSQR-IRMIFQDPS--TSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 QNIGLGLNPGLTLN----ASQREKR-DAIARQMGIESLMARL-PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK15112 104 QRISQILDFPLRLNtdlePEQREKQiIETLRQVGLLPDHASYyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK15112 184 MRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
3.74e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.79 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITwlyhhlpMRF---------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPSRR 71
Cdd:COG4152 1 MLELKGLT-------KRFgdktavddvSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP--LDPEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 72 PVSMLFQENNLFSHLNVQQNIG-LG-LNpGLTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQP 149
Cdd:COG4152 72 RIGYLPEERGLYPKMKVGEQLVyLArLK-GLSKAEAKRRADEWLER-LGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 150 VLLLDEPFSALDP----ALRQEMLTLvsdicRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:COG4152 150 LLILDEPFSGLDPvnveLLKDVIREL-----AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-224 |
6.89e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.62 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 29 AILGPSGAGKSTLL-------NLIAGFlaPASGTLLIAGE---DHTLTPPSRRPVSMLFQENNLFShLNVQQNIGLG--- 95
Cdd:PRK14271 51 SLMGPTGSGKTTFLrtlnrmnDKVSGY--RYSGDVLLGGRsifNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGvra 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 --LNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVS 173
Cdd:PRK14271 128 hkLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 174 DICreRQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASA 224
Cdd:PRK14271 208 SLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-217 |
7.14e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 7.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT-LTPPSRRPVSMLF--QENNLFSHLNVQQNIGL 94
Cdd:PRK15439 32 FTL--HAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArLTPAKAHQLGIYLvpQEPLLFPNLSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 glnpGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAlrqEMLTLVSD 174
Cdd:PRK15439 110 ----GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPA---ETERLFSR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 877977460 175 I--CRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK15439 183 IreLLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-219 |
1.02e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLA------PASGTLLIAGED--HTLTPPSRRPVSMLFQENNLFSHLNVQQ 90
Cdd:PRK14246 30 TIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDifQIDAIKLRKEVGMVFQQPNPFPHLSIYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 91 NIGLGLNP-GLTLNASQREKRDAIARQMGI-ESLMARL---PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:PRK14246 110 NIAYPLKShGIKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 166 QEMLTLVSDIcrERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK14246 190 QAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-221 |
1.14e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgeDHTLtpPS-----------RRPVSMLFQ--ENNLFSH 85
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG--DYAI--PAnlkkikevkrlRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 86 lNVQQNIGLGlnpGLTLNASQREKRDAIARQMGIESL----MARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK13645 107 -TIEKDIAFG---PVNLGENKQEAYKKVPELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 162 PALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQ 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-208 |
1.74e-22 |
|
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: 90.18 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRpvsmlfqennlfshlnvqQNIGLGLN 97
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA------------------IRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGltlnasQReKRDAIARQMGIESLMArLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcR 177
Cdd:cd03215 81 PE------DR-KREGLVLDLSVAENIA-LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-A 151
|
170 180 190
....*....|....*....|....*....|.
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:cd03215 152 DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-212 |
2.51e-22 |
|
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: 90.30 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPA--SGTLLIAGEDHTLTPPSRRpVSMLFQENNLFSHLNVQqniglgl 96
Cdd:cd03213 29 SGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVR------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 npgltlnasqrekrdaiarqmgiESLM--ARLPGeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:cd03213 101 -----------------------ETLMfaAKLRG-LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 877977460 175 ICRErQLTLLMVSHSvedaariaPRS---------IVVADGRIAWQG 212
Cdd:cd03213 157 LADT-GRTIICSIHQ--------PSSeifelfdklLLLSQGRVIYFG 194
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-219 |
2.91e-22 |
|
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: 94.43 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRP-VSMLFQENNLFSHlNVQQNIGLgl 96
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADlSQWDREELGRhIGYLPQDVELFDG-TIAENIAR-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 npgltLNASQREKRDAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDP--- 162
Cdd:COG4618 429 -----FGDADPEKVVAAAKLAGVHEMILRLPdgydtriGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDege 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 163 -ALRQEMLTLvsdicRERQLTLLMVSHSVEdAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4618 504 aALAAAIRAL-----KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-216 |
4.13e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.91 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhtltppsrrpVSMLFqennlfshlnvqqNIGLGLNP 98
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-----------VSALL-------------ELGAGFHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 GLT------LNASQ--------REKRDAIARQMGIESLMaRLP-GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:COG1134 102 ELTgreniyLNGRLlglsrkeiDEKFDEIVEFAELGDFI-DQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 877977460 164 LRQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:COG1134 181 FQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
25-218 |
4.66e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.14 E-value: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLTPPSRRpvsMLFQENNLFshlnVQQNIGLGLNP 98
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYALSEAERR---RLLRTEWGF----VHQHPRDGLRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 GLTLNASQREK------------RDAIARQMG-IESLMAR---LPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDP 162
Cdd:PRK11701 105 QVSAGGNIGERlmavgarhygdiRATAGDWLErVEIDAARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 163 ALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:PRK11701 185 SVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-219 |
5.00e-22 |
|
type I secretion system ABC transporter, PrtD 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: 200134 [Multi-domain] Cd Length: 544 Bit Score: 93.95 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLTPPsrrpVSMLFQENNLFSHlNVQQNI 92
Cdd:TIGR01842 338 SFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADlkqwdrETFGKH----IGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 G-LGLNPgltlnasQREKRDAIARQMGIESLMARLP-----------GELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:TIGR01842 413 ArFGENA-------DPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 161 DP----ALRQEMLTLvsdicRERQLTLLMVSHSVEdAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR01842 486 DEegeqALANAIKAL-----KARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
26-217 |
7.12e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.61 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 26 EQVAILGPSGAGKSTLLNLI--AGFLAP---ASGTLLIAGED----HTLTPPSRRPVSMLFQENNLFShLNVQQNI--GL 94
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNiyspRTDTVDLRKEIGMVFQQPNPFP-MSIYENVvyGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 GLNpGLTLNASQREKRDAIARQMGI-ESLMARLPGE---LSGGQRQRVALARCLVREQPVLLLDEPFSALDP---ALRQE 167
Cdd:PRK14239 111 RLK-GIKDKQVLDEAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPisaGKIEE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 168 MLTLVSDicrerQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK14239 190 TLLGLKD-----DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-230 |
8.02e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.58 E-value: 8.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTL-----AVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIagEDHTLTPPS----RRPVSMLFQE-NNLFSHLN 87
Cdd:PRK13648 23 FTLkdvsfNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY--NNQAITDDNfeklRKHIGIVFQNpDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 88 VQQNIGLGL-NPGLTLNASQREKRDAIaRQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:PRK13648 101 VKYDVAFGLeNHAVPYDEMHRRVSEAL-KQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 167 EMLTLVSDICRERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLSgqaSASALLGI 230
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD---HAEELTRI 239
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-219 |
8.69e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 89.99 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLaPASGTLLIAG---EDHTLTPPSRRPVSMLFQENNLFShLNVQQNIGL 94
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGqplEAWSAAELARHRAYLSQQQTPPFA-MPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 GLNPGLTLNASQREKRDaIARQMGIESLMARLPGELSGGQRQRVALARCLVREQP-------VLLLDEPFSALDPALRQE 167
Cdd:PRK03695 93 HQPDKTRTEAVASALNE-VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDVAQQAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 168 MLTLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK03695 172 LDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-219 |
9.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 9.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAG---EDHTLTPPSRRPVSMLFQE-NNLFSHLNVQQNIGLG 95
Cdd:PRK13644 23 LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDLAFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 lNPGLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:PRK13644 103 -PENLCLPPIEIRKRvDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 877977460 175 IcRERQLTLLMVSHSVEDaARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13644 182 L-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-212 |
1.50e-21 |
|
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: 93.15 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:TIGR01257 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LN-PGLTLNASQREKrDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD 174
Cdd:TIGR01257 1028 AQlKGRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180 190
....*....|....*....|....*....|....*...
gi 877977460 175 ICRERqlTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:TIGR01257 1107 YRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-218 |
1.80e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.39 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAG---EDHTLTPpSRRPVSMLFQENNLFSHlNVQQNIGLGL 96
Cdd:PRK11176 364 FKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLAS-LRNQVALVSQNVHLFND-TIANNIAYAR 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTLNASQREKRDAIArqMGIESLMAR----LPGE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:PRK11176 442 TEQYSREQIEEAARMAYA--MDFINKMDNgldtVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 877977460 169 LTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:PRK11176 520 QAALDELQKNR--TSLVIAHrlsTIEKADEI----LVVEDGEIVERGTHAELL 566
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-221 |
3.10e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.08 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 10 LYHHLPMRFTLaverGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE--DHTLTPPSRRPVSMLFQENNLFSHLN 87
Cdd:PRK10575 26 LLHPLSLTFPA----GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 88 VQQNIGLGLNP---GL-TLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK10575 102 VRELVAIGRYPwhgALgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-188 |
6.85e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 6.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIagedhtltPPSRRpVSMLFQENNLFSHLNVQQNIGLGLNP 98
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR-IGYLPQEPPLDDDLTVLDTVLDGDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 GLTLnasqREKRDAIARQMG---------------------------IESLMARL----------PGELSGGQRQRVALA 141
Cdd:COG0488 89 LRAL----EAELEELEAKLAepdedlerlaelqeefealggweaearAEEILSGLgfpeedldrpVSELSGGWRRRVALA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 142 RCLVREQPVLLLDEPFSALD-PALR--QEMLtlvsdicRERQLTLLMVSH 188
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHLDlESIEwlEEFL-------KNYPGTVLVVSH 207
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-202 |
7.14e-21 |
|
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: 87.85 E-value: 7.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVE-----RGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNvqqni 92
Cdd:cd03237 13 FTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLLSSITK----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGlnpgltlnaSQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDpalrQEMLTLV 172
Cdd:cd03237 88 DFY---------THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VEQRLMA 154
|
170 180 190
....*....|....*....|....*....|....
