|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-262 |
0e+00 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 533.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRTVQREGRLARD 80
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
250 260
....*....|....*....|..
gi 985002877 241 DNERFDHLYRSINRVEENAKAA 262
Cdd:PRK09984 241 DNERFDHLYRSINRVEENAKAA 262
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-251 |
1.99e-137 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 386.72 E-value: 1.99e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 3 TIIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRlaRDI 81
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTS--GE-ILVDGQDVTALRG--RAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKSRAHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
Cdd:COG3638 76 RRLRRRIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFD 241
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELT 235
|
250
....*....|
gi 985002877 242 NERFDHLYRS 251
Cdd:COG3638 236 DAVLREIYGG 245
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-250 |
2.26e-137 |
|
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: 386.27 E-value: 2.26e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSVGSHIELLGRTVQREGrlARDIR 82
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVE---PSSGSILLEGTDITKLR--GKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KSRAHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
....*...
gi 985002877 243 ERFDHLYR 250
Cdd:TIGR02315 236 EVLRHIYG 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-249 |
4.42e-129 |
|
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: 365.35 E-value: 4.42e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRTVQRegrlaRDIRK 83
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG-----KALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 SRAHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
....*.
gi 985002877 244 RFDHLY 249
Cdd:cd03256 236 VLDEIY 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-231 |
7.32e-89 |
|
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: 262.43 E-value: 7.32e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQR--EGRLA 78
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL---DRPTSGEVRVDGTDISKlsEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 79 RdIRksRAHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:cd03255 78 A-FR--RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKK--------ERRERAEELLERVGLGDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHV 231
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-231 |
1.04e-77 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 234.55 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQR--E 74
Cdd:COG1136 1 MSPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTS--GE-VLIDGQDISSlsE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 75 GRLARdIRksRAHTGYIFQQFNLVNRLSVLENVLIGAL--GSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVST 152
Cdd:COG1136 78 RELAR-LR--RRHIGFVFQFFNLLPELTALENVALPLLlaGVSR----------KERRERARELLERVGLGDRLDHRPSQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHV 231
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-250 |
2.97e-70 |
|
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: 216.45 E-value: 2.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRlaRDIRK 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSS--GE-VLLDGRDLASLSR--RELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 SRAhtgYIFQQFNLVNRLSVLENVligALGSTPfWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
Cdd:COG1120 76 RIA---YVPQEPPAPFGLTVRELV---ALGRYP-HLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FDN 242
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvLTP 228
|
....*...
gi 985002877 243 ERFDHLYR 250
Cdd:COG1120 229 ELLEEVYG 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-230 |
3.38e-70 |
|
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: 213.59 E-value: 3.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQregRLARDIRKS 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL---EEPDSGSILIDGEDLT---DLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcfswftgeqkqralqaltrvgmvhfahqrvstLSGGQQQRVAIA 164
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG------------------------------------------LSGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-250 |
6.53e-69 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 212.64 E-value: 6.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRtvqregrlarD 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTS--GT-VRLFGK----------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIFQQFNlVNR---LSVLENVLIGALGSTPFWRtcfsWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
Cdd:COG1121 70 PRRARRRIGYVPQRAE-VDWdfpITVRDVVLMGRYGRRGLFR----RPSRADREAVDEALERVGLEDLADRPIGELSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPE 223
|
250
....*....|...
gi 985002877 238 QQFDNERFDHLYR 250
Cdd:COG1121 224 EVLTPENLSRAYG 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-244 |
7.83e-69 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 212.16 E-value: 7.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRlarDIRK 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDS--GT-ITVDGEDLTDSKK---DINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 SRAHTGYIFQQFNLVNRLSVLENVLIG---ALGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
Cdd:COG1126 75 LRRKVGMVFQQFNLFPHLTVLENVTLApikVKKMSK----------AEAEERAMELLERVGLADKADAYPAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGIT-VVVTlHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTmVVVT-HEMGFAREVADRVVFMDGGRIVEEGPPEE 222
|
....*....
gi 985002877 240 F----DNER 244
Cdd:COG1126 223 FfenpQHER 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-252 |
8.49e-66 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 204.53 E-value: 8.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRLARdirks 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS--GE-VRVLGEDVARDPAEVR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 rAHTGYIFQQFNLVNRLSVLENV-LIGALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLrFFARLYGLP---------RKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
....*....
gi 985002877 244 RFDHLYRSI 252
Cdd:COG1131 222 LLEDVFLEL 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-231 |
4.08e-64 |
|
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: 199.29 E-value: 4.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQREGRlarDIRKS 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD---SGTIIIDGLKLTDDKK---NINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVLIGalgstPFWRtcFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLA-----PIKV--KGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-235 |
1.61e-61 |
|
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: 192.75 E-value: 1.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 6 RVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSVGShIELLGRtvqregrlarDIRKSR 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK--PTSGS-IRVFGK----------PLEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 86 AHTGYIFQQFNlVNR---LSVLENVLIGALGSTPFWRtcfsWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
Cdd:cd03235 68 KRIGYVPQRRS-IDRdfpISVRDVVLMGLYGHKGLFR----RLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALrQGHVFYDG 235
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-240 |
6.14e-61 |
|
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: 191.78 E-value: 6.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRlaRDIRK 83
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTS--GE-VLVDGKDITKKNL--RELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 sraHTGYIFQ----QfnLVNRlSVLENVLIG--ALGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
Cdd:COG1122 76 ---KVGLVFQnpddQ--LFAP-TVEEDVAFGpeNLGLPR----------EEIRERVEEALELVGLEHLADRPPHELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
Cdd:COG1122 140 KQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
...
gi 985002877 238 QQF 240
Cdd:COG1122 219 REV 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-235 |
2.39e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 190.26 E-value: 2.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDK--SVGShIELLGRTVQREGRlaRD 80
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLK----LLYGEErpTSGQ-VLVNGQDLSRLKR--RE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIFQQFNLVNRLSVLENVLIG--ALGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:COG2884 74 IPYLRRRIGVVFQDFRLLPDRTVYENVALPlrVTGKSR----------KEIRRRVREVLDLVGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHqvDYAL--RYCERIVALRQGHVFYDG 235
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATH--DLELvdRMPKRVLELEDGRLVRDE 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-231 |
3.24e-58 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 186.06 E-value: 3.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGR 76
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTS--GE-VLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 77 lardirksraHTGYIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfsWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGG 156
Cdd:COG1116 81 ----------DRGVVFQEPALLPWLTVLDNVALGLELRG--------VPKAERRERARELLELVGLAGFEDAYPHQLSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVV-VTlHQVDYALRYCERIVAL--RQGHV 231
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLfVT-HDVDEAVFLADRVVVLsaRPGRI 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-242 |
5.99e-58 |
|
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: 184.41 E-value: 5.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRlaRD 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS--GE-ILVDGQDITGLSE--KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIFQQFNLVNRLSVLENVligALgstPFWRtcfswFTG----EQKQRALQALTRVGMVHFAHQRVSTLSGG 156
Cdd:COG1127 77 LYELRRRIGMLFQGGALFDSLTVFENV---AF---PLRE-----HTDlseaEIRELVLEKLELVGLPGAADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
....*.
gi 985002877 237 SQQFDN 242
Cdd:COG1127 226 PEELLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-235 |
5.84e-56 |
|
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: 177.63 E-value: 5.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 6 RVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGRlardirKSR 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLL---KPSSGEILLDGKDLASLSP------KEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 86 AhtgyifqqfnlvNRLSVLenvligalgstpfwrtcfswftgeqkqraLQALTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
Cdd:cd03214 72 A------------RKIAYV-----------------------------PQALELLGLAHLADRPFNELSGGERQRVLLAR 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-242 |
1.45e-55 |
|
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: 178.46 E-value: 1.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQREGRlaRDIRKS 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSG---EVLIDGEDISGLSE--AELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVligalgstPFW-RTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENV--------AFPlREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-231 |
9.87e-55 |
|
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: 176.23 E-value: 9.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRlaR 79
Cdd:cd03258 1 MIELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTS--GS-VLVDGTDLTLLSG--K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKSRAHTGYIFQQFNLVNRLSVLENVligALgstPF--WRtcfsWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLSSRTVFENV---AL---PLeiAG----VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-239 |
1.81e-54 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 175.67 E-value: 1.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSVGSHIELLGRTVqregrlarDI 81
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLeeITSGDLIVDGLKVNDPKV--------DE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKSRAHTGYIFQQFNLVNRLSVLENVLIGAL---GSTpfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:PRK09493 73 RLIRQEAGMVFQQFYLFPHLTALENVMFGPLrvrGAS----------KEEAEKQARELLAKVGLAERAHHYPSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQ 221
|
.
gi 985002877 239 Q 239
Cdd:PRK09493 222 V 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-230 |
5.71e-54 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 173.42 E-value: 5.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQregrlARDIRKSRAHTGYIFQQFN- 96
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL---GPTSGEVLVDGKDLT-----KLSLKELRRKVGLVFQNPDd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 -LVNrLSVLENVLIGA--LGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
Cdd:cd03225 87 qFFG-PTVEEEVAFGLenLGLPE----------EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 174 ILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGH 230
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
8.51e-54 |
|
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: 174.46 E-value: 8.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGrlARD 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTS--GR-ILFDGRDITGLP--PHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IrkSRAHTGYIFQQFNLVNRLSVLENVLIGAL--GSTPFWRTCFSWFTG-----EQKQRALQALTRVGMVHFAHQRVSTL 153
Cdd:COG0411 76 I--ARLGIARTFQNPRLFPELTVLENVLVAAHarLGRGLLAALLRLPRArreerEARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
|
...
gi 985002877 234 DGS 236
Cdd:COG0411 234 EGT 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-231 |
8.73e-54 |
|
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: 173.77 E-value: 8.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQA----LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQR--EG 75
Cdd:COG4181 6 APIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL---DRPTSGTVRLAGQDLFAldED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 76 RLARdIRksRAHTGYIFQQFNLVNRLSVLENVLIGA-LGSTPfwrtcfswftgEQKQRALQALTRVGMVHFAHQRVSTLS 154
Cdd:COG4181 83 ARAR-LR--ARHVGFVFQSFQLLPTLTALENVMLPLeLAGRR-----------DARARARALLERVGLGHRLDHYPAQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-239 |
9.73e-54 |
|
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: 173.78 E-value: 9.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVqrEGRLARDIrkS 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS--GS-VLFDGEDI--TGLPPHEI--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTGEQK--QRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-231 |
1.54e-53 |
|
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: 172.66 E-value: 1.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRlard 80
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS--GE-VLVDGEPVTGPGP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 irksraHTGYIFQQFNLVNRLSVLENVLIGALGStpfwrtcfSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
Cdd:cd03293 74 ------DRGYVFQQDALLPWLTVLDNVALGLELQ--------GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVV-VTlHQVDYALRYCERIVAL--RQGHV 231
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLlVT-HDIDEAVFLADRVVVLsaRPGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-249 |
9.78e-53 |
|
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: 178.56 E-value: 9.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQH-----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGR 76
Cdd:COG1123 258 EPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS--GS-ILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 77 laRDIRKSRAHTGYIFQ----QFNlvNRLSVLENVLigalgstpFWRTCFSWFTGEQ-KQRALQALTRVGMV-HFAHQRV 150
Cdd:COG1123 335 --RSLRELRRRVQMVFQdpysSLN--PRMTVGDIIA--------EPLRLHGLLSRAErRERVAELLERVGLPpDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
250 260
....*....|....*....|
gi 985002877 231 VFYDGSSQQ-FDNERfdHLY 249
Cdd:COG1123 483 IVEDGPTEEvFANPQ--HPY 500
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-231 |
1.15e-52 |
|
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: 170.01 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQREGRLARDIrks 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD---SGEILIDGRDVTGVPPERRNI--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 rahtGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
Cdd:cd03259 75 ----GMVFQDYALFPHLTVAENIAFGlKLRGVP---------KAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-247 |
2.99e-52 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 170.19 E-value: 2.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSVGSHIELLGRTVQregrlARDI 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLempRSGTLNIAGNHFDFSKTPS-----DKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKSRAHTGYIFQQFNLVNRLSVLENvLIGA----LGSTpfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQN-LIEApcrvLGLS----------KDQALARAEKLLERLRLKPYADRFPLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPE-SARIVmDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIV-SIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
250
....*....|....
gi 985002877 237 SQQFDN---ERFDH 247
Cdd:PRK11124 225 ASCFTQpqtEAFKN 238
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-244 |
4.65e-52 |
|
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: 169.65 E-value: 4.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRLArdirks 84
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GS-ILIDGEDVRKEPREA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVLIgalgstpfwrtcFSWFTG----EQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRY------------FAELYGlfdeELKKRIEELIELLGLEEFLDRRVGELSTGMKKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
....
gi 985002877 241 DNER 244
Cdd:COG4555 220 REEI 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-231 |
6.43e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 172.25 E-value: 6.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGsHIELLGRTVQregrLARDIRKS 84
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDS--G-RIVLNGRDLF----TNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RahTGYIFQQFNLVNRLSVLENVLIGaLGSTPfwrtcfsWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:COG1118 76 R--VGFVFQHYALFPHMTVAENIAFG-LRVRP-------PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVV-VTlHQVDYALRYCERIVALRQGHV 231
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVfVT-HDQEEALELADRVVVMNQGRI 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
3.19e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 170.66 E-value: 3.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQR---EGRl 77
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDS--GR-ILLDGRDVTGlppEKR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 78 ardirksraHTGYIFQQFNLVNRLSVLENVLIG--ALGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSG 155
Cdd:COG3842 78 ---------NVGMVFQDYALFPHLTVAENVAFGlrMRGVPK----------AEIRARVAELLELVGLEGLADRYPHQLSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVV-VTlHQVDYALRYCERIVALRQGHV 231
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIyVT-HDQEEALALADRIAVMNDGRI 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-231 |
1.08e-49 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 166.41 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQ----HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVqreGRL-A 78
Cdd:COG1135 1 MIELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTS--GS-VLVDGVDL---TALsE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 79 RDIRKSRAHTGYIFQQFNLVNRLSVLENV-----LIGalgstpfwrtcfsWFTGEQKQRALQALTRVGMVHFAHQRVSTL 153
Cdd:COG1135 75 RELRAARRKIGMIFQHFNLLSSRTVAENValpleIAG-------------VPKAEIRKRVAELLELVGLSDKADAYPSQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-181 |
2.26e-49 |
|
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: 159.74 E-value: 2.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQRegrlaRDIRKSRAHTGYIFQQFNLVN 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEG---TILLDGQDLTD-----DERKSLRKEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENVLIGALgstpfwrtCFSWFTGEQKQRALQALTRVGMVHFAHQRV----STLSGGQQQRVAIARALMQQAKVIL 175
Cdd:pfam00005 73 RLTVRENLRLGLL--------LKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLL 144
|
....*.
gi 985002877 176 ADEPIA 181
Cdd:pfam00005 145 LDEPTA 150
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-247 |
3.27e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 162.49 E-value: 3.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSVGSHIELLGRTVQregrlARDI 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETpdsGQLNIAGHQFDFSQKPS-----EKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKSRAHTGYIFQQFNLVNRLSVLENvLIGA----LGSTpfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMEN-LIEApckvLGLS----------KEQAREKAMKLLARLRLTDKADRFPLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA 225
|
250
....*....|...
gi 985002877 238 QQFDN---ERFDH 247
Cdd:COG4161 226 SHFTQpqtEAFAH 238
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-231 |
1.01e-48 |
|
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: 158.71 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRlardirKS 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS--GE-IKVLGKDIKKEPE------EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVligalgstpfwrtcfswftgeqkqralqaltrvgmvhfahqrvsTLSGGQQQRVAIA 164
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL--------------------------------------------KLSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-226 |
1.25e-48 |
|
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: 159.70 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQR-EGRLARDIRksR 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLL---EKFDSGQVYLNGQETPPlNSKKASKFR--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 86 AHTGYIFQQFNLVNRLSVLENVLIGALGSTpfwRTcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
Cdd:TIGR03608 76 EKLGYLFQNFALIENETVEENLDLGLKYKK---LS-----KKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 985002877 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVdYALRYCERIVAL 226
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLELN-DEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-240 |
4.54e-48 |
|
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: 166.23 E-value: 4.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRTVQR--EGR 76
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLElsEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 77 LARDIrksrahtGYIFQQF-NLVNRLSVLENVLIGALgstpfwRTCFSWftGEQKQRALQALTRVGMVHFAHQRVSTLSG 155
Cdd:COG1123 81 RGRRI-------GMVFQDPmTQLNPVTVGDQIAEALE------NLGLSR--AEARARVLELLEAVGLERRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
....*
gi 985002877 236 SSQQF 240
Cdd:COG1123 226 PPEEI 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-235 |
2.63e-47 |
|
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: 157.55 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGD--KSVGSHIELLGRTVQREgrlar 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS----LITGDlpPTYGNDVRLFGERRGGE----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKSRAHTGYI--FQQFNLVNRLSVLENVLIGALGSTPFWRTcfswFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
Cdd:COG1119 72 DVWELRKRIGLVspALQLRFPRDETVLDVVLSGFFDSIGLYRE----PTDEQRERARELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVV-VTlHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVT-HHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-240 |
3.72e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 156.45 E-value: 3.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFnQHQALHAvDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvgshiellgrtvqrEGRLARDirkS 84
Cdd:COG3840 2 LRLDDLTYRY-GDFPLRF-DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPD----------------SGRILWN---G 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGY---------IFQQFNLVNRLSVLENVligALGSTPFWRtcfswFTGEQKQRALQALTRVGMVHFAHQRVSTLSG 155
Cdd:COG3840 61 QDLTALppaerpvsmLFQENNLFPHLTVAQNI---GLGLRPGLK-----LTAEQRAQVEQALERVGLAGLLDRLPGQLSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADG 212
|
....*
gi 985002877 236 SSQQF 240
Cdd:COG3840 213 PTAAL 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-245 |
2.64e-46 |
|
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: 155.69 E-value: 2.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKL-----AKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGRLA- 78
Cdd:TIGR04521 1 IKLKNVsyiyqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLL---KPTSGTVTIDGRDITAKKKKKl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 79 RDIRKsraHTGYIFQQ-----FnlvnRLSVLENVLIG--ALGSTPfwrtcfswftGEQKQRALQALTRVGM-VHFAHQRV 150
Cdd:TIGR04521 78 KDLRK---KVGLVFQFpehqlF----EETVYKDIAFGpkNLGLSE----------EEAEERVKEALELVGLdEEYLERSP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
Cdd:TIGR04521 141 FELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGK 220
|
250
....*....|....*.
gi 985002877 231 VFYDGSSQQ-FDNERF 245
Cdd:TIGR04521 221 IVLDGTPREvFSDVDE 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-241 |
8.24e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 156.77 E-value: 8.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGdksvGShIELLGRTVQREGRLARDIr 82
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLedPTS----GE-ILIGGRDVTDLPPKDRNI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 ksrahtGYIFQQFNLVNRLSVLENVLIG--ALGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
Cdd:COG3839 78 ------AMVFQSYALYPHMTVYENIAFPlkLRKVPK----------AEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESaRIVM-DTLRDINQNDGITVV-VTLHQVDyALRYCERIVALRQGHVfydgssQ 238
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKL-RVEMrAEIKRLHRRLGTTTIyVTHDQVE-AMTLADRIAVMNDGRI------Q 213
|
...
gi 985002877 239 QFD 241
Cdd:COG3839 214 QVG 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-239 |
1.68e-45 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 153.00 E-value: 1.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvgSHIELLGRTVQR--EGRLARd 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDS---GEVRLNGRPLADwsPAELAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 irksraHTGYIFQQFNLVNRLSVLENVligALGSTPfwrtcfsWFTGEQKQRAL--QALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:PRK13548 77 ------RRAVLPQHSSLSFPFTVEEVV---AMGRAP-------HGLSRAEDDALvaAALAQVDLAHLAGRDYPQLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 159 QRVAIARALMQ------QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
Cdd:PRK13548 141 QRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
....*..
gi 985002877 233 YDGSSQQ 239
Cdd:PRK13548 221 ADGTPAE 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-239 |
5.27e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 151.83 E-value: 5.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSVGSHIELLGRTVQREGRLar 79
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeaGTIRVGDITIDTARSLSQQKGL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 dIRKSRAHTGYIFQQFNLVNRLSVLENVLIGAL--GSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
Cdd:PRK11264 80 -IRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVivKGEP---------KEEATARARELLAKVGLAGKETSYPRRLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSS 237
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPA 228
|
..