gi 877977460 173 SDICR----ERQLTLLMVSHSVEDAARIAPRSIV 202
Cdd:cd03237 155 SKVIRrfaeNNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-219 |
9.31e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.49 E-value: 9.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIAGFLAPA---SGTLLIAGedHTLTPPSRRPVSMLFQENNLF-------SHLNVQQNIGL 94
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNG--MPIDAKEMRAISAYVQQDDLFiptltvrEHLMFQAHLRM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 GLNpgltLNASQREKR-DAIARQMGIES-------LMARLPGeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:TIGR00955 129 PRR----VTKKEKRERvDEVLQALGLRKcantrigVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 877977460 167 EMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-163 |
1.19e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 85.87 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 15 PMRFTLAVerGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRrpvsmlfQENNLF-SHLNvqqnig 93
Cdd:TIGR01189 18 GLSFTLNA--GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-------HENILYlGHLP------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 lGLNPGLT-----------LNASQREKRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDP 162
Cdd:TIGR01189 83 -GLKPELSalenlhfwaaiHGGAQRTIEDALA-AVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
.
gi 877977460 163 A 163
Cdd:TIGR01189 161 A 161
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
19-216 |
1.72e-20 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 86.30 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLglnp 98
Cdd:TIGR03740 20 SLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG--HPWTRKDLHKIGSLIESPPLYENLTARENLKV---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 gLTLNASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcR 177
Cdd:TIGR03740 94 -HTTLLGLPDSRiDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQELRELIRSF-P 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:TIGR03740 172 EQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-217 |
4.92e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.68 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtLTPPS-------RRPVSMLFQENnlFSHLNVQQN 91
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD--LLGMKddewravRSDIQMIFQDP--LASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IG-------LGLNPGLTlNASQREKRDAIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK15079 117 IGeiiaeplRTYHPKLS-RQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-207 |
5.15e-20 |
|
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: 84.79 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTL---TPPSRRPVSMLFQENNLFS-HLNV---QQ 90
Cdd:COG4778 30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVdlaQASPREILALRRRTIGYVSqFLRViprVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 91 NIGLGLNPGLTLNASQREKRD---AIARQMGI-ESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:COG4778 110 ALDVVAEPLLERGVDREEARArarELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 877977460 167 EMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:COG4778 190 VVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-209 |
9.82e-20 |
|
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: 84.08 E-value: 9.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFSHlNVQQNi 92
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglHDL----RSRISIIPQDPVLFSG-TIRSN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 glgLNPgltLNASQREKRDAIARQMGIESLMARLPGEL-----------SGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:cd03244 98 ---LDP---FGEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 162 PALRQEMLTLVSDICRERqlTLLMVSHSVE---DAARIaprsIVVADGRIA 209
Cdd:cd03244 172 PETDALIQKTIREAFKDC--TVLTIAHRLDtiiDSDRI----LVLDKGRVV 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-212 |
1.06e-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: 84.12 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedhtltppsrRPVSMLFqennlfshlnvqqnIGLGLNP 98
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLG--------------LGGGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 GLT-----------LNASQREKRDAIARqmgIESLmARLP-------GELSGGQRQRV--ALARCLvrEQPVLLLDEPFS 158
Cdd:cd03220 98 ELTgreniylngrlLGLSRKEIDEKIDE---IIEF-SELGdfidlpvKTYSSGMKARLafAIATAL--EPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 159 ALDPALRQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03220 172 VGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-212 |
1.98e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.11 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFL--------APASGTLLIAGEDHTLTPPSR--RPVSMLFQENNLFSHLNV 88
Cdd:PRK13547 21 SLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIDAPRlaRLRAVLPQAAQPAFAFSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 89 QQNIGLGLNP-GLTLNASQREKRDAIARQM---GIESLMARLPGELSGGQRQRVALARCLVREQP---------VLLLDE 155
Cdd:PRK13547 101 REIVLLGRYPhARRAGALTHRDGEIAWQALalaGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqpprYLLLDE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 156 PFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:PRK13547 181 PTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-197 |
4.69e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.16 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIaGFLAPASGTLLIAG----------EDHTLTPPSRRPVSMLFQENNLFShLNV 88
Cdd:PRK14258 27 SMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGrveffnqniyERRVNLNRLRRQVSMVHPKPNLFP-MSV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 89 QQNIGLGL-----NPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:PRK14258 105 YDNVAYGVkivgwRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPI 184
|
170 180 190
....*....|....*....|....*....|....
gi 877977460 164 LRQEMLTLVSDICRERQLTLLMVSHSVEDAARIA 197
Cdd:PRK14258 185 ASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-188 |
5.05e-19 |
|
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: 85.22 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVE-----RGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLliageDHTLTppsrrpVSMLFQENNLFSHLNVQQNI 92
Cdd:COG1245 354 FSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLK------ISYKPQYISPDYDGTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGLTLNASQREkrdaIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:COG1245 423 RSANTDDFGSSYYKTE----IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170
....*....|....*.
gi 877977460 173 SDICRERQLTLLMVSH 188
Cdd:COG1245 499 RRFAENRGKTAMVVDH 514
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-197 |
5.24e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.91 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLL-------NLIAGFLAPASgtllIAGEDHTLTPPS------RRPVSMLFQENNLFSH 85
Cdd:PRK14243 30 WLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRVEGK----VTFHGKNLYAPDvdpvevRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 86 lNVQQNIGLG-------------LNPGLTLNASQREKRDAIaRQMGIEslmarlpgeLSGGQRQRVALARCLVREQPVLL 152
Cdd:PRK14243 106 -SIYDNIAYGaringykgdmdelVERSLRQAALWDEVKDKL-KQSGLS---------LSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 877977460 153 LDEPFSALDP--ALRQE--MLTLVsdicreRQLTLLMVSHSVEDAARIA 197
Cdd:PRK14243 175 MDEPCSALDPisTLRIEelMHELK------EQYTIIIVTHNMQQAARVS 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-228 |
9.02e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-------------RRpvsmlfqENNLFSHL 86
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairagiayvpedRK-------GEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 87 NVQQNIGLG----LNPGLTLNasqREKRDAIARQMgIESLMARLP------GELSGGQRQRVALARCLVREQPVLLLDEP 156
Cdd:COG1129 346 SIRENITLAsldrLSRGGLLD---RRRERALAEEY-IKRLRIKTPspeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 877977460 157 FSALDPALRQEMLTLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIawqgkTDELLSGQASASALL 228
Cdd:COG1129 422 TRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI-----VGELDREEATEEAIM 487
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-221 |
1.07e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtlTPP----SRRPVSMLFQENNLFSHLNVQQNIgl 94
Cdd:PRK13536 61 SFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP---VPArarlARARIGVVPQFDNLDLEFTVRENL-- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 gLNPGLTLNASQREKRDAIArqmgieSLM--ARLP-------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:PRK13536 136 -LVFGRYFGMSTREIEAVIP------SLLefARLEskadarvSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 166 QemltLVSDICRE---RQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK13536 209 H----LIWERLRSllaRGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-207 |
2.26e-18 |
|
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: 79.82 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedhtltppsrrPVSMLFQENNLFShLNVQQNI--GLGLN 97
Cdd:cd03250 26 LEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQEPWIQN-GTIRENIlfGKPFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PgltlnasQREKR--DAIARQMGIESLMARLP---GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:cd03250 94 E-------ERYEKviKACALEPDLEILPDGDLteiGEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 877977460 169 LTLVsdICRERQL--TLLMVSHSVE---DAARIaprsIVVADGR 207
Cdd:cd03250 167 FENC--ILGLLLNnkTRILVTHQLQllpHADQI----VVLDNGR 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-219 |
3.54e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKS-TLLNLIAGFLAPA----SGTLLIAGED--HTLTPPSRR----PVSMLFQENnlFSHLN 87
Cdd:PRK15134 29 SLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESllHASEQTLRGvrgnKIAMIFQEP--MVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 88 VQQNIG------LGLNPGLTLNASQREKRDAIARqMGIESLMARL---PGELSGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:PRK15134 107 PLHTLEkqlyevLSLHRGMRREAARGEILNCLDR-VGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 159 ALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK15134 186 ALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-219 |
9.68e-18 |
|
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: 81.39 E-value: 9.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGF--LAPASGTLLI----------------AGE------------------- 61
Cdd:TIGR03269 20 SFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVGEpcpvcggtlepeevdfwnl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 62 DHTLTPPSRRPVSMLFQEN-NLFSHLNVQQNIglgLNpglTLNASQREKRDAIAR------QMGIESLMARLPGELSGGQ 134
Cdd:TIGR03269 100 SDKLRRRIRKRIAIMLQRTfALYGDDTVLDNV---LE---ALEEIGYEGKEAVGRavdlieMVQLSHRITHIARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 135 RQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKT 214
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTP 253
|
....*
gi 877977460 215 DELLS 219
Cdd:TIGR03269 254 DEVVA 258
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-163 |
2.65e-17 |
|
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: 77.15 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE-DHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLg 95
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 96 lnpgLTLNASQREKRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:cd03231 97 ----WHADHSDEQVEEALA-RVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
10-161 |
2.94e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 10 LYHHLpmrfTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSrrpvsmlFQENNLF-SHLNv 88
Cdd:PRK13538 16 LFSGL----SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlGHQP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 89 qqniglGLNPGLT----LNASQR----EKRDAIA---RQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPF 157
Cdd:PRK13538 84 ------GIKTELTalenLRFYQRlhgpGDDEALWealAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
....
gi 877977460 158 SALD 161
Cdd:PRK13538 158 TAID 161
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-226 |
3.02e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.20 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKS----TLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMlfqennlfshlnVQQNIGLG 95
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIAT------------IMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGLTLNASQREKRDAIARQMGIESLMARL---------------PGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPADDATLTAALeavglenaarvlklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 161 DPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASA 226
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-207 |
3.94e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.48 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPAS--GTLLIAGED---HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGL 94
Cdd:TIGR02633 22 LEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPlkaSNIRDTERAGIVIIHQELTLVPELSVAENIFL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 G----LNPGLTLNASQREKRDAIARQMGIESL-MARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:TIGR02633 102 GneitLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILL 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 877977460 170 TLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:TIGR02633 182 DIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-206 |
6.36e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT-LTP--PSRRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK09700 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkLDHklAAQLGIGIIYQELSVIDELTVLENLYIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNP-----GLTLN--ASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPAlRQEM 168
Cdd:PRK09700 105 RHLtkkvcGVNIIdwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK-EVDY 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 877977460 169 LTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADG 206
Cdd:PRK09700 184 LFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-207 |
1.25e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTppSRRP-----VSMLFQENNLFSHLNVQQNIGL 94
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA--STTAalaagVAIIYQELHLVPEMTVAENLYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 GLNPG----LTLNASQREKRDAIARqMGIE-SLMARLpGELSGGQRQRVALARCLVREQPVLLLDEPFSALDpALRQEML 169
Cdd:PRK11288 103 GQLPHkggiVNRRLLNYEAREQLEH-LGVDiDPDTPL-KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS-AREIEQL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 877977460 170 TLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:PRK11288 180 FRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-207 |
1.60e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPA---SGTLLIAGED---HTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEElqaSNIRDTERAGIAIIHQELALVKELSVLENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNP---GLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEML 169
Cdd:PRK13549 104 FLGNEItpgGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 877977460 170 TLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:PRK13549 184 DIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-219 |
1.86e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.20 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPMR--FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS----RRPVS 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLkgLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllalRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 75 MLFQ--ENNLFsHLNVQQNIGLGL-NPGLTLNASQREKRDAIA-------RQMGIESLmarlpgelSGGQRQRVALARCL 144
Cdd:PRK13638 81 TVFQdpEQQIF-YTDIDSDIAFSLrNLGVPEAEITRRVDEALTlvdaqhfRHQPIQCL--------SHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 145 VREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-208 |
2.01e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.59 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-----RRPVSMLFQENnlFSHLNVQQNIGLGLNPG 99
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalRRDIQFIFQDP--YASLDPRQTVGDSIMEP 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 LT----LNASQREKRDA-IARQMGIESLMA-RLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVS 173
Cdd:PRK10261 428 LRvhglLPGKAAAARVAwLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180 190
....*....|....*....|....*....|....*
gi 877977460 174 DICRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:PRK10261 508 DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-188 |
2.41e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.54 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPsRRPvsmLFQENNLFSHLnvqqniglgLN 97
Cdd:COG4178 382 LSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLP-QRP---YLPLGTLREAL---------LY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGLTLNASQREKRDAIaRQMGIESLMARL------PGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:COG4178 449 PATAEAFSDAELREAL-EAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL 527
|
170
....*....|....*..
gi 877977460 172 VSDICRErqLTLLMVSH 188
Cdd:COG4178 528 LREELPG--TTVISVGH 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-161 |
3.88e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVE-----RGEQVAILGPSGAGKSTLLNLIAGFLAPASG----TLLIAGEDHTLTPPSRRPVSMLFQENNlfshlnv 88
Cdd:PRK13409 353 FSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpELKISYKPQYIKPDYDGTVEDLLRSIT------- 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 89 qqniglglnPGLTLNASQREkrdaIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK13409 426 ---------DDLGSSYYKSE----IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-234 |
1.01e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 5 IDITWLYHHLPMR-FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhtltpPSRRPVsmlfqENNLF 83
Cdd:PRK15056 12 VTVTWRNGHTALRdASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ------PTRQAL-----QKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 84 SHLNVQQNI--------------GLGLNPGLTLNASQREKR---DAIARqMGIESLMARLPGELSGGQRQRVALARCLVR 146
Cdd:PRK15056 81 AYVPQSEEVdwsfpvlvedvvmmGRYGHMGWLRRAKKRDRQivtAALAR-VDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 147 EQPVLLLDEPFSALDPALRQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVaDGRIAWQGKTDELLSGQASASA 226
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLELA 237
|
....*...
gi 877977460 227 LLGIKSHI 234
Cdd:PRK15056 238 FSGVLRHV 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-161 |
2.82e-15 |
|
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: 74.44 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 14 LPMrftlaVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGtlliageDHTlTPPSRRPVSMLFQENNLFSHLN--VQQN 91
Cdd:COG1245 93 LPV-----PKKGKVTGILGPNGIGKSTALKILSGELKPNLG-------DYD-EEPSWDEVLKRFRGTELQDYFKklANGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IGLGLNP---------------GLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEP 156
Cdd:COG1245 160 IKVAHKPqyvdlipkvfkgtvrELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
....*
gi 877977460 157 FSALD 161
Cdd:COG1245 240 SSYLD 244
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-195 |
3.16e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.39 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 12 HHLPMRF---------TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedHTLTP---PSRRPVSMLFQE 79
Cdd:NF033858 270 RGLTMRFgdftavdhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG--QPVDAgdiATRRRVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 80 NNLFSHLNVQQNiglglnpgLTLNA-------SQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVL 151
Cdd:NF033858 348 FSLYGELTVRQN--------LELHArlfhlpaAEIAARvAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELL 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 877977460 152 LLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAAR 195
Cdd:NF033858 420 ILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER 463
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-189 |
3.78e-15 |
|
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: 70.65 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPA-SGTLLIAGEDHTLTPPsRRPVsmlfqennlfshlnvqqniglgLN 97
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRIGMPEGEDLLFLP-QRPY----------------------LP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 PGlTLnasqrekRDAIARQMGIEslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLtlvsDICR 177
Cdd:cd03223 77 LG-TL-------REQLIYPWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY----QLLK 135
|
170
....*....|..
gi 877977460 178 ERQLTLLMVSHS 189
Cdd:cd03223 136 ELGITVISVGHR 147
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-209 |
4.05e-15 |
|
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: 71.29 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFShlnvqQNIGLGL 96
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlRSSLTIIPQDPTLFS-----GTIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPgltLNA-SQREKRDAIARQMGIESlmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRqemlTLVSDI 175
Cdd:cd03369 103 DP---FDEySDEEIYGALRVSEGGLN--------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD----ALIQKT 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 877977460 176 CRE--RQLTLLMVSH---SVEDAARIaprsIVVADGRIA 209
Cdd:cd03369 168 IREefTNSTILTIAHrlrTIIDYDKI----LVMDAGEVK 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-228 |
8.20e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED-----HtltppsRRPVS-----M---LfqENNLFSH 85
Cdd:NF033858 21 SLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDmadarH------RRAVCpriayMpqgL--GKNLYPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 86 LNVQQNI-------GLGlnpgltlnASQREKR-DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPF 157
Cdd:NF033858 93 LSVFENLdffgrlfGQD--------AAERRRRiDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 158 SALDPALRQEMLTLVSDICRER-QLTLLMVSHSVEDAARIaprSIVVA--DGRIAWQGKTDELLSGQASAS------ALL 228
Cdd:NF033858 165 TGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAERF---DWLVAmdAGRVLATGTPAELLARTGADTleaafiALL 241
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-173 |
8.49e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.99 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGLNPGLTLNA 104
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSL 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 105 SQREK---RDAIARQMGIESLMARLPGE-----LSGGQRQRVALARCLVREQPVLLLDEPFSALDP-ALRQEMLTLVS 173
Cdd:PLN03211 174 TKQEKilvAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDAtAAYRLVLTLGS 251
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-208 |
8.63e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.74 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 12 HHLpmrfTLAVERGEQVAILGPSGAGKSTLLNLIAGflapasgtlliageDH------TLTPPSRRPVS----------M 75
Cdd:PRK10938 277 HNL----SWQVNPGEHWQIVGPNGAGKSTLLSLITG--------------DHpqgysnDLTLFGRRRGSgetiwdikkhI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 76 LFQENNLfsHLNVQQNI--------GLGLNPGLTLNASQREKRdaIARQ----MGIESLMARLP-GELSGGQrQRVAL-A 141
Cdd:PRK10938 339 GYVSSSL--HLDYRVSTsvrnvilsGFFDSIGIYQAVSDRQQK--LAQQwldiLGIDKRTADAPfHSLSWGQ-QRLALiV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 142 RCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAAR-IAPRSIVVADGRI 208
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-228 |
9.56e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 9.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPP--SRRPVSMLFQENN----LFSHLNVQQN 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrdAIRAGIMLCPEDRkaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IGLG-----LNPGLTLNAsQREKRDAiARQmgIESLMARLP------GELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK11288 352 INISarrhhLRAGCLINN-RWEAENA-DRF--IRSLNIKTPsreqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 161 DPALRQEMLTLVSDICrERQLTLLMVSHSVEDAARIAPRSIVVADGRIAwqgktDELLSGQASASALL 228
Cdd:PRK11288 428 DVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIA-----GELAREQATERQAL 489
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-217 |
1.52e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 71.29 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVerGEQVAILGPSGAGKSTLLNLIAGFLAP---ASGTLLIAGEDhTLTPPSRR-------PVSMLFQENnlFSHLN 87
Cdd:PRK09473 37 FSLRA--GETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGRE-ILNLPEKElnklraeQISMIFQDP--MTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 88 VQQNIG------LGLNPGLTLNASQREK---RDAI----ARQMgieslMARLPGELSGGQRQRVALARCLVREQPVLLLD 154
Cdd:PRK09473 112 PYMRVGeqlmevLMLHKGMSKAEAFEESvrmLDAVkmpeARKR-----MKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 155 EPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-218 |
1.86e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.05 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 16 MRFTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTllIAGEDHTLTPPS----RRPVSMLFQENNLFSHlNVQQN 91
Cdd:PRK10789 334 VNFTL--KPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD--IRFHDIPLTKLQldswRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IGLGlNPgltlNASQREKRDAiARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK10789 409 IALG-RP----DATQQEIEHV-ARLASVHDDILRLPqgydtevGErgvmLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 161 DPALRQEMLTLVSDICRERqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELL 218
Cdd:PRK10789 483 DGRTEHQILHNLRQWGEGR--TVIISAHrlsALTEASEI----LVMQHGHIAQRGNHDQLA 537
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-188 |
2.19e-14 |
|
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: 67.86 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgedhtltppsrrpvsmlfqENNLFSHLnvqqniglgln 97
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------STVKIGYF----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 98 pgltlnaSQrekrdaiarqmgieslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPalrqEMLTLVSDICR 177
Cdd:cd03221 69 -------EQ-----------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL----ESIEALEEALK 114
|
170
....*....|.