gi 985002877 238 QQ 239
Cdd:PRK11264 229 KA 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-239 |
1.10e-44 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 151.04 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQR--EGRLARdir 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS---SGEVRLNGRPLAAwsPWELAR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 kSRAhtgyIFQQFNLVN-RLSVLENVligALGSTPfWRTCfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
Cdd:COG4559 76 -RRA----VLPQHSSLAfPFTVEEVV---ALGRAP-HGSS----AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 162 AIARALMQ-------QAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
Cdd:COG4559 143 QLARVLAQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQ 221
|
....*
gi 985002877 235 GSSQQ 239
Cdd:COG4559 222 GTPEE 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-231 |
3.38e-44 |
|
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: 148.92 E-value: 3.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQregrlarDIRKS 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSG---EILLDGKDIT-------NLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGlRLKKLP---------KAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAI 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-236 |
3.55e-44 |
|
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: 149.89 E-value: 3.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQREGRLaRDIR 82
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSG---KVTVDGLDTLDEENL-WEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KsraHTGYIFQ----QFnlVNRLsV-------LENvligaLGsTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVS 151
Cdd:TIGR04520 77 K---KVGMVFQnpdnQF--VGAT-VeddvafgLEN-----LG-VP---------REEMRKRVDEALKLVGMEDFRDREPH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
Cdd:TIGR04520 136 LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKI 214
|
....*
gi 985002877 232 FYDGS 236
Cdd:TIGR04520 215 VAEGT 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-231 |
9.01e-44 |
|
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: 148.41 E-value: 9.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQRegrlaRD 80
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS--GE-VTFDGRPVTR-----RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIFQQ-FNLVN-RLSVLEnvligALgSTPFWRTcfswFTGEQKQRALQALTRVGM-VHFAHQRVSTLSGGQ 157
Cdd:COG1124 74 RKAFRRRVQMVFQDpYASLHpRHTVDR-----IL-AEPLRIH----GLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-231 |
2.72e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.11 E-value: 2.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQregrlARDIRKS 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT---SGEIYLDGKPLS-----AMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVnRLSVLENVligalgSTPFWRTCFSWftgeQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAI 163
Cdd:COG4619 73 RRQVAYVPQEPALW-GGTVRDNL------PFPFQLRERKF----DRERALELLERLGLpPDILDKPVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-231 |
1.74e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 150.94 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQRegrlaRD 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDS--GE-ILLDGEPVRF-----RS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAH-TGYIFQQFNLVNRLSVLENVLIGALGSTPFWrtcFSWftGEQKQRALQALTRVGmVHF-AHQRVSTLSGGQQ 158
Cdd:COG1129 73 PRDAQAAgIAIIHQELNLVPNLSVAENIFLGREPRRGGL---IDW--RAMRRRARELLARLG-LDIdPDTPVGDLSVAQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVV-VT--LHQVdyaLRYCERIVALRQGHV 231
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIyIShrLDEV---FEIADRVTVLRDGRL 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-230 |
3.67e-42 |
|
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: 141.23 E-value: 3.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 6 RVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQRegrlaRDIRKSR 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL---KPTSGEILIDGKDIAK-----LPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 86 AHTGYIFQqfnlvnrlsvlenvligalgstpfwrtcfswftgeqkqralqaltrvgmvhfahqrvstLSGGQQQRVAIAR 165
Cdd:cd00267 73 RRIGYVPQ-----------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGH 230
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-235 |
3.75e-42 |
|
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: 143.80 E-value: 3.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGRLAR 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL---KPTSGSIIFDGKDLLKLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRksRAHTGYIFQQ-FNLVN-RLSVLENVLigalgsTPFWRTCFSWFTGEQKQRALQALTRVGMV-HFAHQRVSTLSGG 156
Cdd:cd03257 78 KIR--RKEIQMVFQDpMSSLNpRMTIGEQIA------EPLRIHGKLSKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-245 |
4.31e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 144.56 E-value: 4.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSVGShiELLGRTVQREGRL---- 77
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETpdsGEIRVGG--EEIRLKPDRDGELvpad 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 78 ARDIRKSRAHTGYIFQQFNLVNRLSVLENVL---IGALGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLS 154
Cdd:COG4598 87 RRQLQRIRTRLGMVFQSFNLWSHMTVLENVIeapVHVLGRPK----------AEAIERAEALLAKVGLADKRDAYPAHLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 155 GGQQQRVAIARALMQQAKVILADEPIASLDPEsarIVMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPE---LVGEVLKVMRDlaEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIE 233
|
250
....*....|....*..
gi 985002877 233 YDGSSQQ-FDN---ERF 245
Cdd:COG4598 234 EQGPPAEvFGNpksERL 250
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-235 |
7.83e-42 |
|
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: 142.43 E-value: 7.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 30 GEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQrEGRLARDIRKSRAHTGYIFQQFNLVNRLSVLENVLI 109
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPD---GGTIVLNGTVLF-DSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 110 GALGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESAR 189
Cdd:cd03297 99 GLKRKRN----------REDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 985002877 190 IVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-230 |
1.10e-41 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 142.16 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKT-FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLItgDKSVGSHIELLGRTVQREgRLAR 79
Cdd:NF038007 1 MLNMQNAEKCYITkTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLL-NIIGMF--DSLDSGSLTLAGKEVTNL-SYSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKSRAHTGYIFQQFNLVNRLSVLENVligALgstPFWRTCFSwfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
Cdd:NF038007 77 KIILRRELIGYIFQSFNLIPHLSIFDNV---AL---PLKYRGVA--KKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 985002877 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDyALRYCERIVALRQGH 230
Cdd:NF038007 149 RVAIARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSDE-ASTYGNRIINMKDGK 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-229 |
1.37e-41 |
|
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: 141.62 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQ-HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQREGRlaRDIR 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRG---QVRIAGEDVNRLRG--RQLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KSRAHTGYIFQQFNLVNRLSVLENV---LIGALGSTPFWRtcfswftgeqkQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
Cdd:TIGR02673 76 LLRRRIGVVFQDFRLLPDRTVYENValpLEVRGKKEREIQ-----------RRVGAALRQVGLEHKADAFPEQLSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG 229
Cdd:TIGR02673 145 RVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-223 |
1.51e-41 |
|
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: 141.46 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRLARdirks 84
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSA--GE-VLWNGEPIRDAREDYR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 rAHTGYIFQQFNLVNRLSVLENVLigalgstpFWRTCFSWFTGEQkqRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:COG4133 75 -RRLAYLGHADGLKPELTVRENLR--------FWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQvDYALRYCERI 223
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ-PLELAAARVL 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-236 |
1.37e-40 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 143.55 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQREGRLARDI 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD---SGRIMLDGQDITHVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 rksraHTgyIFQQFNLVNRLSVLENVLIG-ALGSTPFwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
Cdd:PRK09452 89 -----NT--VFQSYALFPHMTVFENVAFGlRMQKTPA---------AEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-239 |
2.40e-40 |
|
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: 139.40 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgshiellgrTVQREGRLARDIRKS 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSG----------TILFGGEDATDVPVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRTCFSwftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFG-LRVKPRSERPPE---AEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-240 |
3.28e-40 |
|
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: 138.47 E-value: 3.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKS--VGSHIELLGRTVqreGRLARDIR 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapDEGEVLLDGKDI---YDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KSRAHTGYIFQQFNLVnRLSVLENVLIGAlgstpfwRTCFSWFTGEQKQRALQALTRVGMVHFAHQR--VSTLSGGQQQR 160
Cdd:cd03260 78 ELRRRVGMVFQKPNPF-PGSIYDNVAYGL-------RLHGIKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-243 |
9.67e-40 |
|
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: 137.18 E-value: 9.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSVGShIELLGRtvqregrlarDIRKSRAHT------GYI 91
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP--PRSGS-IRFDGR----------DITGLPPHEraragiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 92 FQQFNLVNRLSVLENVLIGAL---GSTPFWRtcfswftgeqKQRALQALTRVGmvHFAHQRVSTLSGGQQQRVAIARALM 168
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYarrRAKRKAR----------LERVYELFPRLK--ERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 169 QQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-231 |
9.92e-40 |
|
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: 137.15 E-value: 9.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSVGShIELLGRTVQREGRlaRDIRK 83
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL--PTSGT-IRVNGQDVSDLRG--RAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 SRAHTGYIFQQFNLVNRLSVLENVLIG--ALGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
Cdd:cd03292 76 LRRKIGVVFQDFRLLPDRNVYENVAFAleVTGVPP----------REIRKRVPAALELVGLSHKHRALPAELSGGEQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-236 |
3.77e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 139.17 E-value: 3.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREGrlARD 80
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL---ERPTSGRVLVDGQDLTALS--EKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIFQQFNLVNRLSVLENV-LIGALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
Cdd:PRK11153 77 LRKARRQIGMIFQHFNLLSSRTVFDNVaLPLELAGTP---------KAEIKARVTELLELVGLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-251 |
5.83e-39 |
|
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: 135.89 E-value: 5.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFN-QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvgshiellGR-TVQREGRLARDIR 82
Cdd:cd03295 1 IEFENVTKRYGgGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTS---------GEiFIDGEDIREQDPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KSRAHTGYIFQQFNLVNRLSVLENVligalGSTPfwrTCFSWFTGEQKQRALQALTRVGM--VHFAHQRVSTLSGGQQQR 160
Cdd:cd03295 72 ELRRKIGYVIQQIGLFPHMTVEENI-----ALVP---KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVfydgssQQF 240
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI------VQV 217
|
250
....*....|.
gi 985002877 241 DNErfDHLYRS 251
Cdd:cd03295 218 GTP--DEILRS 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-239 |
9.97e-39 |
|
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: 135.85 E-value: 9.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 8 EKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGRLA-RDIRKSRA 86
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI---EPTSGKVLIDGQDIAAMSRKElRELRRKKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 87 htGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
Cdd:cd03294 105 --SMVFQSFALLPHRTVLENVAFGlEVQGVP---------RAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLAR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:cd03294 174 ALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-236 |
1.12e-38 |
|
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: 134.42 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREgrlARDIRKS 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL---KPTSGRATVAGHDVVRE---PREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 rahTGYIFQQFNLVNRLSVLENVLI-GALGSTPfWRtcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
Cdd:cd03265 75 ---IGIVFQDLSVDDELTGWENLYIhARLYGVP-GA--------ERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGT 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-239 |
1.64e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.91 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSVGsHIELLGRTVQreg 75
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlpeAGTITVG-GMVLSEETVW--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 76 rlarDIRKsraHTGYIFQqfNLVNRL---SVLENVLIGaLGSTPFWRTcfswftgEQKQRALQALTRVGMVHFAHQRVST 152
Cdd:PRK13635 78 ----DVRR---QVGMVFQ--NPDNQFvgaTVQDDVAFG-LENIGVPRE-------EMVERVDQALRQVGMEDFLNREPHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVF 232
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
....*..
gi 985002877 233 YDGSSQQ 239
Cdd:PRK13635 220 EEGTPEE 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-238 |
4.49e-38 |
|
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: 135.21 E-value: 4.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQREgrlARDIRKSrahTGYI 91
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPT---SGTARVAGYDVVRE---PRKVRRS---IGIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 92 FQQFNLVNRLSVLEN-VLIGALGSTPFWrtcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
Cdd:TIGR01188 72 PQYASVDEDLTGRENlEMMGRLYGLPKD---------EAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 171 AKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
Cdd:TIGR01188 143 PDVLFLDEPTTGLDPRTRRAIWDYIRALKE-EGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-240 |
6.24e-38 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 132.67 E-value: 6.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRtvqregrlarDI--- 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS--GK-ILLDGQ----------DItkl 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 ---RKSRAHTGYIFQQFNLVNRLSVLENVLIgALGSTPFWRTcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:cd03218 68 pmhKRARLGIGYLPQEASIFRKLTVEENILA-VLEIRGLSKK-------EREEKLEELLEEFHITHLRKSKASSLSGGER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
Cdd:cd03218 140 RRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPE 218
|
..
gi 985002877 239 QF 240
Cdd:cd03218 219 EI 220
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-239 |
6.29e-38 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 135.93 E-value: 6.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREGRLARD 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL---ERQTAGTIYQGGRDITRLPPQKRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IrksrahtGYIFQQFNLVNRLSVLENVLIGALGStpfwrtcfSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
Cdd:TIGR03265 78 Y-------GIVFQSYALFPNLTVADNIAYGLKNR--------GMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 161 VAIARALMQQAKVILADEPIASLDpesARI---VMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
Cdd:TIGR03265 143 VALARALATSPGLLLLDEPLSALD---ARVrehLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTP 219
|
..
gi 985002877 238 QQ 239
Cdd:TIGR03265 220 QE 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-235 |
7.40e-38 |
|
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: 131.93 E-value: 7.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGeMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQREGRlardirKS 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSG---TIRIDGQDVLKQPQ------KL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENV-LIGALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVREFLdYIAWLKGIP---------SKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 164 ARALMQQAKVILADEPIASLDPESaRIVMDT-LRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEE-RIRFRNlLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-239 |
8.34e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 135.60 E-value: 8.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREGrlARDirks 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL---EHQTSGHIRFHGTDVSRLH--ARD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 rAHTGYIFQQFNLVNRLSVLENVligALGSTPFWRTcfswftgEQ------KQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:PRK10851 74 -RKVGFVFQHYALFRHMTVFDNI---AFGLTVLPRR-------ERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
.
gi 985002877 239 Q 239
Cdd:PRK10851 223 Q 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-239 |
1.47e-37 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 132.51 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQR--EGRLARDIR 82
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDS--GE-VLVDGLDVATtpSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 ksrahtgyIFQQFNLVN-RLSVLENVligALGSTPFWRtcfSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
Cdd:COG4604 79 --------ILRQENHINsRLTVRELV---AFGRFPYSK---GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-238 |
1.80e-37 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 139.09 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREGR--LARdIRksRAHTGYIFQQFNL 97
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCL---DKPTSGTYRVAGQDVATLDAdaLAQ-LR--REHFGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRLSVLENVLIGAL--GSTpfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
Cdd:PRK10535 98 LSHLTAAQNVEVPAVyaGLE----------RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 176 ADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQ 238
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQ 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-239 |
1.95e-37 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 132.45 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT-GDKSVGSHIELLGRTVQREgrLARdi 81
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTpQSGTVFLGDKPISMLSSRQ--LAR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 rksraHTGYIFQQFNLVNRLSVLENVligALGSTPfWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
Cdd:PRK11231 77 -----RLALLPQHHLTPEGITVRELV---AYGRSP-WLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-242 |
4.61e-37 |
|
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: 130.49 E-value: 4.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRtvqregrlarDIRKSRAHT------GY- 90
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLL---PPRSGSIRFDGE----------DITGLPPHRiarlgiGYv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 91 -----IFQQfnlvnrLSVLENVLIGAlgstpfwrtcfswFTGEQKQRALQALTRVgMVHF------AHQRVSTLSGGQQQ 159
Cdd:COG0410 84 pegrrIFPS------LTVEENLLLGA-------------YARRDRAEVRADLERV-YELFprlkerRRQRAGTLSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
...
gi 985002877 240 FDN 242
Cdd:COG0410 223 LLA 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-239 |
4.85e-37 |
|
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: 130.32 E-value: 4.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQaLHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSVGShIELLGRTVQRegrlarDI 81
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDdlsLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR--PTSGT-AYINGYSIRT------DR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKSRAHTGYIFQQFNLVNRLSVLENVLIgalgstpfwrtcFSWFTG----EQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
Cdd:cd03263 71 KAARQSLGYCPQFDALFDELTVREHLRF------------YARLKGlpksEIKEEVELLLRVLGLTDKANKRARTLSGGM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
..
gi 985002877 238 QQ 239
Cdd:cd03263 217 QE 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
9-235 |
4.12e-36 |
|
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: 127.61 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 9 KLAKTFN--QHQALHaVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvgSHIELLGrtvqreGRLARDIRKSRA 86
Cdd:cd03298 2 RLDKIRFsyGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQ----SGRVLIN------GVDVTAAPPADR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 87 HTGYIFQQFNLVNRLSVLENVligALGSTPFWRtcfswFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARA 166
Cdd:cd03298 71 PVSMLFQENNLFAHLTVEQNV---GLGLSPGLK-----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-242 |
8.84e-36 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 127.80 E-value: 8.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSVGSHIE----LLGRTVQREGRlar 79
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRM--NDLVPGVRIEgkvlFDGQDIYDKKI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKSRAHTGYIFQQFNLVNrLSVLENVLIG--ALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVST----L 153
Cdd:TIGR00972 76 DVVELRRRVGMVFQKPNPFP-MSIYDNIAYGprLHGIKD---------KKELDEIVEESLKKAALWDEVKDRLHDsalgL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERIVALRQGHVFY 233
Cdd:TIGR00972 146 SGGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFYDGELVE 223
|
250
....*....|
gi 985002877 234 DGSSQQ-FDN 242
Cdd:TIGR00972 224 YGPTEQiFTN 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-231 |
1.06e-35 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 131.12 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksVGShIELLGRTVqrEGRLARDIRKS 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT--AGT-VLVAGDDV--EALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGyifQQFNLVNRLSVLENVligALGSTPFwRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:PRK09536 79 VASVP---QDTSLSFEFDVRQVV---EMGRTPH-RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-230 |
1.20e-35 |
|
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: 125.19 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREgrlarDIRKSRAHTGYIFQQ 94
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTS--GE-ILIDGVDLRDL-----DLESLRKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 FNLVNRlSVLENVLigalgstpfwrtcfswftgeqkqralqaltrvgmvhfahqrvstlSGGQQQRVAIARALMQQAKVI 174
Cdd:cd03228 85 PFLFSG-TIRENIL---------------------------------------------SGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 175 LADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGH 230
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-231 |
1.28e-35 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 130.36 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSVGS-HIELLGRTVQREGRLARDIRKSrahTGYIFQQFNL 97
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLI--EPTAGQiFIDGENIMKQSPVELREVRRKK---IGMVFQQFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRLSVLENvligalgsTPFWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
Cdd:TIGR01186 83 FPHMTILQN--------TSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 985002877 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:TIGR01186 155 EAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEI 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-239 |
1.91e-35 |
|
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: 129.46 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQrEGRLARDIRKSRAHTGYIFQQFNLVNRLS 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPD---EGEIVLNGRTLF-DSRKGIFLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 103 VLENVLIGalgstpFWRTcfswfTGEQKQRALQALTRV-GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
Cdd:TIGR02142 92 VRGNLRYG------MKRA-----RPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 182 SLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-235 |
2.24e-35 |
|
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: 125.41 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQREgrlardiRKS 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD---SGEITFDGKSYQKN-------IEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVLIGALGstpfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARL------------LGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-239 |
2.39e-35 |
|
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: 133.42 E-value: 2.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELlgrtvqrEGRLARDIR 82
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS--GR-ILI-------DGIDLRQID 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KS--RAHTGYIFQQFNLVNRlSVLENVLIGALGSTPfwrtcfswftgeqkQRALQALTRVGMVHFAHQ-----------R 149
Cdd:COG2274 544 PAslRRQIGVVLQDVFLFSG-TIRENITLGDPDATD--------------EEIIEAARLAGLHDFIEAlpmgydtvvgeG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQG 229
Cdd:COG2274 609 GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRIIVLDKG 685
|
250
....*....|
gi 985002877 230 HVFYDGSSQQ 239
Cdd:COG2274 686 RIVEDGTHEE 695
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-243 |
2.40e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 127.54 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQregrlAR 79
Cdd:PRK13647 1 MDNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQR--GR-VKVMGREVN-----AE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKSRAHTGYIFQQ-FNLVNRLSVLENVLIGA--LGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGG 156
Cdd:PRK13647 73 NEKWVRSKVGLVFQDpDDQVFSSTVWDDVAFGPvnMGLDK----------DEVERRVEEALKAVRMWDFRDKPPYHLSYG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:PRK13647 143 QKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD 221
|
....*..
gi 985002877 237 SQQFDNE 243
Cdd:PRK13647 222 KSLLTDE 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-250 |
3.33e-35 |
|
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: 132.20 E-value: 3.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSVGShIELLGRTVQRegrLARDIR 82
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL--DPQSGS-ITLGGVDLRD---LDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 ksRAHTGYIFQQFNLVNRlSVLENVLIGALGSTPfwrtcfswftgeqkQRALQALTRVGMVHFAHQ-------RV----S 151
Cdd:COG4987 408 --RRRIAVVPQRPHLFDT-TLRENLRLARPDATD--------------EELWAALERVGLGDWLAAlpdgldtWLgeggR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQVdyALRYCERIVALRQGHV 231
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV-LLITHRLA--GLERMDRILVLEDGRI 547
|
250 260
....*....|....*....|.
gi 985002877 232 FYDGSSQQF--DNERFDHLYR 250
Cdd:COG4987 548 VEQGTHEELlaQNGRYRQLYQ 568
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-235 |
8.00e-35 |
|
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: 124.40 E-value: 8.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVgshIELLGRTVQREGRLAR 79
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGF---ATVDGFDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 dirksrAHTGYIFQQFNLVNRLSVLENVLIgalgstpfwrtcFSWFTGEQKQRALQAL----TRVGMVHFAHQRVSTLSG 155
Cdd:cd03266 78 ------RRLGFVSDSTGLYDRLTARENLEY------------FAGLYGLKGDELTARLeelaDRLGMEELLDRRVGGFST 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:cd03266 140 GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-234 |
8.27e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 125.56 E-value: 8.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSvgSHIELL-GRTVQREGRlaRDIRksr 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL---ETP--SAGELLaGTAPLAEAR--EDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 86 ahtgYIFQQFNLVNRLSVLENVLIGALGStpfWRTcfswftgeqkqRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
Cdd:PRK11247 85 ----LMFQDARLLPWKKVIDNVGLGLKGQ---WRD-----------AALQALAAVGLADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 166 ALMQQAKVILADEPIASLDPESaRIVM-DTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALT-RIEMqDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-231 |
1.20e-34 |
|
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: 130.65 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShiellgrtVQREGRLARDIRKS--RAHTGYIFQQ 94
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS--GS--------ILINGVDLSDLDPAswRRQIAWVPQN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 FNLVNrLSVLENVLIGALGSTPfwrtcfswftgeqkQRALQALTRVGMVHFAHQ-----------RVSTLSGGQQQRVAI 163
Cdd:COG4988 420 PYLFA-GTIRENLRLGRPDASD--------------EELEAALEAAGLDEFVAAlpdgldtplgeGGRGLSGGQAQRLAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHV 231
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLA-LLAQADRILVLDDGRI 549
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
18-216 |
2.16e-34 |
|
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: 122.53 E-value: 2.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREgrlARDIRKSRAHTGYIFQqfNL 97
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLL---RPQSGAVLIDGEPLDYS---RKGLLERRQRVGLVFQ--DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRL---SVLENVLIGA--LGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAK 172
Cdd:TIGR01166 78 DDQLfaaDVDQDVAFGPlnLGLSE----------AEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 985002877 173 VILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYA 216
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRA-EGMTVVISTHDVDLA 190
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-231 |
4.61e-34 |
|
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: 125.98 E-value: 4.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQrEGRLARDIRKSRAHTGYIFQQFNLVNRLS 102
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD---SGRIRLGGEVLQ-DSARGIFLPPHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 103 VLENVLIGAlgstpfWRTcfswFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
Cdd:COG4148 94 VRGNLLYGR------KRA----PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 985002877 183 LDPESARIVMDTLRDINQNDGITVV-VTlHQVDYALRYCERIVALRQGHV 231
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIPILyVS-HSLDEVARLADHVVLLEQGRV 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
5.11e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 124.81 E-value: 5.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQtiIRVEKLAKTFNQH-----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD-------------KSVGS 62
Cdd:PRK13651 1 MQ--IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDtgtiewifkdeknKKKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 63 HIE------LLGRTVQREGRLARDIRKsraHTGYIFQ--QFNLVNRlSVLENVLIGA--LGSTPfwrtcfswftGEQKQR 132
Cdd:PRK13651 79 EKEkvleklVIQKTRFKKIKKIKEIRR---RVGVVFQfaEYQLFEQ-TIEKDIIFGPvsMGVSK----------EEAKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 133 ALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLH 211
Cdd:PRK13651 145 AAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTH 223
|
250 260
....*....|....*....|....
gi 985002877 212 QVDYALRYCERIVALRQGHVFYDG 235
Cdd:PRK13651 224 DLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-236 |
5.17e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 124.03 E-value: 5.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVgshIELLGRTVQREgrlARDIRKSRAHTGYIFQqfNL 97
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGE---VLIKGEPIKYD---KKSLLEVRKTVGIVFQ--NP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRL---SVLENVLIGALGstpfwrtcFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
Cdd:PRK13639 88 DDQLfapTVEEDVAFGPLN--------LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 985002877 175 LADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-239 |
1.31e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 121.61 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFnQHQALHaVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgshiellgrTVQREGRLARDIRKS 84
Cdd:PRK10771 2 LKLTDITWLY-HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASG----------SLTLNGQDHTTTPPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVligALGSTPFWRtcfswFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:PRK10771 70 RRPVSMLFQENNLFSHLTVAQNI---GLGLNPGLK-----LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 165 RALMQQAKVILADEPIASLDPeSARIVMDTL-RDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALDP-ALRQEMLTLvSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-229 |
1.50e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 121.42 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQ--HQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREGRL 77
Cdd:PRK10584 4 ENIVEVHHLKKSVGQgeHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGL---DDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 78 ARDIRKSRaHTGYIFQQFNLVNRLSVLENVLIGAL--GSTpfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSG 155
Cdd:PRK10584 81 ARAKLRAK-HVGFVFQSFMLIPTLNALENVELPALlrGES----------SRQSRNGAKALLEQLGLGKRLDHLPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQG 229
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNG 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-231 |
1.70e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 126.68 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQregrlard 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDS--GE-ILIDGKPVR-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSR----AHTGYIFQQFNLVNRLSVLENVligALGSTPFWRTCFSWFTGEQKQRALQAltRVGM-VHfAHQRVSTLSG 155
Cdd:COG3845 71 IRSPRdaiaLGIGMVHQHFMLVPNLTVAENI---VLGLEPTKGGRLDRKAARARIRELSE--RYGLdVD-PDAKVEDLSV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:COG3845 145 GEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-236 |
2.11e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.91 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREgrlardirk 83
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDS--GE-VLWDGEPLDPE--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 SRAHTGY------IFQqfnlvnRLSVLENVL-IGAL-GSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSG 155
Cdd:COG4152 69 DRRRIGYlpeergLYP------KMKVGEQLVyLARLkGLSK----------AEAKRRADEWLERLGLGDRANKKVEELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
.
gi 985002877 236 S 236
Cdd:COG4152 212 S 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-250 |
2.27e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.06 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREGRLARDIrksrahtGYI 91
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL---EKPTEGQIFIDGEDVTHRSIQQRDI-------CMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 92 FQQFNLVNRLSVLENVLIG--ALGSTpfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGlkMLGVP----------KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQfdnerfdhLY 249
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE--------LY 225
|
.
gi 985002877 250 R 250
Cdd:PRK11432 226 R 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-231 |
3.05e-33 |
|
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: 118.69 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQRegrlaRDIRKS 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS--GE-ILVDGKEVSF-----ASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHtgyifqqfnlvnrlsvlenvligalgstpfwrtcfswftgeqkqralqaltRVGMVHfahQrvstLSGGQQQRVAIA 164
Cdd:cd03216 73 RRA---------------------------------------------------GIAMVY---Q----LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-231 |
3.61e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 120.69 E-value: 3.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREGRLARDIRKSRaHTGYIFQQFNLVN 99
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQPMSKLSSAAKAELRNQ-KLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENV----LIGalGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
Cdd:PRK11629 101 DFTALENVamplLIG--KKKP----------AEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 176 ADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-239 |
4.69e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.84 E-value: 4.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQ----REGRLA-- 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL---EKPSEGSIVVNGQTINlvrdKDGQLKva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 79 --RDIRKSRAHTGYIFQQFNLVNRLSVLENVL---IGALGSTpfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVST- 152
Cdd:PRK10619 83 dkNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeapIQVLGLS----------KQEARERAVKYLAKVGIDERAQGKYPVh 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPEsarIVMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQGH 230
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
....*....
gi 985002877 231 VFYDGSSQQ 239
Cdd:PRK10619 230 IEEEGAPEQ 238
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-241 |
5.81e-33 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 121.74 E-value: 5.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSVGShIELLGRTVQRegrlaRDIRK 83
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLI--EPTSGR-ILIDGEDIRD-----LDPVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 SRAHTGYIFQQFNLVNRLSVLENV-----LIGalgstpfwrtcfsWFTGEQKQRALQALTRVGM--VHFAHQRVSTLSGG 156
Cdd:COG1125 74 LRRRIGYVIQQIGLFPHMTVAENIatvprLLG-------------WDKERIRARVDELLELVGLdpEEYRDRYPHELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDPesarIVMDTLRD----INQNDGITVV-VTlHQVDYALRYCERIVALRQGHV 231
Cdd:COG1125 141 QQQRVGVARALAADPPILLMDEPFGALDP----ITREQLQDellrLQRELGKTIVfVT-HDIDEALKLGDRIAVMREGRI 215
|
250
....*....|
gi 985002877 232 fydgssQQFD 241
Cdd:COG1125 216 ------VQYD 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-229 |
6.20e-33 |
|
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: 119.31 E-value: 6.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVgshIELLGRTVQREGRlardirks 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE---VLFDGKPLDIAAR-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 rAHTGYIFQQFNLVNRLSVLENVL-IGAL-GSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
Cdd:cd03269 70 -NRIGYLPEERGLYPKMKVIDQLVyLAQLkGLKK----------EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG 229
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-236 |
7.97e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 120.96 E-value: 7.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgshiellgrTVQREG---RLARDIRKSRAHTGYI 91
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEG----------KVYVDGldtSDEENLWDIRNKAGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 92 FQqfNLVNRLS---VLENVLIGA--LGSTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARA 166
Cdd:PRK13633 91 FQ--NPDNQIVatiVEEDVAFGPenLGIPP----------EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGS 236
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-231 |
9.00e-33 |
|
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: 118.90 E-value: 9.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvgshiellGRtVQREGRLARDIRKS 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTS---------GR-IYIGGRDVTDLPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRTcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFG-LKLRKVPKD-------EIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 165 RALMQQAKVILADEPIASLDPEsARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAK-LRVQMRAeLKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-239 |
9.78e-33 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 120.48 E-value: 9.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSVGSHIELLGRTVQR--EGRLARDIr 82
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT---PAHGHVWLDGEHIQHyaSKEVARRI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 ksrahtGYIFQQFNLVNRLSVLENVLIGALGSTPFwrtcFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
Cdd:PRK10253 84 ------GLLAQNATTPGDITVQELVARGRYPHQPL----FTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAW 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-229 |
1.40e-32 |
|
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: 119.11 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREG--RLArdirksrahtgyIFQQFNL 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL---AQPTSGGVILEGKQITEPGpdRMV------------VFQNYSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRLSVLENVLIGALGSTPFWRTcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
Cdd:TIGR01184 66 LPWLTVRENIALAVDRVLPDLSK------SERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 985002877 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-218 |
1.63e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 117.72 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 14 FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksvgshiellgrtvQREGRLARdirKSRAHTGYIFQ 93
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR----------------PTSGTVRR---AGGARVAYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 94 QFNLVNRL--SVLENVLIGALGSTPFWRtcfsWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
Cdd:NF040873 63 RSEVPDSLplTVRDLVAMGRWARRGLWR----RLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 985002877 172 KVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALR 218
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRR 184
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-186 |
5.58e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.81 E-value: 5.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 6 RVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGR---TVQREGRlardir 82
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRrltALPAEQR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 ksraHTGYIFQQFNLVNRLSVLENVLIGALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
Cdd:COG4136 77 ----RIGILFQDDLLFPHLSVGENLAFALPPTIG---------RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVA 143
|
170 180
....*....|....*....|....
gi 985002877 163 IARALMQQAKVILADEPIASLDPE 186
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAA 167
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-243 |
1.30e-31 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 121.82 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSVGShIELLGRTVQR-EGRLAR 79
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIH--EPTKGT-ITINNINYNKlDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIrksraHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRT-CFSWftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:PRK09700 79 QL-----GIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVnIIDW--REMRVRAAMMLLRVGLKVDLDEKVANLSISHK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESAR---IVMDTLRdinqNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDylfLIMNQLR----KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
....*...
gi 985002877 236 SSQQFDNE 243
Cdd:PRK09700 228 MVSDVSND 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-231 |
1.43e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 117.27 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQREGrlardirksrAHTGYIFQQF 95
Cdd:COG4525 19 PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS---SGEITLDGVPVTGPG----------ADRGVVFQKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 96 NLVNRLSVLENVligALGSTpfwrtcfswFTG----EQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
Cdd:COG4525 86 ALLPWLNVLDNV---AFGLR---------LRGvpkaERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 985002877 172 KVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL--RQGHV 231
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-244 |
3.58e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 115.51 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGsHIELLGrtvqregrlaRDI-- 81
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS--G-RIFLDG----------EDIth 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 ----RKSRAHTGY------IFQqfnlvnRLSVLENVLIgALGSTPFWRTcfswftgEQKQRALQALTRVGMVHFAHQRVS 151
Cdd:COG1137 70 lpmhKRARLGIGYlpqeasIFR------KLTVEDNILA-VLELRKLSKK-------EREERLEELLEEFGITHLRKSKAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESA----RIVMDtLRDinqnDGITVVVTLHQVDYALRYCERIVALR 227
Cdd:COG1137 136 SLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVadiqKIIRH-LKE----RGIGVLITDHNVRETLGICDRAYIIS 210
|
250
....*....|....*...
gi 985002877 228 QGHVFYDGSSQQF-DNER 244
Cdd:COG1137 211 EGKVLAEGTPEEIlNNPL 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-253 |
6.46e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.10 E-value: 6.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 3 TIIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREgrlARDI 81
Cdd:PRK13636 4 YILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL---KPSSGRILFDGKPIDYS---RKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKSRAHTGYIFQQFNlvNRL---SVLENVLIGALGstpfwrtcFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:PRK13636 78 MKLRESVGMVFQDPD--NQLfsaSVYQDVSFGAVN--------LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
250
....*....|....*
gi 985002877 239 QFDNERfdHLYRSIN 253
Cdd:PRK13636 228 EVFAEK--EMLRKVN 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-229 |
6.66e-31 |
|
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: 114.45 E-value: 6.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQ-------ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDkSVGSHIEL 66
Cdd:COG4778 1 MTTLLEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSILVR-HDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 67 LGRTvqregrlARDIRKSRAHT-GYIFQQFNLVNRLSVLENV---LIgALGSTPfwrtcfswftGEQKQRALQALTRVGM 142
Cdd:COG4778 80 AQAS-------PREILALRRRTiGYVSQFLRVIPRVSALDVVaepLL-ERGVDR----------EEARARARELLARLNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 143 vhfaHQRV-----STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL 217
Cdd:COG4778 142 ----PERLwdlppATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVRE 216
|
250
....*....|..
gi 985002877 218 RYCERIVALRQG 229
Cdd:COG4778 217 AVADRVVDVTPF 228
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-231 |
8.68e-31 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 117.90 E-value: 8.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSVGShIELLGRTVQR--EGRLaRDIRksRAHTGYIFQQFN 96
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLI--EPTAGE-VLIDGEDITKlsKKEL-RELR--RKKMSMVFQHFA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 LVNRLSVLENVligALG----STPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAK 172
Cdd:COG4175 116 LLPHRTVLENV---AFGleiqGVP---------KAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 173 VILADEPIASLDP----EsarivM-DTLRDINQNDGITVV-VTlHQVDYALRYCERIVALRQGHV 231
Cdd:COG4175 184 ILLMDEAFSALDPlirrE-----MqDELLELQAKLKKTIVfIT-HDLDEALRLGDRIAIMKDGRI 242
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-231 |
1.43e-30 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 118.88 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT-GDKSVGSHIEllGRTVQregrlAR 79
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhGTYEGEIIFE--GEELQ-----AS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKS-RAHTGYIFQQFNLVNRLSVLENVLIGAlGSTPFWRTCFSwftgEQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:PRK13549 75 NIRDTeRAGIAIIHQELALVKELSVLENIFLGN-EITPGGIMDYD----AMYLRAQKLLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQG-HV 231
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGrHI 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-209 |
1.47e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 114.36 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG---LITGDKSVGShIELLGRTVqregrL 77
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGARVEGE-ILLDGEDI-----Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 78 ARDIRKS--RAHTGYIFQQFNLVNrLSVLENVLIGAlgstpfwRTcfswfTGEQKQRAL-----QALTRVGM---V-HFA 146
Cdd:COG1117 82 DPDVDVVelRRRVGMVFQKPNPFP-KSIYDNVAYGL-------RL-----HGIKSKSELdeiveESLRKAALwdeVkDRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVV-VT 209
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIViVT 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
1.57e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.12 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFN-----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGShielLGRTVQREGRLAR 79
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT----IGERVITAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKSRAHTGYIFQ--QFNLVNRlSVLENVLIGALGstpfwrtcFSWFTGEQKQRALQALTRVGMVHFAHQRVS-TLSGG 156
Cdd:PRK13634 79 KLKPLRKKVGIVFQfpEHQLFEE-TVEKDICFGPMN--------FGVSEEDAKQKAREMIELVGLPEELLARSPfELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
...
gi 985002877 237 SQQ 239
Cdd:PRK13634 230 PRE 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-235 |
3.11e-30 |
|
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: 111.87 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGShIELLGRTvqregrlaRDIRKSRAHTGYIFQQFNLVN 99
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGE-VLINGRP--------LDKRSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENVLIGAlgstpfwrtcfswftgeqkqralqaltrvgmvhfahqRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
Cdd:cd03213 96 TLTVRETLMFAA-------------------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 180 IASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-231 |
3.51e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.34 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSVGShIELLGRTVqregrlaRDIRKS--RAHTGYIF 92
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY--DPTSGR-ILIDGVDI-------RDLTLEslRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 93 QQFNLVNRlSVLENVLIGALGSTPfwrtcfswftgEQKQRALQAL--------------TRVGmvhfahQRVSTLSGGQQ 158
Cdd:COG1132 421 QDTFLFSG-TIRENIRYGRPDATD-----------EEVEEAAKAAqahefiealpdgydTVVG------ERGVNLSGGQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHV 231
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRILVLDDGRI 552
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-239 |
4.15e-30 |
|
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: 114.90 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 35 LLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQregrlarDIRKSRAHTGYIFQQFNLVNRLSVLENVLIG-ALG 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS--GS-IMLDGEDVT-------NVPPHLRHINMVFQSYALFPHMTVEENVAFGlKMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 114 STPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMD 193
Cdd:TIGR01187 71 KVP---------RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 985002877 194 TLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:TIGR01187 142 ELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEE 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-207 |
4.40e-30 |
|
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: 114.38 E-value: 4.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQ-ALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRTVQR--EGRL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRgVVKAVDgvsFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKlsEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 78 aRDIRKSRAhtGYIFQQ----FNLVNRL--SVLENVLIGALGSTpfwrtcfswftGEQKQRALQALTRVGMVH------- 144
Cdd:COG0444 81 -RKIRGREI--QMIFQDpmtsLNPVMTVgdQIAEPLRIHGGLSK-----------AEARERAIELLERVGLPDperrldr 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 145 FAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVV 207
Cdd:COG0444 147 YPHE----LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAIL 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-231 |
2.86e-29 |
|
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: 110.50 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQaLHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQREGRLARDIrks 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSG---KILLNGKDITNLPPEKRDI--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 rahtGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRTcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:cd03299 74 ----SYVPQNYALFPHMTVYKNIAYG-LKKRKVDKK-------EIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-242 |
7.23e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.87 E-value: 7.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--------ITGDKSVGSHIELLGRTvq 72
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpevtITGSIVYNGHNIYSPRT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 73 regrlarDIRKSRAHTGYIFQQFNLVNrLSVLENVLIGALgstpfwrtcfswFTGEQKQRALQALTRVGMVHFA------ 146
Cdd:PRK14239 80 -------DTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLR------------LKGIKDKQVLDEAVEKSLKGASiwdevk 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 147 ---HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERI 223
Cdd:PRK14239 140 drlHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISDRT 217
|
250 260
....*....|....*....|
gi 985002877 224 VALRQGHVF-YDGSSQQFDN 242
Cdd:PRK14239 218 GFFLDGDLIeYNDTKQMFMN 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-229 |
1.18e-28 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 113.56 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksVGShIELLGRTVQREGRlard 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRD--AGS-ILYLGKEVTFNGP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 iRKSR-AHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcFSWftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
Cdd:PRK10762 74 -KSSQeAGIGIIHQELNLIPQLTIAENIFLGREFVNRFGR--IDW--KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 160 RVAIARALMQQAKVILADEPIASL-DPESARI--VMDTLRDinQNDGItvVVTLHQVDYALRYCERIVALRQG 229
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALtDTETESLfrVIRELKS--QGRGI--VYISHRLKEIFEICDDVTVFRDG 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-234 |
1.70e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.02 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFN-----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQR--EGR 76
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD---SGSILIDGKDVTKlpEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 77 LARDIrksrahtGYIFQqfnlvN-------RLSVLENVLIGALGSTPFWrtcFSW-FTGEQKQ--RALQALTRVGMVHFA 146
Cdd:COG1101 78 RAKYI-------GRVFQ-----DpmmgtapSMTIEENLALAYRRGKRRG---LRRgLTKKRRElfRELLATLGLGLENRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
Cdd:COG1101 143 DTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMM 222
|
....*...