gi 877977460 178 ERQLTLLMVSH 188
Cdd:cd03221 115 EYPGTVILVSH 125
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
2.93e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.82 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPM--RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhtltppSRRPVSMLFQ 78
Cdd:PRK13540 1 MLDVIELDFDYHDQPLlqQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS------IKKDLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 79 ENNLFSHLNvqqniglGLNPGLTLN---------ASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQP 149
Cdd:PRK13540 75 QLCFVGHRS-------GINPYLTLRenclydihfSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 877977460 150 VLLLDEPFSALDpalRQEMLTLVSDICRERQL--TLLMVSH 188
Cdd:PRK13540 148 LWLLDEPLVALD---ELSLLTIITKIQEHRAKggAVLLTSH 185
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-224 |
5.43e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT---LTPpSRRPVSMLFQENNLFShlnvqQNIGL 94
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfgLTD-LRRVLSIIPQSPVLFS-----GTVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 GLNP-------GLTLNASQREKRDAIARQ-MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDpaLRQ 166
Cdd:PLN03232 1329 NIDPfsehndaDLWEALERAHIKDVIDRNpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD--VRT 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 167 EmlTLVSDICRE--RQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQASA 224
Cdd:PLN03232 1407 D--SLIQRTIREefKSCTMLVIAHrlnTIIDCDKI----LVLSSGQVLEYDSPQELLSRDTSA 1463
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-219 |
6.59e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFL----APASGTLLIAGED-HTLTPPSRRP-----VSMLFQENnlFSHL 86
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDlQRISEKERRNlvgaeVAMIFQDP--MTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 87 NVQQNIGLGLNPGLTLN-----ASQREKRDAIARQMGIESLMARL---PGELSGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHqggnkKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 159 ALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-188 |
9.72e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLapasgtlliagedhtltppSRRPVSMLF--QENNLFSHLNVQQNIGL 94
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-------------------KGTPVAGCVdvPDNQFGREASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 95 GLNPGltlnasqrekrDAIAR--QMGIES--LMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:COG2401 109 KGDFK-----------DAVELlnAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170
....*....|....*...
gi 877977460 171 LVSDICRERQLTLLMVSH 188
Cdd:COG2401 178 NLQKLARRAGITLVVATH 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-219 |
1.15e-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: 70.04 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 1 MLKLIDITWLYHHLPM----RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhTLTPPSRRPVSML 76
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpavdRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS-ILTNISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 77 F--QENNLFSHLNVQQNIGLGLNpgltLNASQREKRDAIA----RQMGIESLMARLPGELSGGQRQRVALARCLVREQPV 150
Cdd:TIGR01257 2016 YcpQFDAIDDLLTGREHLYLYAR----LRGVPAEEIEKVAnwsiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 151 LLLDEPFSALDPALRQEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-228 |
1.23e-13 |
|
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: 68.34 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhtltppsrrpVSMLFQennlFSHL---NVQQNIGLGL 96
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQ----FSWImpgTIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 npgltlnaSQREKR-DAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPAL 164
Cdd:cd03291 123 --------SYDEYRyKSVVKACQLEEDITKFPekdntvlGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 165 RQEMLTlvSDICR-ERQLTLLMVSHSVEDaARIAPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:cd03291 195 EKEIFE--SCVCKlMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-212 |
1.36e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.78 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLA--PASGTLLIAGEDHTLTPP---SRRPVSMLFQ---Ennlfshlnvqqn 91
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPderARAGIFLAFQypvE------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IglglnPGLT--------LNASQREKRDAIARQMGIESLMARL------------PGeLSGGQRQRVALARCLVREQPVL 151
Cdd:COG0396 89 I-----PGVSvsnflrtaLNARRGEELSAREFLKLLKEKMKELgldedfldryvnEG-FSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 152 LLDEPFSALD-PALRqemltLVSDIC---RERQLTLLMVSHSvedaAR----IAP-RSIVVADGRIAWQG 212
Cdd:COG0396 163 ILDETDSGLDiDALR-----IVAEGVnklRSPDRGILIITHY----QRildyIKPdFVHVLVDGRIVKSG 223
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-188 |
1.37e-13 |
|
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: 67.78 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 12 HHLPMrftlaVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGtlliageDHTlTPPSRRPVSMLFQENNL---FSHL-- 86
Cdd:cd03236 18 HRLPV-----PREGQVLGLVGPNGIGKSTALKILAGKLKPNLG-------KFD-DPPDWDEILDEFRGSELqnyFTKLle 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 87 -----------------NVQQNIGLGLNpgltlNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQP 149
Cdd:cd03236 85 gdvkvivkpqyvdlipkAVKGKVGELLK-----KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 877977460 150 VLLLDEPFSALDPALRQEMLTLVSDICRERQlTLLMVSH 188
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEH 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-178 |
1.97e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 21 AVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGtlliageDHTlTPPSRRPVSMLFQENNLFSHLN--VQQNIGLGLNP 98
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLG-------DYE-EEPSWDEVLKRFRGTELQNYFKklYNGEIKVVHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 -----------G----LTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDpa 163
Cdd:PRK13409 167 qyvdlipkvfkGkvreLLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-- 244
|
170
....*....|....*
gi 877977460 164 LRQEMltLVSDICRE 178
Cdd:PRK13409 245 IRQRL--NVARLIRE 257
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-212 |
2.26e-13 |
|
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: 66.40 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLA--PASGTLLIAGEDHTLTPP---SRRPVSMLFQENNLFshlnvqqni 92
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPeerARLGIFLAFQYPPEI--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 glglnPGLTLNASQREKRDAiarqmgieslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALD-PALRqemltL 171
Cdd:cd03217 90 -----PGVKNADFLRYVNEG-----------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDiDALR-----L 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 877977460 172 VSDIC---RERQLTLLMVSHSVEDAARIAP-RSIVVADGRIAWQG 212
Cdd:cd03217 143 VAEVInklREEGKSVLIITHYQRLLDYIKPdRVHVLYDGRIVKSG 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-217 |
3.47e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKS----TLLNLI--AGFLAPASGTLL-------IAGEDHTLTPPSR---RPVSMLFQENnl 82
Cdd:PRK10261 36 SFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLrrrsrqvIELSEQSAAQMRHvrgADMAMIFQEP-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 83 FSHLNVQQNIGLGLNPGLTLN-ASQREKRDAIARQM-------GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLD 154
Cdd:PRK10261 114 MTSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMldqvripEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 155 EPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-191 |
4.62e-13 |
|
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: 65.82 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASG------TLLIAGEDHTLTPPSRRPVSMLFQENNLFShLNVQQNI 92
Cdd:cd03290 21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLN-ATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGlNPgltLNaSQREKR--DAIARQMGIESL-------MARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPA 163
Cdd:cd03290 100 TFG-SP---FN-KQRYKAvtDACSLQPDIDLLpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180
....*....|....*....|....*....