gi 985002877 227 RQGHVFYD 234
Cdd:COG1101 223 HEGRIILD 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-229 |
2.28e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.08 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREGRLARDIrk 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF---EQPTAGQIMLDGVDLSHVPPYQRPI-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 srahtGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
Cdd:PRK11607 94 -----NMMFQSYALFPHMTVEQNIAFG-LKQDKLPK-------AEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-244 |
2.74e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 108.08 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT--GDKSVGSHIELLGRTVqregrLAR 79
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEARVSGEVYLDGQDI-----FKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKSRAHTGYIFQQFNLVNRLSVLENVLIGalgsTPFWRTCFSwfTGEQKQRALQALTRVGMVHFAHQRV----STLSG 155
Cdd:PRK14247 76 DVIELRRRVQMVFQIPNPIPNLSIFENVALG----LKLNRLVKS--KKELQERVRWALEKAQLWDEVKDRLdapaGKLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
250
....*....|
gi 985002877 236 SSQQ-FDNER 244
Cdd:PRK14247 228 PTREvFTNPR 237
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-239 |
3.11e-28 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 108.34 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksvGSHIELLGRTVQREGR-LARDIRKSRA-HTGYIFQQFNL 97
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKML----------GRHQPPSEGEILLDAQpLESWSSKAFArKVAYLPQQLPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRLSVLENVligALGSTPfWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
Cdd:PRK10575 97 AEGMTVRELV---AIGRYP-WHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 985002877 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-231 |
3.32e-28 |
|
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: 106.87 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSVGSHIELLGRTVQREGRLARDIrksrahtGYIF 92
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIE---PASGSIKVNDQSHTGLAPYQRPV-------SMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 93 QQFNLVNRLSVLENVligALGSTPFWRtcfswFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAK 172
Cdd:TIGR01277 77 QENNLFAHLTVRQNI---GLGLHPGLK-----LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 173 VILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:TIGR01277 149 ILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-229 |
3.65e-28 |
|
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: 106.57 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 6 RVEKLAKTFNQHQ-ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQRegrlaRDIRKS 84
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI---KESSGSILLNGKPIKA-----KERRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 rahTGYIFQ--QFNLVnRLSVLENVLIGALGstpfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
Cdd:cd03226 73 ---IGYVMQdvDYQLF-TDSVREELLLGLKE------------LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQG 229
Cdd:cd03226 137 IAAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-231 |
1.75e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 105.34 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREGRlaRDIR 82
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI---ERPSAGKIWFSGHDITRLKN--REVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KSRAHTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTGEQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
Cdd:PRK10908 76 FLRRQIGMIFQDHHLLMDRTVYDNVAIPLI---------IAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-249 |
1.80e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 105.75 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIrVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvgshiellGRTVQREgrlaRD 80
Cdd:PRK10895 1 MATLT-AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA---------GNIIIDD----ED 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 I------RKSRAHTGYIFQQFNLVNRLSVLENvLIGALgstpfwrTCFSWFTGEQKQ-RALQALTRVGMVHFAHQRVSTL 153
Cdd:PRK10895 67 IsllplhARARRGIGYLPQEASIFRRLSVYDN-LMAVL-------QIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESA---RIVMDTLRDinqnDGITVVVTLHQVDYALRYCERIVALRQGH 230
Cdd:PRK10895 139 SGGERRRVEIARALAANPKFILLDEPFAGVDPISVidiKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGH 214
|
250 260
....*....|....*....|
gi 985002877 231 VFYDGSSQQ-FDNERFDHLY 249
Cdd:PRK10895 215 LIAHGTPTEiLQDEHVKRVY 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-212 |
3.26e-27 |
|
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: 103.98 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREgrlaRDIRKSRAHtgYIFQQFNLV 98
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL---RPDSGEVRWNGTPLAEQ----RDEPHENIL--YLGHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 99 NRLSVLENVligalgstPFWRTcfswFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
Cdd:TIGR01189 86 PELSALENL--------HFWAA----IHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|....
gi 985002877 179 PIASLDPESARIVMDTLRDINQNDGItVVVTLHQ 212
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGI-VLLTTHQ 186
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-245 |
4.14e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.46 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFN--QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREgrlar 79
Cdd:PRK13632 5 SVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL---KPQSGEIKIDGITISKE----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKSRAHTGYIFQqfNLVNR---LSV-------LENVLIgalgsTPfwrtcfswftGEQKQRALQALTRVGMVHFAHQR 149
Cdd:PRK13632 77 NLKEIRKKIGIIFQ--NPDNQfigATVeddiafgLENKKV-----PP----------KKMKDIIDDLAKKVGMEDYLDKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQG 229
Cdd:PRK13632 140 PQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEG 218
|
250
....*....|....*..
gi 985002877 230 HVFYDGSSQQ-FDNERF 245
Cdd:PRK13632 219 KLIAQGKPKEiLNNKEI 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-245 |
5.29e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.47 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQ-----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT--------GDKSVGSHIELLGRT 70
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKskygtiqvGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 71 VQREGRLARDIRKSRAHTGYIFQ--QFNLVnRLSVLENVLIG--ALGSTPFwrtcfswftgEQKQRALQALTRVGMVH-F 145
Cdd:PRK13631 101 TNPYSKKIKNFKELRRRVSMVFQfpEYQLF-KDTIEKDIMFGpvALGVKKS----------EAKKLAKFYLNKMGLDDsY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 146 AHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVA 225
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIV 248
|
250 260
....*....|....*....|.
gi 985002877 226 LRQGHVFYDGSSQQ-FDNERF 245
Cdd:PRK13631 249 MDKGKILKTGTPYEiFTDQHI 269
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-212 |
9.24e-27 |
|
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: 103.50 E-value: 9.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRtvqregrlARDIRKSRAHTGYIFQQFNL 97
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQ--------PRKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRLSVLENVLIGALGSTPfwrtcfSWFTGEQKQR--ALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
Cdd:cd03234 93 LPGLTVRETLTYTAILRLP------RKSSDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 985002877 176 ADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQ 212
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRI-VILTIHQ 202
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-226 |
9.39e-27 |
|
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: 108.14 E-value: 9.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvgshiellGRTVQREGRLARDIRKS--RAHTGYIFQQFN 96
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT----------EGSIAVNGVPLADADADswRDQIAWVPQHPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 LVNRlSVLENVLIGALGSTPfwrtcfswftgEQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALM 168
Cdd:TIGR02857 407 LFAG-TIAENIRLARPDASD-----------AEIREALERAGLDEFVAALPQGLDTpigeggagLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 169 QQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRyCERIVAL 226
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
8-239 |
2.09e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 107.44 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 8 EKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRtvqregrlARDIRKSRAH 87
Cdd:TIGR00955 29 GCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGM--------PIDAKEMRAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 88 TGYIFQQFNLVNRLSVLENVLIGALgstpfWRTCFSWFTGEQKQRALQALTRVGMVHFAH------QRVSTLSGGQQQRV 161
Cdd:TIGR00955 101 SAYVQQDDLFIPTLTVREHLMFQAH-----LRMPRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALrYC--ERIVALRQGHVFYDGSSQQ 239
Cdd:TIGR00955 176 AFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSSEL-FElfDKIILMAEGRVAYLGSPDQ 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-231 |
2.23e-26 |
|
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: 106.83 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlITGDKSVGSHIELLGRTVQregrlARDIRK 83
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGTWDGEIYWSGSPLK-----ASNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 S-RAHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSwftgEQKQRALQALTRVGMVHFAHQR-VSTLSGGQQQRV 161
Cdd:TIGR02633 75 TeRAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYN----AMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG-HV 231
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGqHV 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-244 |
6.13e-26 |
|
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: 101.45 E-value: 6.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 6 RVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdkSVGShIELLGRTVQRegrlARDIRKSR 85
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPV--KSGS-IRLDGEDITK----LPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 86 AHTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTGEQKQRALQALTRVGMVH-FAHQRVSTLSGGQQQRVAIA 164
Cdd:TIGR03410 75 AGIAYVPQGREIFPRLTVEENLLTG-----------LAALPRRSRKIPDEIYELFPVLKeMLGRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNER 244
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-229 |
9.70e-26 |
|
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: 100.24 E-value: 9.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDksvgshIELLGRTVQREGRLArdirksrahtgYIFQQFNLV 98
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLS----ALLGE------LEKLSGSVSVPGSIA-----------YVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 99 NRlSVLENVLIGAlgstPFwrtcfswftGEQK-QRALQA--------------LTRVGmvhfahQRVSTLSGGQQQRVAI 163
Cdd:cd03250 79 NG-TIRENILFGK----PF---------DEERyEKVIKAcalepdleilpdgdLTEIG------EKGINLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 164 ARALMQQAKVILADEPIASLDPESAR-IVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQG 229
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNNKTRILVT-HQLQL-LPHADQIVVLDNG 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-236 |
1.51e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.73 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQH-----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSVGShIELLGRTVQREg 75
Cdd:PRK13643 1 MIKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpteGKVTVGD-IVVSSTSKQKE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 76 rlardIRKSRAHTGYIFQ--QFNLVNRlSVLENVLIGALGstpfwrtcFSWFTGEQKQRALQALTRVGMV-HFAHQRVST 152
Cdd:PRK13643 79 -----IKPVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQN--------FGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPEsARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK-ARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
....
gi 985002877 233 YDGS 236
Cdd:PRK13643 224 SCGT 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-231 |
2.37e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVgshIELLGRTVQREGRlARDIRKSRAHTGYIFQ-- 93
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGT---ITIAGYHITPETG-NKNLKKLRKKVSLVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 94 QFNLVNRlSVLENVLIGALGstpfwrtcFSWFTGEQKQRALQALTRVGMVH-FAHQRVSTLSGGQQQRVAIARALMQQAK 172
Cdd:PRK13641 95 EAQLFEN-TVLKDVEFGPKN--------FGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 173 VILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:PRK13641 166 ILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-244 |
2.58e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 101.70 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQ---------------------ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGS 62
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPT---SG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 63 HIELLGRT-VQREGRLARDIrksrahtGYIFQQfnlvnR------LSVLEN-VLIGALGSTPfwrtcfswfTGEQKQRaL 134
Cdd:COG4586 78 EVRVLGYVpFKRRKEFARRI-------GVVFGQ-----RsqlwwdLPAIDSfRLLKAIYRIP---------DAEYKKR-L 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 135 QALTRV-GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQV 213
Cdd:COG4586 136 DELVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDM 215
|
250 260 270
....*....|....*....|....*....|....*..
gi 985002877 214 D--YALryCERIVALRQGHVFYDGS----SQQFDNER 244
Cdd:COG4586 216 DdiEAL--CDRVIVIDHGRIIYDGSleelKERFGPYK 250
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-243 |
3.40e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.83 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQREGRLARdirks 84
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG---KITVLGVPVPARARLAR----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 rAHTGYIFQQFNLVNRLSVLENVLIgalgstpFWRTCfswftgEQKQRALQALTRvGMVHFAH------QRVSTLSGGQQ 158
Cdd:PRK13536 114 -ARIGVVPQFDNLDLEFTVRENLLV-------FGRYF------GMSTREIEAVIP-SLLEFARleskadARVSDLSGGMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPH 257
|
....*
gi 985002877 239 QFDNE 243
Cdd:PRK13536 258 ALIDE 262
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-184 |
4.23e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.77 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSVGShIELLGRTVQREGrlardirk 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP--YQHGS-ITLDGKPVEGPG-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 srAHTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
Cdd:PRK11248 70 --AERGVVFQNEGLLPWRNVQDNVAFGlQLAGVE---------KMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVG 138
|
170 180
....*....|....*....|..
gi 985002877 163 IARALMQQAKVILADEPIASLD 184
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALD 160
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-235 |
4.91e-25 |
|
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: 98.82 E-value: 4.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL-ITGDKSVgshieLLGRTVQREGRLArDIRKsraHTGYIFQQ 94
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSV-----LLDGTDIRQLDPA-DLRR---NIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 FNLVNRlSVLENVLIGALGSTpfwrtcfswftgeqKQRALQALTRVGMVHFAHQ-----------RVSTLSGGQQQRVAI 163
Cdd:cd03245 87 VTLFYG-TLRDNITLGAPLAD--------------DERILRAAELAGVTDFVNKhpngldlqigeRGRGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLR--QLLGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-239 |
6.99e-25 |
|
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: 102.96 E-value: 6.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL----------------------ITGDKSVGS 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvalcekcgyVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 63 HIELLGRTVQRE--------GRLARDIRKSRAhtgYIFQQ-FNLVNRLSVLENVL-----IGALGStpfwrtcfswftgE 128
Cdd:TIGR03269 81 PCPVCGGTLEPEevdfwnlsDKLRRRIRKRIA---IMLQRtFALYGDDTVLDNVLealeeIGYEGK-------------E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 129 QKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVV 208
Cdd:TIGR03269 145 AVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVL 224
|
250 260 270
....*....|....*....|....*....|.
gi 985002877 209 TLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:TIGR03269 225 TSHWPEVIEDLSDKAIWLENGEIKEEGTPDE 255
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-244 |
7.68e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 7.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQreGRLARD 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFY---KPTGGTILLRGQHIE--GLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 I-RKSRAHTgyiFQQFNLVNRLSVLENVLI-----------GALGSTPFWRTCfswfTGEQKQRALQALTRVGMVHFAHQ 148
Cdd:PRK11300 77 IaRMGVVRT---FQHVRLFREMTVIENLLVaqhqqlktglfSGLLKTPAFRRA----ESEALDRAATWLERVGLLEHANR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQ 229
|
250
....*....|....*..
gi 985002877 229 GHVFYDGSSQQF-DNER 244
Cdd:PRK11300 230 GTPLANGTPEEIrNNPD 246
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-257 |
8.58e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.85 E-value: 8.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSVGShIELLGRTVQREgrlardIRKSRAHTGYIF 92
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkptTGTVTVDD-ITITHKTKDKY------IRPVRKRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 93 Q--QFNLVNRlSVLENVLIGALGstpfwrtcFSWFTGEQKQRALQALTRVGmvhFAHQRVST----LSGGQQQRVAIARA 166
Cdd:PRK13646 92 QfpESQLFED-TVEREIIFGPKN--------FKMNLDEVKNYAHRLLMDLG---FSRDVMSQspfqMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQfdnerfd 246
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE------- 232
|
250
....*....|.
gi 985002877 247 hLYRSINRVEE 257
Cdd:PRK13646 233 -LFKDKKKLAD 242
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
15-239 |
1.62e-24 |
|
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: 102.25 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShiellgrtVQREGRLARDIRKS--RAHTGYIF 92
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTE--GS--------VLLDGVDIRQIDPAdlRRNIGYVP 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 93 QQfnlvNRL---SVLENVLIGALGSTpfwrtcfswftgeqKQRALQALTRVGMVHFA-----------HQRVSTLSGGQQ 158
Cdd:TIGR03375 546 QD----PRLfygTLRDNIALGAPYAD--------------DEEILRAAELAGVTEFVrrhpdgldmqiGERGRSLSGGQR 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQ 238
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTS-LLDLVDRIIVMDNGRIVADGPKD 684
|
.
gi 985002877 239 Q 239
Cdd:TIGR03375 685 Q 685
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
1.66e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.49 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksVGShIELLGRTVQREGRLARd 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD--AGS-ISLCGEPVPSRARHAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 irksrAHTGYIFQQFNLVNRLSVLENVLIgalgstpFWRTcFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
Cdd:PRK13537 80 -----QRVGVVPQFDNLDPDFTVRENLLV-------FGRY-FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-184 |
1.73e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.81 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTF--------NQHQALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSVGShIELLGR 69
Cdd:COG4608 4 AEPLLEVRDLKKHFpvrgglfgRTVGVVKAVDgvsFDIRRGETLGLVGESGCGKSTLGRLLLRLE--EPTSGE-ILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 70 TVQREGRlaRDIRKSRAHTGYIFQQ-FNLVN-RLSV----LENVLIGALGSTpfwrtcfswftGEQKQRALQALTRVG-- 141
Cdd:COG4608 81 DITGLSG--RELRPLRRRMQMVFQDpYASLNpRMTVgdiiAEPLRIHGLASK-----------AERRERVAELLELVGlr 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 985002877 142 ---MVHFAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
Cdd:COG4608 148 pehADRYPHE----FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-242 |
1.83e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.99 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI--TGDKSVGSHIELLGRTVQREGRLA 78
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelNEEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 79 RDIRKsraHTGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRTcfswfTGEQKQRALQALTRVGMVHFAHQRV----STLS 154
Cdd:PRK14267 81 IEVRR---EVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKS-----KKELDERVEWALKKAALWDEVKDRLndypSNLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
|
....*....
gi 985002877 235 GSSQQ-FDN 242
Cdd:PRK14267 230 GPTRKvFEN 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-238 |
1.99e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 98.42 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGRlar 79
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV---RLASGKISILGQPTRQALQ--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 dirksRAHTGYIFQQFNLVNRLSVL--ENVLIGALGSTPFWRTCfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
Cdd:PRK15056 77 -----KNLVAYVPQSEEVDWSFPVLveDVVMMGRYGHMGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRqGHVFYDGSS 237
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPT 225
|
.
gi 985002877 238 Q 238
Cdd:PRK15056 226 E 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-243 |
2.60e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.58 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQ-----HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGRLAR 79
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL---KPTSGKIIIDGVDITDKKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKSrahTGYIFQ--QFNLVNRlSVLENVLIGA--LGSTpfwrtcfswfTGEQKQRALQALTRVGMVH--FAHQRVSTL 153
Cdd:PRK13637 80 DIRKK---VGLVFQypEYQLFEE-TIEKDIAFGPinLGLS----------EEEIENRVKRAMNIVGLDYedYKDKSPFEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCEL 225
|
250
....*....|
gi 985002877 234 DGSSQQFDNE 243
Cdd:PRK13637 226 QGTPREVFKE 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-239 |
3.59e-24 |
|
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: 96.84 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 16 QHQALHAVDLNIHHGEMVALLGPSGSGKST----LLRH---LSGLITGDksvGSHIELLgrtvqregrlarDIRKSRAHT 88
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERFydpTSGEILLD---GVDIRDL------------NLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 89 GYIFQQFNLVNRlSVLENVLIGALGSTpfwrtcfswfTGEQKQRALQAL-------------TRVGmvhfahQRVSTLSG 155
Cdd:cd03249 80 GLVSQEPVLFDG-TIAENIRYGKPDAT----------DEEVEEAAKKANihdfimslpdgydTLVG------ERGSQLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQG 219
|
....
gi 985002877 236 SSQQ 239
Cdd:cd03249 220 THDE 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-212 |
4.22e-24 |
|
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: 100.51 E-value: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSVGShIELLGRTVQ--REGRLARDIR--KSRAHtgyIFQQ 94
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL--DPLQGE-VTLDGVPVSslDQDEVRRRVSvcAQDAH---LFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 fnlvnrlSVLENVLIGALGSTPfwrtcfswftgeqkQRALQALTRVGMVHFA-----------HQRVSTLSGGQQQRVAI 163
Cdd:TIGR02868 424 -------TVRENLRLARPDATD--------------EELWAALERVGLADWLralpdgldtvlGEGGARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQ 212
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-231 |
4.28e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 99.33 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--IT-GDKSVGshiellgrtvqreGRLARDIRKSRAHTGYIFQQFNLVN 99
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLedITsGDLFIG-------------EKRMNDVPPAERGVGMVFQSYALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENVLIG-ALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
Cdd:PRK11000 89 HLSVAENMSFGlKLAGAK---------KEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 179 PIASLDPeSARIVMDT-LRDINQNDGITVV-VTLHQVDyALRYCERIVALRQGHV 231
Cdd:PRK11000 160 PLSNLDA-ALRVQMRIeISRLHKRLGRTMIyVTHDQVE-AMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-239 |
4.67e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.51 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSVGSHIelLGRTVQREGRLARDIRKSRAHTGYIFQqF--N 96
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHV--PTQGSVR--VDDTLITSTSKNKDIKQIRKKVGLVFQ-FpeS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 LVNRLSVLENVLIGALGstpfwrtcFSWFTGEQKQRALQALTRVGMVH-FAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
Cdd:PRK13649 97 QLFEETVLKDVAFGPQN--------FGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 176 ADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-249 |
4.76e-24 |
|
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: 96.79 E-value: 4.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvgshiellGRTVQREGRLAR-DIRKSRAHTGYIFQQFNL 97
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEN---------GRVLVDGHDLALaDPAWLRRQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRlSVLENVligALGSTpfwrtcfswftGEQKQRALQALTRVGMVHFAHQ-----------RVSTLSGGQQQRVAIARA 166
Cdd:cd03252 88 FNR-SIRDNI---ALADP-----------GMSMERVIEAAKLAGAHDFISElpegydtivgeQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 167 LMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF--DNER 244
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELlaENGL 229
|
....*
gi 985002877 245 FDHLY 249
Cdd:cd03252 230 YAYLY 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-254 |
5.55e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.34 E-value: 5.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSV----GSHIELLGRTVQREGRlardirksRAHTGYIFQQFNLVNR 100
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQvlidGVDIAKISDAELREVR--------RKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 101 LSVLENVLIG-ALGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
Cdd:PRK10070 121 MTVLDNTAFGmELAGIN---------AEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRSINR 254
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-229 |
9.59e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.60 E-value: 9.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQ-REGRLAR 79
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD---AGSILIDGQEMRfASTTAAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DirksrAHTGYIFQQFNLVNRLSVLENVLIGALGSTpfwrtcFSWFTGEQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:PRK11288 78 A-----AGVAIIYQELHLVPEMTVAENLYLGQLPHK------GGIVNRRLlNYEAREQLEHLGVDIDPDTPLKYLSIGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLD-PESARI--VMDTLRDinqnDGITVVVTLHQVDYALRYCERIVALRQG 229
Cdd:PRK11288 147 QMVEIAKALARNARVIAFDEPTSSLSaREIEQLfrVIRELRA----EGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-185 |
1.81e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 95.67 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQH---------QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSVGSHIELLG 68
Cdd:COG4167 1 MSALLEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEptsGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 69 RTVQRegrlARDIRksrahtgYIFQQFN--LVNRLSvlenvlIGALGSTPFWR-TCFSwfTGEQKQRALQALTRVGMV-- 143
Cdd:COG4167 81 DYKYR----CKHIR-------MIFQDPNtsLNPRLN------IGQILEEPLRLnTDLT--AEEREERIFATLRLVGLLpe 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 985002877 144 HfAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDP 185
Cdd:COG4167 142 H-ANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDM 182
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-231 |
1.86e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.95 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQ---ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQREGrl 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG---QIIIDGDLLTEEN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 78 ARDIRKsraHTGYIFQqfNLVNRL---SVLENVLIGaLGSTPFWRTcfswftgEQKQRALQALTRVGMVHFAHQRVSTLS 154
Cdd:PRK13650 76 VWDIRH---KIGMVFQ--NPDNQFvgaTVEDDVAFG-LENKGIPHE-------EMKERVNEALELVGMQDFKEREPARLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVD-YALRycERIVALRQGHV 231
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDeVALS--DRVLVMKNGQV 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-236 |
2.25e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGsHIElLGRTVQregrlardir 82
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDS--G-TVK-LGETVK---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 ksrahTGYIFQ-QFNLVNRLSVLENVLigalgstpfwrtcfSWFTGEQKQRALQALTRVGmvhF----AHQRVSTLSGGQ 157
Cdd:COG0488 380 -----IGYFDQhQEELDPDKTVLDELR--------------DGAPGGTEQEVRGYLGRFL---FsgddAFKPVGVLSGGE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGiTVVVTLHqvD-YAL-RYCERIVALRQGHV-FYD 234
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF---PG-TVLLVSH--DrYFLdRVATRILEFEDGGVrEYP 511
|
..