gi 877977460 164 LRQEMLTL-VSDICRERQLTLLMVSHSVE 191
Cdd:cd03290 175 LSDHLMQEgILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-209 |
4.97e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPP-------------SRRpvsmlfqENNLFSH 85
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayiteSRR-------DNGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 86 LNVQQNIGL-------GLNPGLTLNASQREKRDAIARQ--MGIE-SLMARLPGELSGGQRQRVALARCLVREQPVLLLDE 155
Cdd:PRK09700 356 FSIAQNMAIsrslkdgGYKGAMGLFHEVDEQRTAENQRelLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 877977460 156 PFSALDPALRQEMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIA 209
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLT 488
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-160 |
7.19e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPP--SRRP-VSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPksSQEAgIGIIHQELNLIPQLTIAENIFLG 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 96 LNP----GLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:PRK10762 104 REFvnrfGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-219 |
8.94e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.96 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLliageDHTLTPPSR-------RPVSMLFQENN--LFShlNVQQ 90
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER-----QSQFSHITRlsfeqlqKLVSDEWQRNNtdMLS--PGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 91 NIGLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK10938 97 DTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 877977460 171 LVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK10938 177 LLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
99-217 |
1.01e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 66.30 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 GLTLNASQREKR---DAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:NF000106 111 GR*LDLSRKDARaraDELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM 190
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 877977460 176 CRERQlTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDEL 217
Cdd:NF000106 191 VRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-219 |
1.25e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.98 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFlapASGTLLIAGEDH--------TLTPPSRRP-----VSMLFQENNlf 83
Cdd:PRK15093 25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMrfddidllRLSPRERRKlvghnVSMIFQEPQ-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 84 SHLNVQQNIGLGLN---PGLTLNAS--QR---EKRDAIA--RQMGIE---SLMARLPGELSGGQRQRVALARCLVREQPV 150
Cdd:PRK15093 100 SCLDPSERVGRQLMqniPGWTYKGRwwQRfgwRKRRAIEllHRVGIKdhkDAMRSFPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 151 LLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-161 |
1.29e-12 |
|
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: 66.50 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgedhtltpPSRRpVSMLFQENNLFSHLNVQQNIGLGLNPGL---- 100
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ--------PGIK-VGYLPQEPQLDPTKTVRENVEEGVAEIKdald 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 101 -----------------TLNASQREKRDAIA--------RQMGIESLMARLP------GELSGGQRQRVALARCLVREQP 149
Cdd:TIGR03719 102 rfneisakyaepdadfdKLAAEQAELQEIIDaadawdldSQLEIAMDALRCPpwdadvTKLSGGERRRVALCRLLLSKPD 181
|
170
....*....|..
gi 877977460 150 VLLLDEPFSALD 161
Cdd:TIGR03719 182 MLLLDEPTNHLD 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-227 |
2.19e-12 |
|
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: 65.62 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAG-FLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQE---NNLFSHLNVQQN 91
Cdd:TIGR02633 280 SFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILGVGKN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IGLGlnpglTLNA-SQREKRDAIARQMGIESLMARLP----------GELSGGQRQRVALARCLVREQPVLLLDEPFSAL 160
Cdd:TIGR02633 360 ITLS-----VLKSfCFKMRIDAAAELQIIGSAIQRLKvktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 161 DPALRQEMLTLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASAL 227
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAAAL 500
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-188 |
2.27e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGT------LLIAGEDH---TLTPPSrrpvsmlfqennlfshlNV 88
Cdd:PRK11147 338 FSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihcgtkLEVAYFDQhraELDPEK-----------------TV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 89 QQNIGLGlNPGLTLNASQRE------------KRdaiarqmgieslmARLPGE-LSGGQRQRVALARCLVREQPVLLLDE 155
Cdd:PRK11147 401 MDNLAEG-KQEVMVNGRPRHvlgylqdflfhpKR-------------AMTPVKaLSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|...
gi 877977460 156 PFSALDpalrQEMLTLVSDICRERQLTLLMVSH 188
Cdd:PRK11147 467 PTNDLD----VETLELLEELLDSYQGTVLLVSH 495
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
15-188 |
2.49e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.76 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 15 PMRFTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHLNVQQni 92
Cdd:PRK10522 341 PINLTI--KRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDFHLFDQLLGPE-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGLTLNASQR-EKRDAIARQMGIESLMarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTL 171
Cdd:PRK10522 417 GKPANPALVEKWLERlKMAHKLELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV 491
|
170
....*....|....*..
gi 877977460 172 VSDICRERQLTLLMVSH 188
Cdd:PRK10522 492 LLPLLQEMGKTIFAISH 508
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-175 |
3.47e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 22 VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdHTLTPPSRRPVSMLFQENNLFSHLNVQQNigLGLNPGLT 101
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-TATRGDRSRFMAYLGHLPGLKADLSTLEN--LHFLCGLH 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 102 LNASQREKRDAIArQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPalrqEMLTLVSDI 175
Cdd:PRK13543 111 GRRAKQMPGSALA-IVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGITLVNRM 179
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-219 |
4.23e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.54 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAP----ASGTLLIAGEDHT-LTPPSRRPV-----SMLFQENNlfSHL 86
Cdd:COG4170 25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLkLSPRERRKIigreiAMIFQEPS--SCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 87 NVQQNIGLGLN---PGLTLNAS--QR---EKRDAIA--RQMGI---ESLMARLPGELSGGQRQRVALARCLVReQPVLLL 153
Cdd:COG4170 103 DPSAKIGDQLIeaiPSWTFKGKwwQRfkwRKKRAIEllHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAIAN-QPRLLI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 154 -DEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:COG4170 182 aDEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
70-221 |
4.86e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 70 RRPVSMLFQENNLFShLNVQQNIGLGLNpgltlNASqREKRDAIARQMGIESLMARLPGE-----------LSGGQRQRV 138
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFN-MSIYENIKFGKE-----DAT-REDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRI 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 139 ALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMVSHSVEDAARiaPRSIVVADGR------IAWQG 212
Cdd:PTZ00265 1368 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR--SDKIVVFNNPdrtgsfVQAHG 1445
|
....*....
gi 877977460 213 KTDELLSGQ 221
Cdd:PTZ00265 1446 THEELLSVQ 1454
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-209 |
6.37e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.50 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 27 QVAILGPSGAGKSTLLNLIAGFLAPASGTLLiagedhtLTPPSRRPVsmlfqennlFSHLNVqQNIGLGLNPGLTLN--- 103
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTVF-------RSAKVRMAV---------FSQHHV-DGLDLSSNPLLYMMrcf 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 104 -ASQREKRDAIARQMGIESLMARLPG-ELSGGQRQRVALARCLVREQPVLLLDEPFSALD----PALRQEMLTLvsdicr 177
Cdd:PLN03073 600 pGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDldavEALIQGLVLF------ 673
|
170 180 190
....*....|....*....|....*....|..
gi 877977460 178 erQLTLLMVSHSVEDAARIAPRSIVVADGRIA 209
Cdd:PLN03073 674 --QGGVLMVSHDEHLISGSVDELWVVSEGKVT 703
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-219 |
9.08e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgedhtltppsRRPVSMLFQENNLFShLNVQQNIGLGLnpg 99
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVI----------RGTVAYVPQVSWIFN-ATVRDNILFGS--- 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 lTLNASQREKR-DAIARQMGIESLmarlPG-----------ELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:PLN03130 704 -PFDPERYERAiDVTALQHDLDLL----PGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQ 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 168 mltlVSDICRERQL---TLLMVS---HSVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:PLN03130 779 ----VFDKCIKDELrgkTRVLVTnqlHFLSQVDRI----ILVHEGMIKEEGTYEELSN 828
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-161 |
9.45e-12 |
|
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: 63.80 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIaGEDHTLT--PPSRrpvsmlfqeNNLFSHLNVQQNIGL 94
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAyvDQSR---------DALDPNKTVWEEISG 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 95 GLNPgLTLNASQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:TIGR03719 410 GLDI-IKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-228 |
1.21e-11 |
|
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: 63.78 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDhTLTPPSRRPVSMLFQENNLFshlnvqqniglglnp 98
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI-SFSPQTSWIMPGTIKDNIIF--------------- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 GLTLNasqrEKR-DAIARQMGIESLMARLP-------GE----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:TIGR01271 510 GLSYD----EYRyTSVIKACQLEEDIALFPekdktvlGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 877977460 167 EMLTlvSDICR-ERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:TIGR01271 586 EIFE--SCLCKlMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-228 |
1.24e-11 |
|
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: 63.81 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdHTLTPPSRRPVSMLFQENNLFSH-LN---VQQNI-G 93
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQAWIQNDSLRENILFGKaLNekyYQQVLeA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGLNPGLTLNASQreKRDAIARQmGIEslmarlpgeLSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVs 173
Cdd:TIGR00957 737 CALLPDLEILPSG--DRTEIGEK-GVN---------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV- 803
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 174 dICRERQL---TLLMVSHSVEdaarIAPRS---IVVADGRIAWQGKTDELLSGQASASALL 228
Cdd:TIGR00957 804 -IGPEGVLknkTRILVTHGIS----YLPQVdviIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-188 |
1.39e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLiagedhtlTPPSRRpVSMLFQENNLFSHLNVQQNIGLGLNP 98
Cdd:PRK09544 24 SLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR-IGYVPQKLYLDTTLPLTVNRFLRLRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 GLtlnasqrEKRD---AIARQMGIESLMARLPgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDI 175
Cdd:PRK09544 95 GT-------KKEDilpALKRVQAGHLIDAPMQ-KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
|
170
....*....|...
gi 877977460 176 CRERQLTLLMVSH 188
Cdd:PRK09544 167 RRELDCAVLMVSH 179
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-212 |
1.96e-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: 61.12 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPA---SGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQnig 93
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPyKEFAEKYPGEIIYVSEEDVHFPTLTVRE--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 lglnpglTLNASQREKRDAIARqmGIeslmarlpgelSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVS 173
Cdd:cd03233 103 -------TLDFALRCKGNEFVR--GI-----------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 877977460 174 DICRERQLTLLM-VSHSVEDAARIAPRSIVVADGRIAWQG 212
Cdd:cd03233 163 TMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
25-161 |
2.75e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGtlliageDHTLTPPSRrpVSMLFQENNLFSHLNVQQNIGLGLnpGLTLNA 104
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIK--VGYLPQEPQLDPEKTVRENVEEGV--AEVKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 105 SQR------------EKRDAIARQMG-----IESL----------MA----RLP------GELSGGQRQRVALARCLVRE 147
Cdd:PRK11819 102 LDRfneiyaayaepdADFDALAAEQGelqeiIDAAdawdldsqleIAmdalRCPpwdakvTKLSGGERRRVALCRLLLEK 181
|
170
....*....|....
gi 877977460 148 QPVLLLDEPFSALD 161
Cdd:PRK11819 182 PDMLLLDEPTNHLD 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-207 |
4.62e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED---HTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLG 95
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENGISMVHQELNLVLQRSVMDNMWLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 LNPGLTLNASQREK-RD--AIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLV 172
Cdd:PRK10982 98 RYPTKGMFVDQDKMyRDtkAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTII 177
|
170 180 190
....*....|....*....|....*....|....*
gi 877977460 173 SDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:PRK10982 178 RKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-208 |
4.68e-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: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT-LTPPSRRPVSMLF-----QENNLFSHLNVQQN 91
Cdd:COG3845 277 VSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITgLSPRERRRLGVAYipedrLGRGLVPDMSVAEN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IGLG------LNPGLTLNasqREKRDAIARQMgIESLMARLPGE------LSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:COG3845 357 LILGryrrppFSRGGFLD---RKAIRAFAEEL-IEEFDVRTPGPdtparsLSGGNQQKVILARELSRDPKLLIAAQPTRG 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 877977460 160 LDP----ALRQEMLTLvsdicRERQLTLLMVSHSVEDAARIAPRSIVVADGRI 208
Cdd:COG3845 433 LDVgaieFIHQRLLEL-----RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-209 |
7.01e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT-LTP-----------PSRRPVSMLFQENNLfsHL 86
Cdd:PRK15439 283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINaLSTaqrlarglvylPEDRQSSGLYLDAPL--AW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 87 NV----QQNIGLGLNPGltlnasqREKR--DAIARQMGIESLMARLP-GELSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:PRK15439 361 NVcaltHNRRGFWIKPA-------RENAvlERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 160 LDPALRQEMLTLVSDICrERQLTLLMVSHSVEDAARIAPRSIVVADGRIA 209
Cdd:PRK15439 434 VDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-207 |
8.49e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPA---SGTLLIAGED---HTLTPPSRRPVSMLFQENNLFSHLNVQQNI 92
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVcrfKDIRDSEALGIVIIHQELALIPYLSIAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPG----LTLNASQREKRDAIARqMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEM 168
Cdd:NF040905 100 FLGNERAkrgvIDWNETNRRARELLAK-VGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAAL 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 877977460 169 LTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGR 207
Cdd:NF040905 179 LDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-221 |
9.37e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.89 E-value: 9.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 28 VAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGedHTLTPPS----RRPVSMLFQENNLFSHlNVQQNIGLG--LNPGLT 101
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG--RPLSSLShsvlRQGVAMVQQDPVVLAD-TFLANVTLGrdISEEQV 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 102 LNASQREKRDAIARQM--GIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ---EMLTLVsdic 176
Cdd:PRK10790 447 WQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQaiqQALAAV---- 522
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 877977460 177 rERQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQ 221
Cdd:PRK10790 523 -REHTTLVVIAHrlsTIVEADTI----LVLHRGQAVEQGTHQQLLAAQ 565
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
24-202 |
2.07e-10 |
|
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: 57.38 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 24 RGEQVAILGPSGAGKSTLLNLIAGFLAPASGT-LLIAGEDHTLTPPSRRpvsmlfqennlfshlnvqqniglglnpgltl 102
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQL------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 103 nasqrekrdaiarqmgIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSD-----ICR 177
Cdd:smart00382 50 ----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKS 113
|
170 180
....*....|....*....|....*
gi 877977460 178 ERQLTLLMVSHSVEDAARIAPRSIV 202
Cdd:smart00382 114 EKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-161 |
2.44e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 4 LIDIT--WL---YHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE----------------- 61
Cdd:PRK11147 3 LISIHgaWLsfsDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprnvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 62 -----------------------DHTLTPPSRRPVSMLFQENNLFSHLN-------VQQNIG-LGLNPGLTLNasqrekr 110
Cdd:PRK11147 83 vydfvaegieeqaeylkryhdisHLVETDPSEKNLNELAKLQEQLDHHNlwqlenrINEVLAqLGLDPDAALS------- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 111 daiarqmgieslmarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK11147 156 ------------------SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-224 |
3.98e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 26 EQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHT---LTPpSRRPVSMLFQENNLFShlnvqQNIGLGLNPGLTL 102
Cdd:PLN03130 1266 EKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfgLMD-LRKVLGIIPQAPVLFS-----GTVRFNLDPFNEH 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 103 N------ASQREK-RDAIARQ-MGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD---PALRQEMLtl 171
Cdd:PLN03130 1340 NdadlweSLERAHlKDVIRRNsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrtDALIQKTI-- 1417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 172 vsdicRE--RQLTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLSGQASA 224
Cdd:PLN03130 1418 -----REefKSCTMLIIAHrlnTIIDCDRI----LVLDAGRVVEFDTPENLLSNEGSA 1466
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-217 |
4.80e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgedhtltppsRRPVSMLFQENNLFShLNVQQNIGLGLNpg 99
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI----------RGSVAYVPQVSWIFN-ATVRENILFGSD-- 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 100 ltlNASQREKR--DAIARQMGIESLMARLPGEL-------SGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEmlt 170
Cdd:PLN03232 705 ---FESERYWRaiDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ--- 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 877977460 171 lVSDICRERQL---TLLMVSHSVEDAARIaPRSIVVADGRIAWQGKTDEL 217
Cdd:PLN03232 779 -VFDSCMKDELkgkTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-219 |
8.89e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.98 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 3 KLIDITW-----LYHHLPMRFTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhtltppsrrpVSMLF 77
Cdd:PRK13545 23 KLKDLFFrskdgEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 78 QENNLFSHLNVQQNIGL-GLNPGLTlnasqREKRDAIARQM----GIESLMARLPGELSGGQRQRVALARCLVREQPVLL 152
Cdd:PRK13545 92 ISSGLNGQLTGIENIELkGLMMGLT-----KEKIKEIIPEIiefaDIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 153 LDEPFSALDPALRQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLS 219
Cdd:PRK13545 167 IDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-219 |
1.71e-09 |
|
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: 57.65 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFShlnvqQNI 92
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakiglHDL----RFKITIIPQDPVLFS-----GSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPgltlnASQREKRDA-IARQMG-IESLMARLP----------GE-LSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:TIGR00957 1377 RMNLDP-----FSQYSDEEVwWALELAhLKTFVSALPdkldhecaegGEnLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 160 LD---PALRQEMLTLVSDICrerqlTLLMVSH---SVEDAARIaprsIVVADGRIAWQGKTDELLS 219
Cdd:TIGR00957 1452 VDletDNLIQSTIRTQFEDC-----TVLTIAHrlnTIMDYTRV----IVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-161 |
2.32e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAveRGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIaGEDhtltppsrrpVSMLFQE---NNLFSHLNVQQNIGL 94
Cdd:PRK11819 345 FSLP--PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GET----------VKLAYVDqsrDALDPNKTVWEEISG 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 95 GLNpglTLNASQRE--KRDAIAR--------QmgieslmaRLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PRK11819 412 GLD---IIKVGNREipSRAYVGRfnfkggdqQ--------KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-227 |
2.49e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 21 AVERGEQVAILGPSGAGKSTLLNLIAG-FLAPASGTLLIAGEDHTLTPPS---RRPVSMLFQE---NNLFSHLNVQQNIG 93
Cdd:PRK13549 284 SLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPQqaiAQGIAMVPEDrkrDGIVPVMGVGKNIT 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 94 LGlnpglTLNASQREKR-DAIARQMGIESLMARLP----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDP 162
Cdd:PRK13549 364 LA-----ALDRFTGGSRiDDAAELKTILESIQRLKvktaspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 163 ALRQEMLTLVSDICRErQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELLSGQASASAL 227
Cdd:PRK13549 439 GAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQVMEAAL 502
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-155 |
2.51e-09 |
|
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: 56.73 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 2 LKLIDITWLYHHL--PMRFT-----LAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhTLTPPS----R 70
Cdd:COG4615 328 LELRGVTYRYPGEdgDEGFTlgpidLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ--PVTADNreayR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 71 RPVSMLFQENNLFSHLnvqqnigLGLnpgltlnasQREKRDAIARQmgiesLMARL--------------PGELSGGQRQ 136
Cdd:COG4615 406 QLFSAVFSDFHLFDRL-------LGL---------DGEADPARARE-----LLERLeldhkvsvedgrfsTTDLSQGQRK 464
|
170
....*....|....*....