gi 985002877 235 GS 236
Cdd:COG0488 512 GG 513
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-239 |
2.86e-23 |
|
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: 94.21 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVgshIELLGRTVqregrlaRDIRKS--RAHTGYIF 92
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQ---ILIDGIDI-------RDISRKslRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 93 QQFNLVNRlSVLENVLIGALGSTpfwrtcfswftgeqKQRALQALTRVGMVHF-----------AHQRVSTLSGGQQQRV 161
Cdd:cd03254 84 QDTFLFSG-TIMENIRLGRPNAT--------------DEEVIEAAKEAGAHDFimklpngydtvLGENGGNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDE 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-231 |
3.02e-23 |
|
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: 92.66 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGRLARdirksRAHTGYIFQQ 94
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL---RPTSGRVRLDGADISQWDPNEL-----GDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 FNLVNRlSVLENVLigalgstpfwrtcfswftgeqkqralqaltrvgmvhfahqrvstlSGGQQQRVAIARALMQQAKVI 174
Cdd:cd03246 85 DELFSG-SIAENIL---------------------------------------------SGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDyALRYCERIVALRQGHV 231
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIA-HRPE-TLASADRILVLEDGRV 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-242 |
3.68e-23 |
|
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: 97.83 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGShIELLGRTVQREGRlaRDIRKSRAHTG 89
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI---PSEGE-IRFDGQDLDGLSR--RALRPLRRRMQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 90 YIFQQ-FNLVN-RLSVLENV----LIGALGSTPfwrtcfswftGEQKQRALQALTRVG----MVH-FAHQrvstLSGGQQ 158
Cdd:COG4172 366 VVFQDpFGSLSpRMTVGQIIaeglRVHGPGLSA----------AERRARVAEALEEVGldpaARHrYPHE----FSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDpES--ARIVmDTLRDINQNDGITVVVTLH--QVDYALryCERIVALRQGHVFYD 234
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALD-VSvqAQIL-DLLRDLQREHGLAYLFISHdlAVVRAL--AHRVMVMKDGKVVEQ 507
|
....*....
gi 985002877 235 GSSQQ-FDN 242
Cdd:COG4172 508 GPTEQvFDA 516
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-235 |
4.37e-23 |
|
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: 93.94 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQ---------------------ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSV 60
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQptsGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 61 GSHIELlgrtvQREGRLARDIrksrahtGYIFQQFN-LVNRLSVLEnvligalgSTPFWRTCFSWFTGEQKQR--ALQAL 137
Cdd:cd03267 81 AGLVPW-----KRRKKFLRRI-------GVVFGQKTqLWWDLPVID--------SFYLLAAIYDLPPARFKKRldELSEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 138 TRVGmvHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAL 217
Cdd:cd03267 141 LDLE--ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIE 218
|
250
....*....|....*...
gi 985002877 218 RYCERIVALRQGHVFYDG 235
Cdd:cd03267 219 ALARRVLVIDKGRLLYDG 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-243 |
5.16e-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: 5.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSVGSHIELLGRTVQrEGRLARD 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG---DPRATSGRIVFDGKDIT-DWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAhtgYIFQQFNLVNRLSVLENVLIGALGStpfwrtcfswftgeQKQRALQALTRV-----GMVHFAHQRVSTLSG 155
Cdd:PRK11614 78 MREAVA---IVPEGRRVFSRMTVEENLAMGGFFA--------------ERDQFQERIKWVyelfpRLHERRIQRAGTMSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGH-VFYD 234
Cdd:PRK11614 141 GEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHvVLED 219
|
....*....
gi 985002877 235 GSSQQFDNE 243
Cdd:PRK11614 220 TGDALLANE 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-231 |
7.56e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 7.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVqreGRLARDIRKS-RAHTGYIFQQ- 94
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL---ESPSQGNVSWRGEPL---AKLNRAQRKAfRRDIQMVFQDs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 FNLVN-RLSVlenvliGALGSTPFwRTCFSWFTGEQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQAK 172
Cdd:PRK10419 99 ISAVNpRKTV------REIIREPL-RHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 173 VILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-236 |
7.91e-23 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 94.12 E-value: 7.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKS-----VGSHIELLGRTVQR--EGR 76
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAprgarVTGDVTLNGEPLAAidAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 77 LA--RDIRKSRAHTGYIFqqfnlvnrlSVLENVLigaLGSTPFWRTcfswfTGEQKQR----ALQALTRVGMVHFAHQRV 150
Cdd:PRK13547 81 LArlRAVLPQAAQPAFAF---------SAREIVL---LGRYPHARR-----AGALTHRdgeiAWQALALAGATALVGRDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 151 STLSGGQQQRVAIARALMQ---------QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCE 221
Cdd:PRK13547 144 TTLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHAD 223
|
250
....*....|....*
gi 985002877 222 RIVALRQGHVFYDGS 236
Cdd:PRK13547 224 RIAMLADGAIVAHGA 238
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-239 |
1.68e-22 |
|
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: 92.29 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITG--DKSVGShIELLGRTVqregrlaRDIRKS--RAHTGYIFQQ 94
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVN----LIPRfyDVDSGR-ILIDGHDV-------RDYTLAslRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 FNLVNRlSVLENVLIGALGSTPfwrtcfswftgEQKQRALQAL--------------TRVGmvhfahQRVSTLSGGQQQR 160
Cdd:cd03251 85 VFLFND-TVAENIAYGRPGATR-----------EEVEEAARAAnahefimelpegydTVIG------ERGVKLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEE 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-236 |
3.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.94 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRTVQregrlARDI 81
Cdd:PRK13640 5 IVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLT-----AKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKSRAHTGYIFQqfNLVNRL---SVLENVLIGaLGSTPFWRTcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:PRK13640 80 WDIREKVGIVFQ--NPDNQFvgaTVGDDVAFG-LENRAVPRP-------EMIKIVRDVLADVGMLDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHVFYDGS 236
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGS 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-243 |
5.20e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.91 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSG--------LITGdksvgshIELlgrtvqregrlaRDIRKS--RAHTGYIF 92
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslKING-------IEL------------RELDPEswRKHLSWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 93 QQFNLVNRlSVLENVLIGALGSTPfwrtcfswftgeqkQRALQALTRVGMVHFAHQ-----------RVSTLSGGQQQRV 161
Cdd:PRK11174 430 QNPQLPHG-TLRDNVLLGNPDASD--------------EQLQQALENAWVSEFLPLlpqgldtpigdQAAGLSVGQAQRL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgITVVVTlHQVDyALRYCERIVALRQGHVFYDGSSQQFD 241
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ-TTLMVT-HQLE-DLAQWDQIWVMQDGQIVQQGDYAELS 571
|
..
gi 985002877 242 NE 243
Cdd:PRK11174 572 QA 573
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-213 |
8.69e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 91.25 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSVGSHIELLGRTVQrEGRLarDIR 82
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMneLESEVRVEGRVEFFNQNIY-ERRV--NLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KSRAHTGYIFQQFNLVNrLSVLENVLIGA--LGstpfWRTCFSwfTGEQKQRALQALTRVGMV-HFAHQRVSTLSGGQQQ 159
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYGVkiVG----WRPKLE--IDDIVESALKDADLWDEIkHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 985002877 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQV 213
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNL 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-231 |
1.04e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 89.03 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQRegRLARDIRKS--------RAHTGy 90
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGL---RPPASGEITLDGKPVTR--RSPRDAIRAgiayvpedRKREG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 91 ifqqfnLVNRLSVLENVLIGALgstpfwrtcfswftgeqkqralqaltrvgmvhfahqrvstLSGGQQQRVAIARALMQQ 170
Cdd:cd03215 89 ------LVLDLSVAENIALSSL----------------------------------------LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 985002877 171 AKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-238 |
1.38e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvgshiellGRTVQReGRLARDIR 82
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQK---------GKVLVS-GIDTGDFS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 K---SRAHTGYIFQ--QFNLVNRlSVLENVLIGA--LGSTPFwrtcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSG 155
Cdd:PRK13644 71 KlqgIRKLVGIVFQnpETQFVGR-TVEEDLAFGPenLCLPPI----------EIRKRVDRALAEIGLEKYRHRSPKTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
Cdd:PRK13644 140 GQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEG 217
|
...
gi 985002877 236 SSQ 238
Cdd:PRK13644 218 EPE 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-231 |
1.64e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.83 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITgdksvGSHIELLGRTV-QREGRlARD 80
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLerIT-----SGEIWIGGRVVnELEPA-DRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IrksrahtGYIFQQFNLVNRLSVLENVligALG----STPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGG 156
Cdd:PRK11650 78 I-------AMVFQNYALYPHMSVRENM---AYGlkirGMP---------KAEIEERVAEAARILELEPLLDRKPRELSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDpesA--RIVMDT-LRDINQNDGIT-VVVTLHQVDyALRYCERIVALRQGHV 231
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLD---AklRVQMRLeIQRLHRRLKTTsLYVTHDQVE-AMTLADRVVVMNGGVA 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-231 |
1.90e-21 |
|
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: 92.83 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQ----HQALHAVDLNIHHGEMVALLGPSGSGKS----TLLRHLSGlitGDKSVGSHIELLGRTVQ 72
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPD---PAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 73 R--EGRLaRDIRKSRAhtGYIFQQ--------FNLVNRLS-VLEnvLIGALGSTpfwrtcfswftgEQKQRALQALTRVG 141
Cdd:COG4172 80 GlsEREL-RRIRGNRI--AMIFQEpmtslnplHTIGKQIAeVLR--LHRGLSGA------------AARARALELLERVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 142 -------MVHFAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHqvD 214
Cdd:COG4172 143 ipdperrLDAYPHQ----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH--D 216
|
250
....*....|....*....
gi 985002877 215 YAL--RYCERIVALRQGHV 231
Cdd:COG4172 217 LGVvrRFADRVAVMRQGEI 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-218 |
2.08e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.23 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLR---HLSGLITGDKSVGSHI----ELLGRTVqre 74
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGFRVEGKVTfhgkNLYAPDV--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 75 grlarDIRKSRAHTGYIFQQFNLVNRlSVLENVLIGALgstpfwrtcFSWFTG---EQKQRAL-QALTRVGMVHFAHQRV 150
Cdd:PRK14243 85 -----DPVEVRRRIGMVFQKPNPFPK-SIYDNIAYGAR---------INGYKGdmdELVERSLrQAALWDEVKDKLKQSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALR 218
Cdd:PRK14243 150 LSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
2.18e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGRLAR-D 80
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLI---EIYDSKIKVDGKVLYFGKDIFQiD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIFQQFNLVNRLSVLENVligalgSTPFwRTCFSWFTGEQKQRALQALTRVGMVHFAHQRV----STLSGG 156
Cdd:PRK14246 85 AIKLRKEVGMVFQQPNPFPHLSIYDNI------AYPL-KSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspaSQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
...
gi 985002877 237 SQQ 239
Cdd:PRK14246 236 SNE 238
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-212 |
2.50e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 30 GEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRtvqregrlARDIRKSRAHTGYIFQQFNLVNRLSVLENVLi 109
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLL---PPAAGTIKLDGG--------DIDDPDVAEACHYLGHRNAMKPALTVAENLE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 110 galgstpFWRTCFswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESAR 189
Cdd:PRK13539 96 -------FWAAFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|...
gi 985002877 190 IVMDTLRDINQNDGITVVVTlHQ 212
Cdd:PRK13539 165 LFAELIRAHLAQGGIVIAAT-HI 186
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-211 |
3.41e-21 |
|
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: 88.61 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQRegrlaRDIRKs 84
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSG---EIIFDGHPWTR-----KDLHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 rahTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcfswFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:TIGR03740 72 ---IGSLIESPPLYENLTARENLKVHTT------------LLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIA 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 985002877 165 RALMQQAKVILADEPIASLDPesarIVMDTLRDINQN---DGITVVVTLH 211
Cdd:TIGR03740 137 IALLNHPKLLILDEPTNGLDP----IGIQELRELIRSfpeQGITVILSSH 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-212 |
4.61e-21 |
|
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: 87.93 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQREgrlaRDIRKSRAHtgYIFQQFNLVNRLS 102
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG---RVLLNGGPLDFQ----RDSIARGLL--YLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 103 VLENVligalgstPFWRTCFSwftgeqKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
Cdd:cd03231 90 VLENL--------RFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|
gi 985002877 183 LDPESARIVMDTLRDINQNDGItVVVTLHQ 212
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGM-VVLTTHQ 184
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-240 |
6.37e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.00 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 14 FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSVGShIELLGRTVQRegrlARDIRKSRAHTGY 90
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkVSGYRYSGD-VLLGGRSIFN----YRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 91 IFQQFNLVNrLSVLENVLIGALGSTPFWRtcfSWFTGEQKQRalqaLTRVGMVHFAHQRVST----LSGGQQQRVAIARA 166
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKLVPR---KEFRGVAQAR----LTEVGLWDAVKDRLSDspfrLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 167 LMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-214 |
1.01e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 87.32 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 6 RVEKLAKTFN------QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGShIELLGRTVQREGRLAR 79
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC-VDVPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIrksrahtgYIFQQFNLVnrLSVLENVligALGSTPFWRTCFSwftgeqkqralqaltrvgmvhfahqrvsTLSGGQQQ 159
Cdd:COG2401 105 AI--------GRKGDFKDA--VELLNAV---GLSDAVLWLRRFK----------------------------ELSTGQKF 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVD 214
Cdd:COG2401 144 RFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-238 |
1.63e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.88 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSVGShiellGRTVQREGRL-ARDIRKSRAHTGYIFQQfnl 97
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAK----LMIGIEKVKS-----GEIFYNNQAItDDNFEKLRKHIGIVFQN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 vnrlsvLENVLIGALGS--TPFWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
Cdd:PRK13648 92 ------PDNQFVGSIVKydVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 176 ADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQ 238
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-231 |
2.31e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 3 TIIRVEKL-AKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQREGRlaRDI 81
Cdd:COG3845 256 VVLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS--GS-IRLDGEDITGLSP--RER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKS--------RAHTGyifqqfnLVNRLSVLENVLIGALGSTPFWRtcFSWFtgeqKQRALQALTRVGMVHF------AH 147
Cdd:COG3845 331 RRLgvayipedRLGRG-------LVPDMSVAENLILGRYRRPPFSR--GGFL----DRKAIRAFAEELIEEFdvrtpgPD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALR 227
Cdd:COG3845 398 TPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMY 476
|
....
gi 985002877 228 QGHV 231
Cdd:COG3845 477 EGRI 480
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-239 |
2.33e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKST----LLRHLSglitgdkSVGShIELLGRTVQREGRlaRD 80
Cdd:PRK15134 287 IRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-------SQGE-IWFDGQPLHNLNR--RQ 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIFQQFN--LVNRLSVLENVLIGALGSTPfwrtcfSWFTGEQKQRALQALTRVGMVHFAHQRV-STLSGGQ 157
Cdd:PRK15134 357 LLPVRHRIQVVFQDPNssLNPRLNVLQIIEEGLRVHQP------TLSAAQREQQVIAVMEEVGLDPETRHRYpAEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDC 510
|
..
gi 985002877 238 QQ 239
Cdd:PRK15134 511 ER 512
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-229 |
3.08e-20 |
|
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: 89.48 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTF-----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKS-----VGSH-IELLGRTVQ 72
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrVGDEwVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 73 REGRLARDIrksrahtGYIFQQFNLVNRLSVLENvLIGALG-STPFWRTcfswftgeqKQRALQALTRVGM-----VHFA 146
Cdd:TIGR03269 359 GRGRAKRYI-------GILHQEYDLYPHRTVLDN-LTEAIGlELPDELA---------RMKAVITLKMVGFdeekaEEIL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
Cdd:TIGR03269 422 DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM 501
|
...
gi 985002877 227 RQG 229
Cdd:TIGR03269 502 RDG 504
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-239 |
6.38e-20 |
|
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: 88.62 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlsglitgdksvgshIELLGRTVQ-REGRLARD--------IRKSRAHTG 89
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTL-----------------VNLIPRFYEpDSGQILLDghdladytLASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 90 YIFQQFNLVNRlSVLENVLIGALGSTPfwrtcfswftGEQKQRALQA--LTRV--GMVHFAHQRV----STLSGGQQQRV 161
Cdd:TIGR02203 410 LVSQDVVLFND-TIANNIAYGRTEQAD----------RAEIERALAAayAQDFvdKLPLGLDTPIgengVLLSGGQRQRL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNE 553
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-239 |
7.07e-20 |
|
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: 88.65 E-value: 7.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQR--EGRLARdirksraHTGYIFQQFNL 97
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW---PPTAGSVRLDGADLSQwdREELGR-------HIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRlSVLENVligalgstpfwrtcfSWFTGEQKQRALQALTRVGmvhfAHQRV---------------STLSGGQQQRVA 162
Cdd:COG4618 418 FDG-TIAENI---------------ARFGDADPEKVVAAAKLAG----VHEMIlrlpdgydtrigeggARLSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-212 |
8.12e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.47 E-value: 8.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 21 HAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQREG-RLARDIRksrahtgYIFQQFNLVN 99
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPD---AGEVLWQGEPIRRQRdEYHQDLL-------YLGHQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENVLIgalgstpfwrtcFSWFTGEQKQRAL-QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
Cdd:PRK13538 88 ELTALENLRF------------YQRLHGPGDDEALwEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....
gi 985002877 179 PIASLDPESARIVMDTLRDINQNDGItVVVTLHQ 212
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQGGM-VILTTHQ 188
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-231 |
1.07e-19 |
|
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: 84.97 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQH-QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDksvgshiellgrtvqregr 76
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGSILID------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 77 lARDIRKS-----RAHTGYIFQQFNLVNRlSVLENVLIGALGSTPfwrtcfswftgEQKQRALQAL-------------- 137
Cdd:cd03253 62 -GQDIREVtldslRRAIGVVPQDTVLFND-TIGYNIRYGRPDATD-----------EEVIEAAKAAqihdkimrfpdgyd 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 138 TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYAL 217
Cdd:cd03253 129 TIVG------ERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIV 200
|
250
....*....|....
gi 985002877 218 RyCERIVALRQGHV 231
Cdd:cd03253 201 N-ADKIIVLKDGRI 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-236 |
1.27e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.44 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 14 FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVgshIELLGRTV--QREGRLARdirksRAHTGYI 91
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGA---VLWQGKPLdySKRGLLAL-----RQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 92 FQQ---------------FNLVNrLSVLENvligalgstpfwrtcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSGG 156
Cdd:PRK13638 83 FQDpeqqifytdidsdiaFSLRN-LGVPEA---------------------EITRRVDEALTLVDAQHFRHQPIQCLSHG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:PRK13638 141 QKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-235 |
1.31e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvgshiellgrtvqrEGRLardIRKSRA 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD----------------SGEV---SIPKGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 87 HTGYIFQQFNLVNRLSVLENVLIGAlgsTPFW-----------RTCFSWFTGEQ----------------KQRALQALTR 139
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLDGD---AELRaleaeleeleaKLAEPDEDLERlaelqeefealggweaEARAEEILSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 140 VGMVHFAHQR-VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndGITVVVTlHqvDyalR 218
Cdd:COG0488 139 LGFPEEDLDRpVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP---GTVLVVS-H--D---R 209
|
250 260
....*....|....*....|...
gi 985002877 219 Y-----CERIVALRQGHVF-YDG 235
Cdd:COG0488 210 YfldrvATRILELDRGKLTlYPG 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-235 |
1.39e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.13 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDksvgshIELLGRTVQREGRLARDIRKSRAHT-GYIFQ 93
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLL----QLLTGD------LKPQQGEITLDGVPVSDLEKALSSLiSVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 94 QFNLVNRlSVLENVligalgstpfwrtcfswftGEQkqralqaltrvgmvhfahqrvstLSGGQQQRVAIARALMQQAKV 173
Cdd:cd03247 83 RPYLFDT-TLRNNL-------------------GRR-----------------------FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 985002877 174 ILADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQVdyALRYCERIVALRQGHVFYDG 235
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTL-IWITHHLT--GIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-239 |
2.05e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.85 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREgrlarDIRKSRAHTGYIFQQFN- 96
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL---KPTSGSVLIRGEPITKE-----NIREVRKFVGLVFQNPDd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 LVNRLSVLENVLIGALGstpfwrtcFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
Cdd:PRK13652 90 QIFSPTVEQDIAFGPIN--------LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 177 DEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-243 |
2.27e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQRegrlard 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD---SGTLEIGGNPCAR------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIF---QQFNLVNRLSVLENVLIGALGStpfwrtcfswftgEQKQRALQALTRVGMVHFA-HQRVSTLSGG 156
Cdd:PRK15439 78 LTPAKAHQLGIYlvpQEPLLFPNLSVKENILFGLPKR-------------QASMQKMKQLLAALGCQLDlDSSAGSLEVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:PRK15439 145 DRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
....*..
gi 985002877 237 SQQFDNE 243
Cdd:PRK15439 224 TADLSTD 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-236 |
2.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.06 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSVGSHiellgrTVQREGRLARDIRKSRAHT 88
Cdd:PRK13645 19 KTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiseTGQTIVGDY------AIPANLKKIKEVKRLRKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 89 GYIFQ--QFNLVNRlSVLENVLIGALGstpfwrtcfswfTGEQKQRALQALTRV-GMVHFAHQRVS----TLSGGQQQRV 161
Cdd:PRK13645 93 GLVFQfpEYQLFQE-TIEKDIAFGPVN------------LGENKQEAYKKVPELlKLVQLPEDYVKrspfELSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-236 |
3.47e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTF----------------------NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 59 svgshiellGRtVQREGRLArdirksrA----HTGyifqqFNlvNRLSVLENV-LIGA-LGstpfwrtcfswFTGEQKQR 132
Cdd:COG1134 81 ---------GR-VEVNGRVS-------AllelGAG-----FH--PELTGRENIyLNGRlLG-----------LSRKEIDE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 133 ALQ---ALTRVGmvHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVT 209
Cdd:COG1134 126 KFDeivEFAELG--DFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVS 203
|
250 260
....*....|....*....|....*..
gi 985002877 210 lHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:COG1134 204 -HSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-229 |
4.26e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.00 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL-----ITGDksvgshIELLGRTVQregrlARDIRKSRA 86
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsYEGE------ILFDGEVCR-----FKDIRDSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 87 HtGY--IFQQFNLVNRLSVLENVLigaLGSTPFWRTCFSWftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
Cdd:NF040905 78 L-GIviIHQELALIPYLSIAENIF---LGNERAKRGVIDW--NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG 229
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-184 |
7.06e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.24 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvgshiellgRTVQREGRLard 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE----------GVIKRNGKL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 irksraHTGYIFQQFNLVNRLsvlenvligALGSTPFWRTcfswFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
Cdd:PRK09544 68 ------RIGYVPQKLYLDTTL---------PLTVNRFLRL----RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQR 128
|
170 180
....*....|....*....|....
gi 985002877 161 VAIARALMQQAKVILADEPIASLD 184
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVD 152
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-239 |
1.14e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 30 GEMVALLGPSGSGKSTLLRHLSGLITGDksvGShIELLGRTVQ--REGRLARdirksraHTGYIFQQFNLVNRLSVLENV 107
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAGLLPGQ---GE-ILLNGRPLSdwSAAELAR-------HRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 108 LIGALGSTPfwrtcfswftGEQKQRALQALT-RVGMVHFAHQRVSTLSGGQQQRVAIARALMQ-------QAKVILADEP 179
Cdd:COG4138 91 ALHQPAGAS----------SEAVEQLLAQLAeALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 180 IASLD--PESArivMDTLrdINQ--NDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:COG4138 161 MNSLDvaQQAA---LDRL--LRElcQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-231 |
1.29e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.28 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK-SV------GSHIELLGRTVQR 73
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAgEVhyrmrdGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 74 EGRLARdirksrAHTGYIFQQFNLVNRLSVLENVLIG----ALGstpfWRtcfswFTGEQKQRALQALTRVgmvHFAHQR 149
Cdd:PRK11701 83 RRRLLR------TEWGFVHQHPRDGLRMQVSAGGNIGerlmAVG----AR-----HYGDIRATAGDWLERV---EIDAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 150 V----STLSGGQQQRVAIARALMQQAKVILADEPIASLDPE-SARIvMDTLRDINQNDGITVVVTLHQVDYALRYCERIV 224
Cdd:PRK11701 145 IddlpTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSvQARL-LDLLRGLVRELGLAVVIVTHDLAVARLLAHRLL 223
|
....*..
gi 985002877 225 ALRQGHV 231
Cdd:PRK11701 224 VMKQGRV 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-235 |
2.49e-18 |
|
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: 81.04 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgshiellgrTVQREGRLARDIrksRAHTGyifqqFN 96
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG----------TVTVRGRVSSLL---GLGGG-----FN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 lvNRLSVLENVLIGA--LGSTpfwRTCFswftgEQKQRALQALTRVGmvHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
Cdd:cd03220 97 --PELTGRENIYLNGrlLGLS---RKEI-----DEKIDEIIEFSELG--DFIDLPVKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 985002877 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDG 235
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVS-HDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-250 |
3.33e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.47 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDksvGSHIellgRTVQREGrLARDIrksrah 87
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILID---GTDI----RTVTRAS-LRRNI------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 88 tGYIFQQFNLVNRlSVLENVLIGALGSTPfwrtcfswftgEQKQRAL---QAL-----------TRVGmvhfahQRVSTL 153
Cdd:PRK13657 412 -AVVFQDAGLFNR-SIEDNIRVGRPDATD-----------EEMRAAAeraQAHdfierkpdgydTVVG------ERGRQL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFY 233
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLS-TVRNADRILVFDNGRVVE 549
|
250 260
....*....|....*....|..
gi 985002877 234 DGSsqqFD-----NERFDHLYR 250
Cdd:PRK13657 550 SGS---FDelvarGGRFAALLR 568
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-242 |
4.07e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.06 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 14 FNQHQALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGrlARDIRKSRAHTGY 90
Cdd:PRK15079 28 WQPPKTLKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLV---KATDGEVAWLGKDLLGMK--DDEWRAVRSDIQM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 91 IFQQ--FNLVNRLSvlenvlIGALGSTPFwRTCFSWFTGEQ-KQRALQALTRVGMV-----HFAHQrvstLSGGQQQRVA 162
Cdd:PRK15079 103 IFQDplASLNPRMT------IGEIIAEPL-RTYHPKLSRQEvKDRVKAMMLKVGLLpnlinRYPHE----FSGGQCQRIG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FD 241
Cdd:PRK15079 172 IARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEvYH 251
|
.
gi 985002877 242 N 242
Cdd:PRK15079 252 N 252
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-239 |
4.87e-18 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 80.65 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRTVQREgRLARDI 81
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELY-QLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKSRAHTGYIFQQFNLVN--RLSVLENVLIG----ALGSTPFwrtcfswftGEQKQRALQALTRVgmvHFAHQRV----S 151
Cdd:TIGR02323 80 RRRLMRTEWGFVHQNPRDglRMRVSAGANIGerlmAIGARHY---------GNIRATAQDWLEEV---EIDPTRIddlpR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
....*...
gi 985002877 232 FYDGSSQQ 239
Cdd:TIGR02323 228 VESGLTDQ 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-240 |
5.77e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.91 E-value: 5.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTFNQH---QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVgshiellgRTVQREGRL 77
Cdd:PRK13642 1 MNKILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGK--------VKIDGELLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 78 ARDIRKSRAHTGYIFQQfnlvnrlsvLENVLIGAL--GSTPFWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSG 155
Cdd:PRK13642 73 AENVWNLRRKIGMVFQN---------PDNQFVGATveDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDG 235
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
....*
gi 985002877 236 SSQQF 240
Cdd:PRK13642 223 APSEL 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-236 |
6.51e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 83.14 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 7 VEKLAKTFNQH--QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSVGshiellGRTVQRegrlarDI 81
Cdd:TIGR01257 931 VKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLpptSGTVLVG------GKDIET------NL 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKSRAHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWrtcfswftgEQKQRALQA-LTRVGMVHFAHQRVSTLSGGQQQR 160
Cdd:TIGR01257 999 DAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW---------EEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRK 1069
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
Cdd:TIGR01257 1070 LSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-231 |
7.21e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.37 E-value: 7.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 3 TIIRVEKLAKtfnqHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQRegrlaRDIR 82
Cdd:COG1129 255 VVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGA---DPADSGEIRLDGKPVRI-----RSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KS-----------RAHTGyifqqfnLVNRLSVLENVLIGALGStpfwrtcFSWF----TGEQKQRALQALTRVGM-VHFA 146
Cdd:COG1129 323 DAiragiayvpedRKGEG-------LVLDLSIRENITLASLDR-------LSRGglldRRRERALAEEYIKRLRIkTPSP 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVT---LHQVdyaLRYCERI 223
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVIsseLPEL---LGLSDRI 464
|
....*...
gi 985002877 224 VALRQGHV 231
Cdd:COG1129 465 LVMREGRI 472
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-231 |
1.44e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 34 ALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRT-VQREGRLARDIRKSRahTGYIFQQFNLVNRLSVLENVLIGAL 112
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKG---RIVLNGRVlFDAEKGICLPPEKRR--IGYVFQDARLFPHYKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 113 GSTPfwrtcfswftgEQKQRALQALtrvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVM 192
Cdd:PRK11144 103 KSMV-----------AQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 985002877 193 DTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-252 |
3.04e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSVGS-HIELLGRTVQ--REGRLardirksRAHTGYI 91
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLTRAWDPQQgEILLNGQPIAdySEAAL-------RQAISVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 92 FQQFNLVNRlSVLENVLIGALGSTpfwrtcfswftgeqKQRALQALTRVGMVHFAHQRVS----------TLSGGQQQRV 161
Cdd:PRK11160 420 SQRVHLFSA-TLRDNLLLAAPNAS--------------DEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVdYALRYCERIVALRQGHVFYDGSSQQF- 240
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELl 561
|
250
....*....|...
gi 985002877 241 -DNERFDHLYRSI 252
Cdd:PRK11160 562 aQQGRYYQLKQRL 574
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-239 |
4.26e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.18 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 16 QHQALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGL------ITGDKSVGSHIELLGRTV-QREGRLARDIrksr 85
Cdd:COG4170 16 PQGRVKAVDrvsLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnwhVTADRFRWNGIDLLKLSPrERRKIIGREI---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 86 ahtGYIFQqfnlvNRLSVL------ENVLIGALGSTPFWRTCFSWFtGEQKQRALQALTRVG-------MVHFAHQrvst 152
Cdd:COG4170 92 ---AMIFQ-----EPSSCLdpsakiGDQLIEAIPSWTFKGKWWQRF-KWRKKRAIELLHRVGikdhkdiMNSYPHE---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
....*..
gi 985002877 233 YDGSSQQ 239
Cdd:COG4170 239 ESGPTEQ 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-239 |
6.80e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.88 E-value: 6.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSV----GSHIELLGRTvqregRLardiRKSRAHTGYIFQQFNLV 98
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEilfdGENIPAMSRS-----RL----YTVRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 99 NRLSVLENVligalgstpfwrtcfSWFTGEQKQ--------RALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
Cdd:PRK11831 97 TDMNVFDNV---------------AYPLREHTQlpapllhsTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 171 AKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQV-------DYALrycerIVAlrQGHVFYDGSSQQ 239
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVpevlsiaDHAY-----IVA--DKKIVAHGSAQA 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-212 |
8.39e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvgshieLLGRTVQREGRLARDIRKsraHTGYI 91
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN-------FTGTILANNRKPTKQILK---RTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 92 FQQFNLVNRLSVLENVLIGALGSTPfwrtcfSWFTGEQKQRALQA------LTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCSLLRLP------KSLTKQEKILVAESviselgLTKCENTIIGNSFIRGISGGERKRVSIAH 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 985002877 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQ 212
Cdd:PLN03211 220 EMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQ 265
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-229 |
8.81e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.47 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGdksvgsHIEL--LGRTV---QR----EGRLARdirksrah 87
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpyGSG------RIARpaGARVLflpQRpylpLGTLRE-------- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 88 tgyifqqfnlvnrlsvlenvligALgSTPFWRTCFSwftgeqKQRALQALTRVGMVHFAHQ--------RVstLSGGQQQ 159
Cdd:COG4178 445 -----------------------AL-LYPATAEAFS------DAELREALEAVGLGHLAERldeeadwdQV--LSLGEQQ 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDinQNDGITVVVTLHQVDYAlRYCERIVALRQG 229
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLA-AFHDRVLELTGD 559
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-230 |
1.60e-16 |
|
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: 74.02 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHlsglitgdksvgshieLLGRTVQREGRLARDirkS 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKL----------------IAGELEPDEGIVTWG---S 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTGYiFQQfnlvnrlsvlenvligalgstpfwrtcfswftgeqkqralqaltrvgmvhfahqrvstLSGGQQQRVAIA 164
Cdd:cd03221 62 TVKIGY-FEQ----------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHqvDYAL--RYCERIVALRQGH 230
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSH--DRYFldQVATKIIELEDGK 144
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-237 |
1.82e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.75 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLAKTF--------NQH-QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSVGSHIELLG 68
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtgwfrRQTvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIeptSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 69 RTVQREGRlardIRksrahtgYIFQ----QFNLVNRlsvlenvlIGALGSTPFwRTCFSWFTGEQKQRALQALTRVGMV- 143
Cdd:PRK15112 81 DYSYRSQR----IR-------MIFQdpstSLNPRQR--------ISQILDFPL-RLNTDLEPEQREKQIIETLRQVGLLp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 144 ----HFAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRY 219
Cdd:PRK15112 141 dhasYYPHM----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHI 216
|
250
....*....|....*...
gi 985002877 220 CERIVALRQGHVFYDGSS 237
Cdd:PRK15112 217 SDQVLVMHQGEVVERGST 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-209 |
1.96e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.66 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQREGRlARdirksraHTG 89
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESG---QIQIDGKTATRGDR-SR-------FMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 90 YIFQQFNLVNRLSVLENV--LIGALGSTPfwrtcfswftgeqKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARAL 167
Cdd:PRK13543 86 YLGHLPGLKADLSTLENLhfLCGLHGRRA-------------KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLW 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 985002877 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVT 209
Cdd:PRK13543 153 LSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTT 194
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-231 |
2.16e-16 |
|
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: 78.16 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQRegrlaRDIRKSRAHTGYIFQQF 95
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIW---PPTSGSVRLDGADLKQ-----WDRETFGKHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 96 NLVNRlSVLENVligalgstpfwrtcfSWFTGEQKQRALQALTRVGMVHFAHQRV------------STLSGGQQQRVAI 163
Cdd:TIGR01842 402 ELFPG-TVAENI---------------ARFGENADPEKIIEAAKLAGVHELILRLpdgydtvigpggATLSGGQRQRIAL 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-211 |
7.97e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.60 E-value: 7.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITG--DKSVGShIELLGRTVqREGRLArdirKSRAHTGYIFQ 93
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTI----ANLLTRfyDIDEGE-ILLDGHDL-RDYTLA----SLRNQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 94 QFNLVNRlSVLENVLIGALGStpfwrtcfswFTGEQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIAR 165
Cdd:PRK11176 425 NVHLFND-TIANNIAYARTEQ----------YSREQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIAR 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 985002877 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLH 211
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH 537
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-229 |
9.49e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.61 E-value: 9.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL------ITGDKSVGSHIELLGRTvqregrlARDIRKSRAHT-GY 90
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrVTADRMRFDDIDLLRLS-------PRERRKLVGHNvSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 91 IFQQFNlvNRLSVLENV---LIGALGSTPF---WRTCFSWftgeQKQRALQALTRVG-------MVHFAHQrvstLSGGQ 157
Cdd:PRK15093 94 IFQEPQ--SCLDPSERVgrqLMQNIPGWTYkgrWWQRFGW----RKRRAIELLHRVGikdhkdaMRSFPYE----LTEGE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-231 |
1.56e-15 |
|
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: 73.27 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQregrlARDIRKSRAHTGYIFQQFN 96
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFY---QPQGGQVLLDGKPIS-----QYEHKYLHSKVSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 LVNRlSVLENVLIGaLGSTPFwrtcfswftGEQKQRALQALTRVGMVHFAH-------QRVSTLSGGQQQRVAIARALMQ 169
Cdd:cd03248 99 LFAR-SLQDNIAYG-LQSCSF---------ECVKEAAQKAHAHSFISELASgydtevgEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 985002877 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQGHV 231
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-184 |
1.76e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 74.62 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgLItgDKSVGSHIELLGRTVQREGRLARDIRKSRAHTgyIFQQ-FN 96
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MI--ETPTGGELYYQGQDLLKADPEAQKLLRQKIQI--VFQNpYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 LVN-RLSV---LENVLI--GALGSTpfwrtcfswftgEQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQ 169
Cdd:PRK11308 104 SLNpRKKVgqiLEEPLLinTSLSAA------------ERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALML 171
|
170
....*....|....*
gi 985002877 170 QAKVILADEPIASLD 184
Cdd:PRK11308 172 DPDVVVADEPVSALD 186
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-185 |
2.18e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.05 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 14 FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSVG--SHIELLGRtvQR-EGRLARDIRKsraHTGY 90
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL----SLITGDHPQGysNDLTLFGR--RRgSGETIWDIKK---HIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 91 IFQQFNLVNRLSV-LENVLI-GALGSTPFWRTCfswfTGEQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARAL 167
Cdd:PRK10938 341 VSSSLHLDYRVSTsVRNVILsGFFDSIGIYQAV----SDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRAL 416
|
170
....*....|....*...
gi 985002877 168 MQQAKVILADEPIASLDP 185
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDP 434
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-229 |
6.46e-15 |
|
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: 71.59 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGRLARDIRkSRAHTGYIFQQFNLVN 99
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM---QTLEGKVHWSNKNESEPSFEATRSR-NRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RlSVLENVLIGalgsTPFwrtcfswftgeQKQR------ALQALTRVGMVHFAHQ-----RVSTLSGGQQQRVAIARALM 168
Cdd:cd03290 93 A-TVEENITFG----SPF-----------NKQRykavtdACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 985002877 169 QQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTLHQVDYaLRYCERIVALRQG 229
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-239 |
1.02e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.60 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKST---LLRHL----SGLITGDksvgshiellgrtvqregrlARDIRKSRAHtgY 90
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLyqptGGQVLLD--------------------GVPLVQYDHH--Y 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 91 IFQQFNLVN------RLSVLENVLIGaLGSTPF-------WRTCFSWFTGEQKQralQALTRVGmvhfahQRVSTLSGGQ 157
Cdd:TIGR00958 553 LHRQVALVGqepvlfSGSVRENIAYG-LTDTPDeeimaaaKAANAHDFIMEFPN---GYDTEVG------EKGSQLSGGQ 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARivmdTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHVFYDGSS 237
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTH 697
|
..
gi 985002877 238 QQ 239
Cdd:TIGR00958 698 KQ 699
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-239 |
2.42e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.44 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLL----RHLsglitgDKSVGShIELLGRTVQRegrLARDIRKSR----A 86
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLsliqRHF------DVSEGD-IRFHDIPLTK---LQLDSWRSRlavvS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 87 HTGYIFQQfnlvnrlSVLENVLIGALGSTPfwrtcfswftgEQKQRALQA--------------LTRVGmvhfahQRVST 152
Cdd:PRK10789 396 QTPFLFSD-------TVANNIALGRPDATQ-----------QEIEHVARLasvhddilrlpqgyDTEVG------ERGVM 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVF 232
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIA 528
|
....*..