gi 877977460 137 RVALARCLVREQPVLLLDE 155
Cdd:COG4615 465 RLALLVALLEDRPILVFDE 483
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-222 |
4.53e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIA--------GEDHTltppsrrpvSMLFQENNLFSHLnvq 89
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenanigyyAQDHA---------YDFENDLTLFDWM--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 qniglglnpgltlnaSQ--REKRDaiaRQMgIESLMARL----------PGELSGGQRQRVALARCLVREQPVLLLDEP- 156
Cdd:PRK15064 406 ---------------SQwrQEGDD---EQA-VRGTLGRLlfsqddikksVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPt 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 877977460 157 -------FSALDPALrqEMLtlvsdicrerQLTLLMVSHSVEDAARIAPRSI-VVADGRIAWQGKTDELLSGQA 222
Cdd:PRK15064 467 nhmdmesIESLNMAL--EKY----------EGTLIFVSHDREFVSSLATRIIeITPDGVVDFSGTYEEYLRSQG 528
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
22-203 |
1.11e-08 |
|
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: 52.96 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 22 VERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTlliagEDHTLTPPSRRPvsmlfqennlfshlnvqQNIglglnpglt 101
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-----DEWDGITPVYKP-----------------QYI--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 102 lnasqrekrdaiarqmgieslmarlpgELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQL 181
Cdd:cd03222 71 ---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|..
gi 877977460 182 TLLMVSHSVEDAARIAPRSIVV 203
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVF 145
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-188 |
1.58e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.37 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 17 RFTLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPASGTlliagedhTLTPPSrrpvsmlfqENNLFsHLNVQQNIGLG- 95
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGG--------RLTKPA---------KGKLF-YVPQRPYMTLGt 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 96 -----LNPGLTLNASQREKRDA--------------IARQMGIESlMARLPGELSGGQRQRVALARCLVREQPVLLLDEP 156
Cdd:TIGR00954 531 lrdqiIYPDSSEDMKRRGLSDKdleqildnvqlthiLEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 877977460 157 FSALDPALRQEMLTLvsdiCRERQLTLLMVSH 188
Cdd:TIGR00954 610 TSAVSVDVEGYMYRL----CREFGITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-161 |
2.08e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 16 MRFTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIaGEDHTLTPPS----RRPVSMLFQENNLFSHlNVQQN 91
Cdd:PTZ00265 404 LNFTL--TEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII-NDSHNLKDINlkwwRSKIGVVSQDPLLFSN-SIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 92 IGLGL--------------------NPGLTLNASQREK---------------------------RDA----IARQMGIE 120
Cdd:PTZ00265 480 IKYSLyslkdlealsnyynedgndsQENKNKRNSCRAKcagdlndmsnttdsneliemrknyqtiKDSevvdVSKKVLIH 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 877977460 121 SLMARLP-----------GELSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:PTZ00265 560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-191 |
6.86e-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: 52.61 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGfLAPASGTLLIAGE--DHTLTPPSRRPVSMLFQENNLFSHlNVQQNiglgL 96
Cdd:TIGR01271 1239 SFSVEGGQRVGLLGRTGSGKSTLLSALLR-LLSTEGEIQIDGVswNSVTLQTWRKAFGVIPQKVFIFSG-TFRKN----L 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTLNASQREKrdaIARQMGIESLMARLPGEL-----------SGGQRQRVALARCLVREQPVLLLDEPFSALDPA-- 163
Cdd:TIGR01271 1313 DPYEQWSDEEIWK---VAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVtl 1389
|
170 180 190
....*....|....*....|....*....|
gi 877977460 164 --LRQEMLTLVSDiCrerqlTLLMVSHSVE 191
Cdd:TIGR01271 1390 qiIRKTLKQSFSN-C-----TVILSEHRVE 1413
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-228 |
7.68e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 18 FTLavERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEDHTLTPPS-------------RRP----VSMLFQEN 80
Cdd:PRK10762 273 FTL--RKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivyisedRKRdglvLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 81 NLFSHLNVQQNIGLGLNpgltlNASQREKRDAIARQMGIES-LMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSA 159
Cdd:PRK10762 351 MSLTALRYFSRAGGSLK-----HADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 877977460 160 LDPALRQEMLTLVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIawqgkTDELLSGQASASALL 228
Cdd:PRK10762 426 VDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI-----SGEFTREQATQEKLM 488
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
25-233 |
7.83e-08 |
|
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: 51.45 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFShlnvqQNIGLGLNP 98
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDisklplHTL----RSRLSIILQDPILFS-----GSIRFNLDP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 GLTLNASQREKRDAIARqmgIESLMARLPGEL-----------SGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQE 167
Cdd:cd03288 118 ECKCTDDRLWEALEIAQ---LKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 168 MLTLVSDICRERQ-LTLLMVSHSVEDAARIaprsIVVADGRIAWQGKTDELLSGQASASALLgIKSH 233
Cdd:cd03288 195 LQKVVMTAFADRTvVTIAHRVSTILDADLV----LVLSRGILVECDTPENLLAQEDGVFASL-VRTD 256
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-216 |
1.22e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIA----GFLAPASGTLLIAGED-HTLTPPSRRPVSMLFQENNLFSHLNVQQNI------- 92
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITpEEIKKHYRGDVVYNAETDVHFPHLTVGETLdfaarck 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNP-GLTLNASQREKRDAIARQMGIESLMARLPGE-----LSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:TIGR00956 167 TPQNRPdGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAL 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 167 EMLTLVSDICRERQLTLLM-VSHSVEDAARIAPRSIVVADGRIAWQGKTDE 216
Cdd:TIGR00956 247 EFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFGPADK 297
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-191 |
1.83e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 24 RGEQVAILGPSGAGKSTLLNliAGFlaPASGTLLIAGedhTLTPPSRRPVSMLFQENNLFshlnvqqNIGLGLnpgLTLN 103
Cdd:cd03238 20 LNVLVVVTGVSGSGKSTLVN--EGL--YASGKARLIS---FLPKFSRNKLIFIDQLQFLI-------DVGLGY---LTLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 104 asqrekrdaiarqmgieslmaRLPGELSGGQRQRVALARCLVREQP--VLLLDEPFSALDPalrQEMLTLVSDICRERQL 181
Cdd:cd03238 83 ---------------------QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ---QDINQLLEVIKGLIDL 138
|
170
....*....|..
gi 877977460 182 --TLLMVSHSVE 191
Cdd:cd03238 139 gnTVILIEHNLD 150
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-212 |
1.91e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLiagedhtltppSRRPVSMLFQENNLFShLNVQQNIgLGLNP 98
Cdd:PTZ00243 680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQAWIMN-ATVRGNI-LFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 gltlnasQREKR--DAIaRQMGIESLMARLPG-----------ELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:PTZ00243 747 -------EDAARlaDAV-RVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 877977460 166 QEmltLVSDIC--RERQLTLLMVSHSVEDAARiAPRSIVVADGRIAWQG 212
Cdd:PTZ00243 819 ER---VVEECFlgALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSG 863
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-161 |
2.12e-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: 49.55 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 21 AVERGEQVAILGPSGAGKSTLLNLIAG--FLAPASGTLLIAGedhtltppsrRPVSMLFQENNLFSHlnvQQNIglgLNP 98
Cdd:cd03232 29 YVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILING----------RPLDKNFQRSTGYVE---QQDV---HSP 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 877977460 99 GLTLnasqrekrdaiarqmgIESLM--ARLPGeLSGGQRQRVALARCLVREQPVLLLDEPFSALD 161
Cdd:cd03232 93 NLTV----------------REALRfsALLRG-LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-166 |
2.24e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.24 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLApASGTLLIAGEDHTLTPPS--RRPVSMLFQENNLFSHlNVQQNiglgL 96
Cdd:cd03289 24 SFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQkwRKAFGVIPQKVFIFSG-TFRKN----L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 97 NPGLTLNASQREKrdaIARQMGIESLMARLPGEL-----------SGGQRQRVALARCLVREQPVLLLDEPFSALDPALR 165
Cdd:cd03289 98 DPYGKWSDEEIWK---VAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
.
gi 877977460 166 Q 166
Cdd:cd03289 175 Q 175
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-194 |
2.88e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 29 AILGPSGAGKSTLLNLI--AGF-LAPASGTLLIAGEDHTLTPPSRRPVSMLFQENNlfshlnvqqniglglnpGLTLNAS 105
Cdd:cd03240 26 LIVGQNGAGKTTIIEALkyALTgELPPNSKGGAHDPKLIREGEVRAQVKLAFENAN-----------------GKKYTIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 106 QREK--RDAI-ARQMGIESLMARLPGELSGGQRQ------RVALARCLVREQPVLLLDEPFSALDPA-LRQEMLTLVSDI 175
Cdd:cd03240 89 RSLAilENVIfCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEER 168
|
170 180
....*....|....*....|.