gi 985002877 233 YDGSSQQ 239
Cdd:PRK10789 529 QRGNHDQ 535
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-239 |
2.78e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 30 GEMVALLGPSGSGKSTLLRHLSGLITGDKSvgshIELLGRTVQ--REGRLARdirksraHTGYIFQQfnlvnrlsvlenv 107
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLLPGSGS----IQFAGQPLEawSAAELAR-------HRAYLSQQ------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 108 ligalGSTPFWRTCFSWFT-----GEQKQRALQALTRV----GMVHFAHQRVSTLSGGQQQRVAIARALMQ-------QA 171
Cdd:PRK03695 78 -----QTPPFAMPVFQYLTlhqpdKTRTEAVASALNEVaealGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 172 KVILADEPIASLD--PESArivMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK03695 153 QLLLLDEPMNSLDvaQQAA---LDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-231 |
5.12e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 71.39 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSVGShIELLGRtvqregrlarDIR----KS-RAHTGYI 91
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY--DVTSGR-ILIDGQ----------DIRdvtqASlRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 92 FQQFNLVNRlSVLENVLIGALGSTPfwrtcfswftgEQKQRALQAL--------------TRVGmvhfahQRVSTLSGGQ 157
Cdd:COG5265 438 PQDTVLFND-TIAYNIAYGRPDASE-----------EEVEAAARAAqihdfieslpdgydTRVG------ERGLKLSGGE 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQ----VDyalryCERIVALRQGHV 231
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRlstiVD-----ADEILVLEAGRI 570
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-239 |
5.34e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.31 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSVGS-HIELLGrtvqreGRLARdiR 82
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL----SLIAGARKIQQgRVEVLG------GDMAD--A 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KSRAHTG----YIFQQF--NLVNRLSVLENVligalgstPFWRTCFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGG 156
Cdd:NF033858 69 RHRRAVCpriaYMPQGLgkNLYPTLSVFENL--------DFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 157 QQQRVAIARALMQQAKVILADEPIASLDPESAR---IVMDTLRDinQNDGITVVVTLHQVDYALRYcERIVALRQGHVFY 233
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRqfwELIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLA 217
|
....*.
gi 985002877 234 DGSSQQ 239
Cdd:NF033858 218 TGTPAE 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-229 |
7.96e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELLGRTVQ-REGRLARDIRKSRAHt 88
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS--GS-ILFQGKEIDfKSSKEALENGISMVH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 89 gyifQQFNLVNRLSVLENVLigaLGSTPFWrtcfSWFTGEQKQ-RALQAL-TRVGMVHFAHQRVSTLSGGQQQRVAIARA 166
Cdd:PRK10982 80 ----QELNLVLQRSVMDNMW---LGRYPTK----GMFVDQDKMyRDTKAIfDELDIDIDPRAKVATLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 167 LMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQG 229
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-229 |
1.00e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSVGSHIELLGRTVQregrlARDIRKSRAHTGYIFQQFNLV 98
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQ---PQSGEILLDGKPVT-----AEQPEDYRKLFSAVFTDFHLF 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 99 NRlsvlenvLIGALGSTPFWRTCFSWftgeqkqralqaLTRVGMVH---FAHQRVST--LSGGQQQRVAIARALMQQAKV 173
Cdd:PRK10522 410 DQ-------LLGPEGKPANPALVEKW------------LERLKMAHkleLEDGRISNlkLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQG 229
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNG 525
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-235 |
1.12e-13 |
|
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: 67.67 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRTVqregrlarDIRKSRAHTGYI 91
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPY--------KEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 92 F--QQFNLVNRLSVLENVligalgstPFWRTCFswftgeqkqralqaltrvgmvhfAHQRVSTLSGGQQQRVAIARALMQ 169
Cdd:cd03233 87 YvsEEDVHFPTLTVRETL--------DFALRCK-----------------------GNEFVRGISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVD---YALryCERIVALRQGHVFYDG 235
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdeiYDL--FDKVLVLYEGRQIYYG 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-231 |
1.15e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSVGShIELLGRTVQregrlARDIrKSRAHTGYIFQQFNLVNRLS 102
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL--PASEGE-AWLFGQPVD-----AGDI-ATRRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 103 VLENVLIGA-LGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
Cdd:NF033858 356 VRQNLELHArLFHLP---------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 985002877 182 SLDPeSARivmD----TLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
Cdd:NF033858 427 GVDP-VAR---DmfwrLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRV 475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-260 |
1.15e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksvgSHIEllgrtvqregRLARDIRKSRAHTGYIFQQFNLvn 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL-------SHAE----------TSSVVIRGSVAYVPQVSWIFNA-- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 rlSVLENVLIGA-LGSTPFWRTCFSwfTGEQKQRALQA---LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVIL 175
Cdd:PLN03232 694 --TVRENILFGSdFESERYWRAIDV--TALQHDLDLLPgrdLTEIG------ERGVNISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 176 ADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQF--DNERFDHLYRSIN 253
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHF-LPLMDRIILVSEGMIKEEGTFAELskSGSLFKKLMENAG 841
|
....*..
gi 985002877 254 RVEENAK 260
Cdd:PLN03232 842 KMDATQE 848
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-213 |
1.31e-13 |
|
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: 68.59 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 26 NIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQREGRlardirksrahtgYIFQQFNLvnRLSVLE 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPD---EGDIEIELDTVSYKPQ-------------YIKADYEG--TVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 106 NVLIGALGSTPFWRTcfswftgeqkqralQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDP 185
Cdd:cd03237 83 SSITKDFYTHPYFKT--------------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180
....*....|....*....|....*...
gi 985002877 186 ESARIVMDTLRDINQNDGITVVVTLHQV 213
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDI 176
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-244 |
1.72e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.82 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgshiellgrTVQREGRlarDI-----RKSRAHTGYIFQQ 94
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSG----------TLLFEGE---DIstlkpEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 FNLVNRlSVLENVLigalgstpfwrtcFSWFTGEQK---QRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQ 170
Cdd:PRK10247 90 PTLFGD-TVYDNLI-------------FPWQIRNQQpdpAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985002877 171 AKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVALrQGHVfydGSSQQFDNER 244
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKVITL-QPHA---GEMQEARYEL 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-229 |
1.99e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQ----HQALHAVDLNIHHGEMVALLGPSGSGKS----TLLRHLSG----LITGDksvgshIELLGR 69
Cdd:PRK15134 3 QPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvvYPSGD------IRFHGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 70 TVQR--EGRLaRDIRKSRahTGYIFQQ-FNLVNRLSVLENVLIGALgstpfwrtcfSWFTGEQKQRA----LQALTRVGM 142
Cdd:PRK15134 77 SLLHasEQTL-RGVRGNK--IAMIFQEpMVSLNPLHTLEKQLYEVL----------SLHRGMRREAArgeiLNCLDRVGI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 143 VH-------FAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDY 215
Cdd:PRK15134 144 RQaakrltdYPHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSI 219
|
250
....*....|....
gi 985002877 216 ALRYCERIVALRQG 229
Cdd:PRK15134 220 VRKLADRVAVMQNG 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-211 |
2.19e-13 |
|
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: 69.43 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 27 IHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvgshiellgrtvqrEGRLARDIR---KSRahtgYIFQQFNLVNRlSV 103
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPD----------------EGEVDEDLKisyKPQ----YISPDYDGTVE-EF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 104 LENVLIGALGStpfwrtcfSWFTGEqkqralqALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASL 183
Cdd:COG1245 422 LRSANTDDFGS--------SYYKTE-------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180
....*....|....*....|....*...
gi 985002877 184 DPESARIVMDTLRDINQNDGITVVVTLH 211
Cdd:COG1245 487 DVEQRLAVAKAIRRFAENRGKTAMVVDH 514
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-235 |
5.27e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.63 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL----ITGdksvGShIELLGRTVqregrLARDIRKsRAHTG--YIFQ 93
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkyeVTS----GS-ILLDGEDI-----LELSPDE-RARAGifLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 94 Q------FNLVNRLSVLENVLIGALGSTPFWRtcfswftgeqkQRALQALTRVGM-VHFAHQRV-STLSGGQQQRVAIAR 165
Cdd:COG0396 85 YpveipgVSVSNFLRTALNARRGEELSAREFL-----------KLLKEKMKELGLdEDFLDRYVnEGFSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvdYALRYcerIVALRQgHVFYDG 235
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ--RILDY---IKPDFV-HVLVDG 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-212 |
6.47e-13 |
|
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: 64.87 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLA-KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksVGShiellgrtvqreGRLardIRK 83
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP----WGS------------GRI---GMP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 SRAHTGYIFQQ--FNLVNRLSVLenvligalgstpfwrtCFSWFtgeqkqralqaltrvgmvhfahqrvSTLSGGQQQRV 161
Cdd:cd03223 62 EGEDLLFLPQRpyLPLGTLREQL----------------IYPWD-------------------------DVLSGGEQQRL 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDinqnDGITVVVTLHQ 212
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE----LGITVISVGHR 147
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-240 |
1.15e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 66.68 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSG--KSTLLRHLSGLITGDKSVGSHIELLGR-TVQREGRLARDI 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRrALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 RKSRAHTGYIFQQFNLVNRLSVLENvligalgstpfwrtcfswftGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
Cdd:NF000106 94 R*GRRESFSGRENLYMIGR*LDLSR--------------------KDARARADELLERFSLTEAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-239 |
1.48e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.06 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdKSVGSHIELLGRtVQREGRLARDIRK 83
Cdd:TIGR00956 61 GFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS-----NTDGFHIGVEGV-ITYDGITPEEIKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 84 S-RAHTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCfswftGEQKQRALQALTRVGMVHF--AHQR--------VST 152
Cdd:TIGR00956 135 HyRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNRPD-----GVSREEYAKHIADVYMATYglSHTRntkvgndfVRG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVD---YALryCERIVALRQG 229
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSqdaYEL--FDKVIVLYEG 287
|
250
....*....|
gi 985002877 230 HVFYDGSSQQ 239
Cdd:TIGR00956 288 YQIYFGPADK 297
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-212 |
2.66e-12 |
|
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: 63.80 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 30 GEMVALLGPSGSGKSTLLRHLS-----GLITGDksvgshIELLGRtvqregRLARDIRKSrahTGYIFQQFNLVNRLSVL 104
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAgrktaGVITGE------ILINGR------PLDKNFQRS---TGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 105 ENVLigalgstpfwrtcFSwftgeqkqralqALTRvgmvhfahqrvsTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
Cdd:cd03232 98 EALR-------------FS------------ALLR------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|....*...
gi 985002877 185 PESARIVMDTLRDInQNDGITVVVTLHQ 212
Cdd:cd03232 141 SQAAYNIVRFLKKL-ADSGQAILCTIHQ 167
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-236 |
3.64e-12 |
|
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: 64.05 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdksVGSHIELLGRTVQREGRlaRDIRKSRAhtgyIFQQFNLV 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL---SSGSILIDGVDISKIGL--HDLRSRIS----IIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 99 NRLSVLENVligalgsTPFwrtcfswftGEQKQRAL-QALTRVGMVHFAHQRV-----------STLSGGQQQRVAIARA 166
Cdd:cd03244 90 FSGTIRSNL-------DPF---------GEYSDEELwQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 167 LMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-240 |
3.70e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsglitgdksvgshiELLGRTVQREGRL--ARDIrksrahtGYIFQQFNL 97
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ----------------SLLSQFEISEGRVwaERSI-------AYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRlSVLENVLigalgstpfwrtcfsWFTGEQKQRaLQALTRV------------GMVHFAHQRVSTLSGGQQQRVAIAR 165
Cdd:PTZ00243 733 MNA-TVRGNIL---------------FFDEEDAAR-LADAVRVsqleadlaqlggGLETEIGEKGVNLSGGQKARVSLAR 795
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 166 ALMQQAKVILADEPIASLDPE-SARIVMDTLRdiNQNDGITVVVTLHQVdYALRYCERIVALRQGHVFYDGSSQQF 240
Cdd:PTZ00243 796 AVYANRDVYLLDDPLSALDAHvGERVVEECFL--GALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADF 868
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-215 |
4.82e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQaLHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvgshiellgrtvqrEGRLARDI 81
Cdd:PRK13409 338 ETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPD----------------EGEVDPEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 R---KSRahtgYIFQQFNLVNRLsVLENVlIGALGSTPFWrtcfswftgeqkqraLQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:PRK13409 401 KisyKPQ----YIKPDYDGTVED-LLRSI-TDDLGSSYYK---------------SEIIKPLQLERLLDKNVKDLSGGEL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQV---DY 215
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIymiDY 519
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-239 |
7.70e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.38 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQA-LHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLIT-GDKSVGSHIELLGRTVQREGRLA 78
Cdd:PRK11022 3 LLNVDKLSVHFGDESApFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 79 RdiRK-SRAHTGYIFQQ------------FNLVNRLSVLEnvligalGSTPFWRtcfswftgeqKQRALQALTRVGMVH- 144
Cdd:PRK11022 83 R--RNlVGAEVAMIFQDpmtslnpcytvgFQIMEAIKVHQ-------GGNKKTR----------RQRAIDLLNQVGIPDp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 145 ------FAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALR 218
Cdd:PRK11022 144 asrldvYPHQ----LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAE 219
|
250 260
....*....|....*....|.
gi 985002877 219 YCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK11022 220 AAHKIIVMYAGQVVETGKAHD 240
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-240 |
7.85e-12 |
|
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: 64.97 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsglitgdksvgshiELLGRTVQREGRLArdIRKSRAhtgYIFQQFNLVN 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLS----------------ALLAEMDKVEGHVH--MKGSVA---YVPQQAWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RlSVLENVLIGALGSTPFWRtcfswftgeQKQRALQALTRVGMVHFAHQ-----RVSTLSGGQQQRVAIARALMQQAKVI 174
Cdd:TIGR00957 713 D-SLRENILFGKALNEKYYQ---------QVLEACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 175 LADEPIASLDPESARIVMD-TLRDINQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQF 240
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-224 |
1.52e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 1.52e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIV 224
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIV 1429
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-229 |
1.53e-11 |
|
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: 64.26 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQAlHAVD---LNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSVGShiellGRTVQREGRLARD 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSS-PAVDrlcVGVRPGECFGLLGVNGAGKTTTFK----MLTGDTTVTS-----GDATVAGKSILTN 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIfQQFNLVNRL-SVLENVLIGA-LGSTPfwrtcfswfTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
Cdd:TIGR01257 2007 ISDVHQNMGYC-PQFDAIDDLlTGREHLYLYArLRGVP---------AEEIEKVANWSIQSLGLSLYADRLAGTYSGGNK 2076
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 985002877 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQG 229
Cdd:TIGR01257 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-257 |
1.70e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdKSVGSHIellgrtvqregrlardIRKSRAHTGYIFQQ 94
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP-RSDASVV----------------IRGTVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 FNLvnrlSVLENVLIGA-LGSTPFWRTCFswFTGEQKQRALQA---LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQ 170
Cdd:PLN03130 691 FNA----TVRDNILFGSpFDPERYERAID--VTALQHDLDLLPggdLTEIG------ERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 171 AKVILADEPIASLDPESARIVMDT-LRDINQNDgiTVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDN--ERFDH 247
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQVFDKcIKDELRGK--TRVLVTNQLHF-LSQVDRIILVHEGMIKEEGTYEELSNngPLFQK 835
|
250
....*....|
gi 985002877 248 LYRSINRVEE 257
Cdd:PLN03130 836 LMENAGKMEE 845
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-244 |
1.79e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.80 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELlGRTVQ----REGRLAR 79
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDS--GT-IEI-GETVKlayvDQSRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 80 DIRKSrahtgyIFQQFNLVNRLSVLENVLIGAlgstpfwRTCFSWF--TGEQKQralqaltrvgmvhfahQRVSTLSGGQ 157
Cdd:TIGR03719 398 DPNKT------VWEEISGGLDIIKLGKREIPS-------RAYVGRFnfKGSDQQ----------------KKVGQLSGGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVTlHQVDYALRYCERIVALR-QGHV-FYDG 235
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVIS-HDRWFLDRIATHILAFEgDSHVeWFEG 524
|
....*....
gi 985002877 236 SSQQFDNER 244
Cdd:TIGR03719 525 NFSEYEEDK 533
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-235 |
2.07e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.71 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGShIELLGRTVQREgRLARDirksrahTGYIFQQFNL 97
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGD-IRISGFPKKQE-TFARI-------SGYCEQNDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRLSVLENVLIGALGSTPfwrtcfSWFTGEQKQRAL-QALTRVGMVHFAHQRV-----STLSGGQQQRVAIARALMQQA 171
Cdd:PLN03140 965 SPQVTVRESLIYSAFLRLP------KEVSKEEKMMFVdEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANP 1038
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 172 KVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQ--VDYALRYCERIVALRQGHVFYDG 235
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYSG 1103
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-244 |
2.09e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSVGSHIELLGRTVQ-REGRLArdIR-------KSRAHTGyifqq 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYG---ATRRTAGQVYLDGKPIDiRSPRDA--IRagimlcpEDRKAEG----- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 fnLVNRLSVLENVLIGAlgstpfwRTCFSWF-----------TGEQKQRALQALTRVgmvhfAHQRVSTLSGGQQQRVAI 163
Cdd:PRK11288 342 --IIPVHSVADNINISA-------RRHHLRAgclinnrweaeNADRFIRSLNIKTPS-----REQLIMNLSGGNQQKAIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATER 486
|
.
gi 985002877 244 R 244
Cdd:PRK11288 487 Q 487
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-239 |
2.63e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.20 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQREGRLArdIRKSRAhtgyIFQQFNLVN 99
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEG---EIRLDGRPLSSLSHSV--LRQGVA----MVQQDPVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENVLIGA-LGSTPFWRTCfswftgEQKQraLQALTRvGMVHFAHQRV----STLSGGQQQRVAIARALMQQAKVI 174
Cdd:PRK10790 428 ADTFLANVTLGRdISEEQVWQAL------ETVQ--LAELAR-SLPDGLYTPLgeqgNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 175 LADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQ 560
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-244 |
4.01e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSVGShIELLGRTVQ----REGrLARD---IRKSRAHTGyif 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP--RTSGY-VTLDGHEVVtrspQDG-LANGivyISEDRKRDG--- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 93 qqfnLVNRLSVLENVLIGALGStpfwrtcFSWFTGEQKQRALQALtrVGmvHF----------AHQRVSTLSGGQQQRVA 162
Cdd:PRK10762 341 ----LVLGMSVKENMSLTALRY-------FSRAGGSLKHADEQQA--VS--DFirlfniktpsMEQAIGLLSGGNQQKVA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 163 IARALMQQAKVILADEPIASLDPESARIVMDTlrdINQ--NDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQL---INQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQA 482
|
....
gi 985002877 241 DNER 244
Cdd:PRK10762 483 TQEK 486
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-187 |
4.52e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFN-QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKsvgshiELLGrtvqrEGRLARD 80
Cdd:TIGR03719 2 QYIYTMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DK------DFNG-----EARPQPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRksrahTGYIFQQFNLVNRLSVLENVL---------------IGALGSTPfwRTCFSWFTGEQK--QRALQAL------ 137
Cdd:TIGR03719 68 IK-----VGYLPQEPQLDPTKTVRENVEegvaeikdaldrfneISAKYAEP--DADFDKLAAEQAelQEIIDAAdawdld 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 138 TRVGMVHFA------HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
Cdd:TIGR03719 141 SQLEIAMDAlrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-231 |
5.82e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVqrEGRLARDIRKSRAHTGYIFQQ--FN 96
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV---ESQGGEIIFNGQRI--DTLSPGKLQALRRDIQFIFQDpyAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 LVNRL----SVLENVLIGALGSTPFWRTCFSWFtgeqkqralqaLTRVGMV-HFAHQRVSTLSGGQQQRVAIARALMQQA 171
Cdd:PRK10261 414 LDPRQtvgdSIMEPLRVHGLLPGKAAAARVAWL-----------LERVGLLpEHAWRYPHEFSGGQRQRICIARALALNP 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 172 KVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:PRK10261 483 KVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-226 |
9.45e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 9.45e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVAL 226
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-231 |
4.00e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.56 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 1 MQTIIRVEKLakTFNQHQAL-HAVDLNIHHGEMVALLGPSGSGKS-TLLRHLSGLITGDKSVGSHIELLGRTVQREGRLA 78
Cdd:PRK10418 1 MPQQIELRNI--ALQAAQPLvHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 79 RdirksraHTGYIFQQ----FNLVN--RLSVLENVLigALGSTPfwrtcfswftgeQKQRALQALTRVGMVHfaHQRVST 152
Cdd:PRK10418 79 R-------KIATIMQNprsaFNPLHtmHTHARETCL--ALGKPA------------DDATLTAALEAVGLEN--AARVLK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 153 L-----SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALR 227
Cdd:PRK10418 136 LypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMS 215
|
....