gi 877977460 176 CRERQLTLLMVSH--SVEDAA 194
Cdd:cd03240 169 KSQKNFQLIVITHdeELVDAA 189
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-209 |
3.65e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 24 RGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE---DHTLTPPSRRPVSMLFQE---NNLFSHLNVQ-----QNI 92
Cdd:PRK10982 273 KGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinNHNANEAINHGFALVTEErrsTGIYAYLDIGfnsliSNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPgLTLNASQREKRDAiarQMGIESLMARLP------GELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQ 166
Cdd:PRK10982 353 RNYKNK-VGLLDNSRMKSDT---QWVIDSMRVKTPghrtqiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKF 428
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 877977460 167 EMLTLVSDICRERQlTLLMVSHSVEDAARIAPRSIVVADGRIA 209
Cdd:PRK10982 429 EIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-217 |
1.59e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGED------HTLtppsRRPVSMLFQENNLFSHlNVQQNiglgLNP 98
Cdd:PTZ00243 1336 REKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigayglREL----RRQFSMIPQDPVLFDG-TVRQN----VDP 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 glTLNASQRE---------KRDAIARQM-GIESLMARLPGELSGGQRQRVALARCLV-REQPVLLLDEPFSALDPAL-RQ 166
Cdd:PTZ00243 1407 --FLEASSAEvwaalelvgLRERVASESeGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALdRQ 1484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 877977460 167 EMLTLVSDICRERQLTLLMVSHSVEDAARIaprsIVVADGRIAWQGKTDEL 217
Cdd:PTZ00243 1485 IQATVMSAFSAYTVITIAHRLHTVAQYDKI----IVMDHGAVAEMGSPREL 1531
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-218 |
1.38e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGEdhtltppsrrpVSMLFQENNLFSHLNVQQNIGLGLnp 98
Cdd:PRK13546 44 SLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIEFKM-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 99 gLTLNASQREKRDAIARQMGIESLmarlpGEL--------SGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLT 170
Cdd:PRK13546 111 -LCMGFKRKEIKAMTPKIIEFSEL-----GEFiyqpvkkySSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 877977460 171 LVSDIcRERQLTLLMVSHSVEDAARIAPRSIVVADGRIAWQGKTDELL 218
Cdd:PRK13546 185 KIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-188 |
2.42e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 25 GEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAgEDHTLTPPSRRPVSMLFQENNLFSHLNvqqniglglnpGLTLNA 104
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGIKLGYFAQHQLEFLRADESPLQHLA-----------RLAPQE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 105 SQREKRDAIARQMGIESLMARLPGELSGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDIcrerQLTLL 184
Cdd:PRK10636 406 LEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF----EGALV 481
|
....
gi 877977460 185 MVSH 188
Cdd:PRK10636 482 VVSH 485
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
29-202 |
2.49e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.80 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 29 AILGPSGAGKSTLLNLIagflapasgTLLIAGEdhTLTPPSRRPVSMLFQENNLFSHLNVQQNIGLGL-----NPGLTLN 103
Cdd:cd03279 32 LICGPTGAGKSTILDAI---------TYALYGK--TPRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKyrverSRGLDYD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 104 ASqreKRDAIARQMGIESLMARLPGELSGGQRQRVALARCL--------VREQPV--LLLDEPFSALDPALRQEMLTLVS 173
Cdd:cd03279 101 QF---TRIVLLPQGEFDRFLARPVSTLSGGETFLASLSLALalsevlqnRGGARLeaLFIDEGFGTLDPEALEAVATALE 177
|
170 180
....*....|....*....|....*....
gi 877977460 174 DICRERQLtLLMVSHSVEDAARIAPRSIV 202
Cdd:cd03279 178 LIRTENRM-VGVISHVEELKERIPQRLEV 205
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-71 |
3.94e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 3.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGFlaPA----SGTLLIAGEDHTLTPPSRR 71
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEPEER 81
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
24-47 |
6.46e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.39 E-value: 6.46e-05
10 20
....*....|....*....|....
gi 877977460 24 RGEQVAILGPSGAGKSTLLNLIAG 47
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-218 |
1.58e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 15 PMRFTLavergeqvaILGPSGAGKSTLLNLIAGFLAPasgTLLIAGE----DHTLTPPSRRPVSMLFQENNL-FSHLNVQ 89
Cdd:PLN03140 190 PSRMTL---------LLGPPSSGKTTLLLALAGKLDP---SLKVSGEitynGYRLNEFVPRKTSAYISQNDVhVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 90 QNI-------GLGLNPGLTLNASQREKRDAIARQMGIESLMARLPGE--------------------------------L 130
Cdd:PLN03140 258 ETLdfsarcqGVGTRYDLLSELARREKDAGIFPEAEVDLFMKATAMEgvksslitdytlkilgldickdtivgdemirgI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 131 SGGQRQRVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVSDICRERQLTLLMvshsveDAARIAPRS-------IVV 203
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLM------SLLQPAPETfdlfddiILL 411
|
250
....*....|....*
gi 877977460 204 ADGRIAWQGKTDELL 218
Cdd:PLN03140 412 SEGQIVYQGPRDHIL 426
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
127-191 |
2.22e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 877977460 127 PGELSGGQRQ---RVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVsDICRERQLTLLMVSHSVE 191
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELL-KELSRNGAQLILTTHSPL 300
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-188 |
3.29e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPASGTLLIAGE-----DHTLTPPSRRP-VSMLFQENNLFSHLNVQQNI 92
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawVNQETPALPQPaLEYVIDGDREYRQLEAQLHD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 93 GLGLNPGLTLnASQREKRDAIArQMGIESLMARLPGEL--------------SGGQRQRVALARCLVREQPVLLLDEPFS 158
Cdd:PRK10636 101 ANERNDGHAI-ATIHGKLDAID-AWTIRSRAASLLHGLgfsneqlerpvsdfSGGWRMRLNLAQALICRSDLLLLDEPTN 178
|
170 180 190
....*....|....*....|....*....|....*
gi 877977460 159 ALDpalrqemltLVSDICRERQL-----TLLMVSH 188
Cdd:PRK10636 179 HLD---------LDAVIWLEKWLksyqgTLILISH 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
131-191 |
3.77e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 3.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 877977460 131 SGGQRQRVALARCLVREQPVLLLDEPFSALDpalRQEMLTLVSDICRERQlTLLMVSHSVE 191
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPK-TFIVVSHARE 402
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
27-53 |
9.27e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.98 E-value: 9.27e-04
10 20
....*....|....*....|....*..
gi 877977460 27 QVAILGPSGAGKSTLLNLIAGFLAPAS 53
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVS 27
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
24-47 |
1.33e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.29 E-value: 1.33e-03
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-194 |
1.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 1.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 877977460 130 LSGGQRQ------RVALARCLVREQPVLLLDEPFSALDPALRQEMLTLVsdicrERQL----TLLMVSHSVE--DAA 194
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIM-----ERYLrkipQVIIVSHDEElkDAA 860
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
28-175 |
1.76e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.45 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 28 VAILGPSGAGKSTLLNLIA-GFLAPASGTllIAGEDHTLTPPSRRP-VSMLFQENNLFSHLNVQQNIGLGLnpgltLNAS 105
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRyALYGKARSR--SKLRSDLINVGSEEAsVELEFEHGGKRYRIERRQGEFAEF-----LEAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 106 QREKRDAIARQMGI---ESLMARL---------------------------------PGELSGGQRQRVALARcLVReqp 149
Cdd:COG0419 99 PSERKEALKRLLGLeiyEELKERLkeleealesaleelaelqklkqeilaqlsgldpIETLSGGERLRLALAD-LLS--- 174
|
170 180
....*....|....*....|....*.
gi 877977460 150 vLLLDepFSALDPALRQEMLTLVSDI 175
Cdd:COG0419 175 -LILD--FGSLDEERLERLLDALEEL 197
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
25-47 |
2.88e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.99 E-value: 2.88e-03
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
25-47 |
4.77e-03 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 36.70 E-value: 4.77e-03
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
28-68 |
5.31e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 36.71 E-value: 5.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 877977460 28 VAILGPSGAGKSTLLNLIAGFLAPASGtLLIA-----------GEDH-TLTPP 68
Cdd:COG3709 8 IYVVGPSGAGKDSLLAAARARLAADPR-LVFArryitrpadagGEDHdALSEA 59
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
30-47 |
5.42e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.11 E-value: 5.42e-03
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
28-46 |
5.54e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 37.62 E-value: 5.54e-03
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-53 |
5.72e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 5.72e-03
10 20 30
....*....|....*....|....*....|....*
gi 877977460 19 TLAVERGEQVAILGPSGAGKSTLLNLIAGFLAPAS 53
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-161 |
6.70e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 36.69 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 20 LAVERGEQVAILGPSGAGKSTLLNLIAGF--LAPASGTLLIAGEDHTLTPPSRRP---VSMLFQ--------ENNLFSHL 86
Cdd:PRK09580 22 LEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAgegIFMAFQypveipgvSNQFFLQT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 877977460 87 NVQQniglglnpglTLNASQREKRDAIARQMGIESLMARL--PGEL---------SGGQRQRVALARCLVREQPVLLLDE 155
Cdd:PRK09580 102 ALNA----------VRSYRGQEPLDRFDFQDLMEEKIALLkmPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDE 171
|
....*.
gi 877977460 156 PFSALD 161
Cdd:PRK09580 172 SDSGLD 177
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
129-162 |
7.41e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 36.51 E-value: 7.41e-03
10 20 30
....*....|....*....|....*....|....*...
gi 877977460 129 ELSGGQRQRVAL----ARCLVREQPVLLLDEPFSALDP 162
Cdd:cd03273 166 ELSGGQRSLVALslilALLLFKPAPMYILDEVDAALDL 203
|
|
| PRK13830 |
PRK13830 |
conjugal transfer protein TrbE; Provisional |
15-46 |
7.75e-03 |
|
conjugal transfer protein TrbE; Provisional
Pssm-ID: 237525 [Multi-domain] Cd Length: 818 Bit Score: 37.13 E-value: 7.75e-03
10 20 30
....*....|....*....|....*....|..
gi 877977460 15 PMRFTLAVERGEQVAILGPSGAGKSTLLNLIA 46
Cdd:PRK13830 446 PFRLNLHVDDVGHTLIFGPTGSGKSTLLALIA 477
|
|
|