gi 985002877 228 QGHV 231
Cdd:PRK10418 216 HGRI 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-242 |
4.42e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQREGRL------ARDIRKSRAHTGYiFQQFN 96
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGV---DKRAGGEIRLNGKDISPRSPLdavkkgMAYITESRRDNGF-FPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 LVNRLSVLENVLIGALGSTpfWRTCFSwfTGEQK----QRALQALTrvgmVHFAHQRVSTLSGGQQQRVAIARALMQQAK 172
Cdd:PRK09700 358 IAQNMAISRSLKDGGYKGA--MGLFHE--VDEQRtaenQRELLALK----CHSVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985002877 173 VILADEPIASLDPES-ARI--VMDTLRDinqnDGITVVVTLHQVDYALRYCERIVALRQGHVfydgsSQQFDN 242
Cdd:PRK09700 430 VIIFDEPTRGIDVGAkAEIykVMRQLAD----DGKVILMVSSELPEIITVCDRIAVFCEGRL-----TQILTN 493
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-212 |
4.71e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 30 GEMVALLGPSGSGKSTLLRHLS-----GLIT-GDKSVGSHiellgrtvqregrlARDIRKSRAhTGYIFQQFNLVNRLSV 103
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAervttGVITgGDRLVNGR--------------PLDSSFQRS-IGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 104 LENVLIGALGSTPfwrtcfSWFTGEQKQRALQALTR-VGMVHFAHQRVST----LSGGQQQRVAIARALMQQAKVIL-AD 177
Cdd:TIGR00956 854 RESLRFSAYLRQP------KSVSKSEKMEYVEEVIKlLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190
....*....|....*....|....*....|....*
gi 985002877 178 EPIASLDPESARIVMDTLRDInQNDGITVVVTLHQ 212
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQ 961
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-236 |
7.11e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.15 E-value: 7.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlITGDKSVGSHIELLGrtvqregrlaRDIrksrahtgyifqqfnlvN 99
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYEVTEGEILFKG----------EDI-----------------T 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENVLIGAlgstpfwrtcfswFTGEQKQRALQALTrvgMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
Cdd:cd03217 68 DLPPEERARLGI-------------FLAFQYPPEIPGVK---NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQvdyalRYCERIVALRqGHVFYDGS 236
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSVLIITHYQ-----RLLDYIKPDR-VHVLYDGR 182
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-236 |
8.25e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 8.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 22 AV-DLN--IHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRTV----QREgrlardIRKSRA-HTGYIFQ 93
Cdd:PRK09473 31 AVnDLNfsLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREIlnlpEKE------LNKLRAeQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 94 ----QFNLVNRLS-VLENVLI---GALGSTPFwrtcfswftgEQKQRALQALT------RVGMvhFAHQrvstLSGGQQQ 159
Cdd:PRK09473 105 dpmtSLNPYMRVGeQLMEVLMlhkGMSKAEAF----------EESVRMLDAVKmpearkRMKM--YPHE----FSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG---------H 230
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGrtmeygnarD 248
|
....*.
gi 985002877 231 VFYDGS 236
Cdd:PRK09473 249 VFYQPS 254
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-224 |
1.32e-09 |
|
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: 55.79 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHlsglitgdksvgshiellgrtvqregrlardirksrahTGYIFQQFN 96
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--------------------------------------GLYASGKAR 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 LVNRLSVLENVLIGALGStpfwrtcfswftgeqkqraLQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQAK--V 173
Cdd:cd03238 50 LISFLPKFSRNKLIFIDQ-------------------LQFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtL 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 985002877 174 ILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQvDYALRYCERIV 224
Cdd:cd03238 111 FILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHN-LDVLSSADWII 159
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-231 |
1.37e-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: 58.42 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsGLITGDKSVGSHIELLGRTVQREGrlardirksrAHtgyifqqfNLVN 99
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGLNIAKIG----------LH--------DLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENVLIGALGSTPFWRTCFSWFTGEQKQRALQALTRVGMV--------HFAHQRVSTLSGGQQQRVAIARALMQQA 171
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVsalpdkldHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 172 KVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEV 1497
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-231 |
2.31e-09 |
|
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: 55.88 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKLAKTFNQH--QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSVGSHIELlgrtvqreg 75
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfrfleaeEGKIEIDGIDISTIPL--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 76 rlaRDIRKSrahTGYIFQQFNLvnrlsvlenvLIGALGST--PFWRtcfswFTGEQKQRALqaltrvgmvhfahqRVS-- 151
Cdd:cd03369 78 ---EDLRSS---LTIIPQDPTL----------FSGTIRSNldPFDE-----YSDEEIYGAL--------------RVSeg 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 152 --TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQvdyaLRY---CERIVAL 226
Cdd:cd03369 123 glNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTN--STILTIAHR----LRTiidYDKILVM 196
|
....*
gi 985002877 227 RQGHV 231
Cdd:cd03369 197 DAGEV 201
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-246 |
6.45e-09 |
|
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: 55.25 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdksvgshIELLGRTVQREGRLArdirksraHTGYIF--QQFNL 97
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLL----------------MLILGELEPSEGKIK--------HSGRISfsSQFSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRLSVLENVLIGALGSTPFWRtcfSWFTGEQKQRALQALTRVGMVHFAHQRVsTLSGGQQQRVAIARALMQQAKVILAD 177
Cdd:cd03291 109 IMPGTIKENIIFGVSYDEYRYK---SVVKACQLEEDITKFPEKDNTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFD 246
Cdd:cd03291 185 SPFGYLDVFTEKEIFESCVCKLMANKTRILVT-SKMEH-LKKADKILILHEGSSYFYGTFSELQSLRPD 251
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
153-256 |
6.69e-09 |
|
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: 55.25 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVF 232
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIE-AMLECQRFLVIEENKVR 215
|
90 100
....*....|....*....|....
gi 985002877 233 YDGSSQQFDNERfDHLYRSINRVE 256
Cdd:cd03289 216 QYDSIQKLLNEK-SHFKQAISPSD 238
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-212 |
6.86e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSvgsHIELLGRTVQRegrlarDIRKSRAHTGYIFQQFNLVN 99
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG---EILFERQSIKK------DLCTYQKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENVLigalgstpfwrtcFSWFTGEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
Cdd:PRK13540 88 YLTLRENCL-------------YDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 985002877 180 IASLDPESARIVMDTLRDiNQNDGITVVVTLHQ 212
Cdd:PRK13540 155 LVALDELSLLTIITKIQE-HRAKGGAVLLTSHQ 186
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-187 |
1.22e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVgshiellgrtvqregrlardIRKS-R 85
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT--------------------VKWSeN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 86 AHTGYIFQ----QFNlvNRLSVLEnvligalgstpfWrtcFSWFT----GEQKQRALqaltrVGMVHF----AHQRVSTL 153
Cdd:PRK15064 382 ANIGYYAQdhayDFE--NDLTLFD------------W---MSQWRqegdDEQAVRGT-----LGRLLFsqddIKKSVKVL 439
|
170 180 190
....*....|....*....|....*....|....
gi 985002877 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-214 |
1.31e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksvgshiELLGRTVQREGRLARDIRKSrahtgyiFQQ 94
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG------------ELPLLSGERQSQFSHITRLS-------FEQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 95 FN-LVNRLSVLENVLIGALGSTPFWRTCFSWFTGEQK--QRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
Cdd:PRK10938 75 LQkLVSDEWQRNNTDMLSPGEDDTGRTTAEIIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 985002877 172 KVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVD 214
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFD 196
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-246 |
1.74e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdksvgshIELLGRTVQREGRLArdirksraHTGYIF--QQFNL 97
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLL----------------MMIMGELEPSEGKIK--------HSGRISfsPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 98 VNRLSVLENVLIGaLGSTPFWRTcfSWFTGEQKQRALQALTRVGMVHFAHQRVsTLSGGQQQRVAIARALMQQAKVILAD 177
Cdd:TIGR01271 498 IMPGTIKDNIIFG-LSYDEYRYT--SVIKACQLEEDIALFPEKDKTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 178 EPIASLDPESARIVMDT-LRDINQNDgiTVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFD 246
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFEScLCKLMSNK--TRILVTSKLEH-LKKADKILLLHEGVCYFYGTFSELQAKRPD 640
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-244 |
2.18e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvgSHIELLGRTVQregrlARDIRKSRAHTGYIFQqfnlvn 99
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE----GEIQIDGVSWN-----SVTLQTWRKAFGVIPQ------ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENVLIGALGSTPFWRTCFSWFTGEQkqralqaltrVGMVHFAHQRVS-----------TLSGGQQQRVAIARALM 168
Cdd:TIGR01271 1300 KVFIFSGTFRKNLDPYEQWSDEEIWKVAEE----------VGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSIL 1369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRVE-ALLECQQFLVIEGSSVKQYDSIQKLLNET 1442
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-215 |
3.47e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.72 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG-----LITGDksvgshIELLGRTVqregr 76
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykILEGD------ILFKGESI----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 77 LARDIRKsRAHTGyIFQQFNLvnrlsvleNVLIGALGSTPFWRTCFSwftGEQKQRAL-------------QALTRVGM- 142
Cdd:CHL00131 74 LDLEPEE-RAHLG-IFLAFQY--------PIEIPGVSNADFLRLAYN---SKRKFQGLpeldplefleiinEKLKLVGMd 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 143 VHFAHQRVST-LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDI-NQNDGItVVVTLHQ--VDY 215
Cdd:CHL00131 141 PSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmTSENSI-ILITHYQrlLDY 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-187 |
5.62e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 14 FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvgshiellgrtvqrEGRL--ARDIRKSR------ 85
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLD----------------DGRIiyEQDLIVARlqqdpp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 86 ---------------AHTGYIFQQF-------------NLVNRLSVLENVLIGALGstpfWRTcfswftgeqKQRALQAL 137
Cdd:PRK11147 77 rnvegtvydfvaegiEEQAEYLKRYhdishlvetdpseKNLNELAKLQEQLDHHNL----WQL---------ENRINEVL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 985002877 138 TRVGMVhfAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
Cdd:PRK11147 144 AQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-231 |
1.12e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKtfnqhQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSVGSHIELLGRTVQregrlARDI 81
Cdd:PRK15439 266 APVLTVEDLTG-----EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGL---RPARGGRIMLNGKEIN-----ALST 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 82 rKSRAHTGYIF-----QQFNLVNRLSVLENVLIGALGSTPFW-RTCFSWFTGEQKQRALQaltrvgmVHFAH--QRVSTL 153
Cdd:PRK15439 333 -AQRLARGLVYlpedrQSSGLYLDAPLAWNVCALTHNRRGFWiKPARENAVLERYRRALN-------IKFNHaeQAARTL 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPeSARI-VMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV-SARNdIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-187 |
1.33e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 35 LLGPSGSGKSTLLRHLSGLitgDKsvgshiELLGrtvqrEGRLARDIRksrahTGYIFQQFNLVNRLSVLENVL------ 108
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGV---DK------EFEG-----EARPAPGIK-----VGYLPQEPQLDPEKTVRENVEegvaev 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 109 ---------IGALGSTP---FWRTCfswftgeQKQRALQAL----------TRVGMVHFA------HQRVSTLSGGQQQR 160
Cdd:PRK11819 99 kaaldrfneIYAAYAEPdadFDALA-------AEQGELQEIidaadawdldSQLEIAMDAlrcppwDAKVTKLSGGERRR 171
|
170 180
....*....|....*....|....*..
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPES 187
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-186 |
2.87e-07 |
|
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: 50.95 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksvGSHIELLGRTVQREGRLARdirksRAHTGYIFQQFNLVNRls 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE---SGEILLDGQPVTADNREAY-----RQLFSAVFSDFHLFDR-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 103 vlenvLIGALGstpfwrtcfswftGEQKQRALQALTRVGM---VHFAHQRVST--LSGGQQQRVAIARALMQQAKVILAD 177
Cdd:COG4615 421 -----LLGLDG-------------EADPARARELLERLELdhkVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFD 482
|
....*....
gi 985002877 178 EPIASLDPE 186
Cdd:COG4615 483 EWAADQDPE 491
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-231 |
2.92e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.04 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTllrhLSGLITgdksvgshiellGRTVQREGRLarDIRKSRAhtgYIFQQFN 96
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKST----LSNLIA------------GVTMPNKGTV--DIKGSAA---LIAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 97 LVNRLSVLENVLIGALgstpfwrtcFSWFTGEQKQRAL-QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
Cdd:PRK13545 96 LNGQLTGIENIELKGL---------MMGLTKEKIKEIIpEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 985002877 176 ADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:PRK13545 167 IDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-211 |
3.30e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 30 GEMVALLGPSGSGKSTLLRHLSGLIT---GD----------------KSVGSHIELLgrtvqREGRLaRDIRKSRaHTGY 90
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKpnlGDydeepswdevlkrfrgTELQDYFKKL-----ANGEI-KVAHKPQ-YVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 91 IFQQFNLVNRlSVLENVligalgstpfwrtcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
Cdd:COG1245 172 IPKVFKGTVR-ELLEKV--------------------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 985002877 171 AKVILADEPIASLDP----ESARIVMDTLrdinqNDGITVVVTLH 211
Cdd:COG1245 231 ADFYFFDEPSSYLDIyqrlNVARLIRELA-----EEGKYVLVVEH 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-184 |
4.04e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 33 VALLGPSGSGKSTLLRhlsgLITGDksvgshIELLGRTVQREG--RLArdirksrahtgyIFQQFNlVNRLSVLENVLIg 110
Cdd:PLN03073 538 IAMVGPNGIGKSTILK----LISGE------LQPSSGTVFRSAkvRMA------------VFSQHH-VDGLDLSSNPLL- 593
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 111 algstpFWRTCFSWFTgEQKQRA-LQALTRVGmvHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
Cdd:PLN03073 594 ------YMMRCFPGVP-EQKLRAhLGSFGVTG--NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-243 |
4.55e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSglitgdksvgshiellgRTVQRE-GRLARDirksrahtGYIFQQFNLV 98
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF-----------------RIVELEkGRIMID--------DCDVAKFGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 99 N---RLSVLENVLIGALGSTPFWRTCFSWFTGEQKQRALQ------ALTR--VGMVHFAHQRVSTLSGGQQQRVAIARAL 167
Cdd:PLN03232 1307 DlrrVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALErahikdVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985002877 168 MQQAKVILADEPIASLDPESARIVMDTLRDinQNDGITVVVTLHQVDYALRyCERIVALRQGHVF-YDGSSQQFDNE 243
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLeYDSPQELLSRD 1460
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-196 |
5.99e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsvGShIELlGRTVQ-------RE 74
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDS--GT-IKI-GETVKlayvdqsRD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 75 G------------------RLARDIRKSRAHTGyifqQFNlvnrlsvlenvligalgstpfwrtcfswFTGEQKQralqa 136
Cdd:PRK11819 398 AldpnktvweeisggldiiKVGNREIPSRAYVG----RFN----------------------------FKGGDQQ----- 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 137 ltrvgmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPEsarivmdTLR 196
Cdd:PRK11819 441 -----------KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE-------TLR 482
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-239 |
6.83e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 2 QTIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSVGSHIELLGRTVQRE--- 74
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQvie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 75 --GRLARDIRKSR-AHTGYIFQQ--FNLVNRLSVLENVligalgstpfwRTCFSWFTGEQKQRALQALTRV--------- 140
Cdd:PRK10261 90 lsEQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQI-----------AESIRLHQGASREEAMVEAKRMldqvripea 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 141 --GMVHFAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALR 218
Cdd:PRK10261 159 qtILSRYPHQ----LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAE 234
|
250 260
....*....|....*....|.
gi 985002877 219 YCERIVALRQGHVFYDGSSQQ 239
Cdd:PRK10261 235 IADRVLVMYQGEAVETGSVEQ 255
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-208 |
1.41e-06 |
|
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: 48.13 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 30 GEMVALLGPSGSGKSTLLRHLSGLITGD----KSVGSHIELL----GRTVQ------REGRLaRDIRK-------SRAHT 88
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNlgkfDDPPDWDEILdefrGSELQnyftklLEGDV-KVIVKpqyvdliPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 89 GYIFQQFNLVNRLSVLENVLigalgstpfwrtcfswftgeqkqralqalTRVGMVHFAHQRVSTLSGGQQQRVAIARALM 168
Cdd:cd03236 105 GKVGELLKKKDERGKLDELV-----------------------------DQLELRHVLDRNIDQLSGGELQRVAIAAALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 985002877 169 QQAKVILADEPIASLDP----ESARIVmdtlRDINQNDGITVVV 208
Cdd:cd03236 156 RDADFYFFDEPSSYLDIkqrlNAARLI----RELAEDDNYVLVV 195
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
148-233 |
1.83e-06 |
|
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: 47.18 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 148 QRVStLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIvalr 227
Cdd:cd03222 68 QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI---- 142
|
....*.
gi 985002877 228 qgHVFY 233
Cdd:cd03222 143 --HVFE 146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-207 |
1.91e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 30 GEMVALLGPSGSGKSTLLRHLSGLIT---GD-KSVGSHIELL----GRTVQ------REGRLaRDIRKSRaHTGYIFQQF 95
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIpnlGDyEEEPSWDEVLkrfrGTELQnyfkklYNGEI-KVVHKPQ-YVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 96 N-LVNRLsvLENVligalgstpfwrtcfswftgEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
Cdd:PRK13409 177 KgKVREL--LKKV--------------------DERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....
gi 985002877 175 LADEPIASLDPESaRI-VMDTLRDINQNDGITVV 207
Cdd:PRK13409 235 FFDEPTSYLDIRQ-RLnVARLIRELAEGKYVLVV 267
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
14-198 |
2.42e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.93 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 14 FNQHQALHAVDLnihHGEMVALLGPSGSGKSTLLRHLSGLITG--------------DKSVGSHIELL----GRTVQ--- 72
Cdd:COG0419 10 FRSYRDTETIDF---DDGLNLIVGPNGAGKSTILEAIRYALYGkarsrsklrsdlinVGSEEASVELEfehgGKRYRier 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 73 REGRLARDIRKSRAHTGYIFQQFNLVNRLSVLENVLiGALGSTpfwrtcfswftGEQKQRALQALTRVGMVHFAH----Q 148
Cdd:COG0419 87 RQGEFAEFLEAKPSERKEALKRLLGLEIYEELKERL-KELEEA-----------LESALEELAELQKLKQEILAQlsglD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 985002877 149 RVSTLSGGQQQRVAIARALmqqaKVILaDepIASLDPESARIVMDTLRDI 198
Cdd:COG0419 155 PIETLSGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDALEEL 197
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-210 |
2.95e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 24 DLNIHHGEMVALLGPSGSGKSTLLRHLsGLITGDKSVGSHiellgrtvqregrlardiRKSRAHTGYIfqqfnlvnrlsv 103
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAI-GLALGGAQSATR------------------RRSGVKAGCI------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 104 lenvligalgstpfwrtcfswftgeqkqRALQALTRVGMVHfahqrvsTLSGGQQQRVAIARAL----MQQAKVILADEP 179
Cdd:cd03227 64 ----------------------------VAAVSAELIFTRL-------QLSGGEKELSALALILalasLKPRPLYILDEI 108
|
170 180 190
....*....|....*....|....*....|.
gi 985002877 180 IASLDPESARIVMDTLRDINQNDGITVVVTL 210
Cdd:cd03227 109 DRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-240 |
7.92e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 130 KQRaLQALTRVGMVHFAHQR-VSTLSGGQQQRVAIARALMQQAKVI--LADEPIASLDPESARIVMDTLRDInQNDGITV 206
Cdd:PRK00635 454 KSR-LSILIDLGLPYLTPERaLATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKL-RDQGNTV 531
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 985002877 207 VVTLHQvDYALRYCERIV------ALRQGHVFYDGSSQQF 240
Cdd:PRK00635 532 LLVEHD-EQMISLADRIIdigpgaGIFGGEVLFNGSPREF 570
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
5-211 |
1.27e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.94 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 5 IRVEKlAKTFNqhqaLHAVDLNIHHGEMVALLGPSGSGKSTL--------------------LRHLSGLItgDKSVGSHI 64
Cdd:cd03270 1 IIVRG-AREHN----LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryveslsayARQFLGQM--DKPDVDSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 65 ELLGRTVQREGRLARdiRKSRAHTGYI----------FQQFNLVNRLSVLENVLIGALgstpfwrtcfswftgeqkqral 134
Cdd:cd03270 74 EGLSPAIAIDQKTTS--RNPRSTVGTVteiydylrllFARVGIRERLGFLVDVGLGYL---------------------- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 135 qALTRvgmvhfahqRVSTLSGGQQQRVAIARAL-MQQAKVI-LADEPIASLDPESARIVMDTLRDInQNDGITVVVTLH 211
Cdd:cd03270 130 -TLSR---------SAPTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEH 197
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
20-214 |
2.55e-05 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLL-----RHLSGLITGDK-SVGSH-----IELLGRTVQRE----GRLARDIrkS 84
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKeQPGNHdriegLEHIDKVIVIDqspiGRTPRSN--P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 85 RAHTG---YIFQQFNLV------NRlSVLENVLIGALGSTPFWRTCF---SWFTGEQK-QRALQALTRVGM--VHFAhQR 149
Cdd:cd03271 89 ATYTGvfdEIRELFCEVckgkryNR-ETLEVRYKGKSIADVLDMTVEealEFFENIPKiARKLQTLCDVGLgyIKLG-QP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985002877 150 VSTLSGGQQQRVAIARALMQQAK----VILaDEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVD 214
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKRSTgktlYIL-DEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLD 233
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
13-60 |
7.34e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.89 E-value: 7.34e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 985002877 13 TFNQHQalhavdLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSV 60
Cdd:pfam13555 11 TFDGHT------IPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAKRA 52
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-236 |
1.46e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSVGSHIELLGRTVQREGrlARDIRksrahtgyifQQFNLVN 99
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMV---EVCGGEIRVNGREIGAYG--LRELR----------RQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 100 RLSVLENVLIgALGSTPFWRTcfswfTGEQKQRALQAltrVGMV-HFAHQ------RV----STLSGGQQQRVAIARALM 168
Cdd:PTZ00243 1391 QDPVLFDGTV-RQNVDPFLEA-----SSAEVWAALEL---VGLReRVASEsegidsRVleggSNYSVGQRQLMCMARALL 1461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 169 QQ-AKVILADEPIASLDPESARIVMDTLRDINQN-DGITVVVTLHQVdyalRYCERIVALRQGHVFYDGS 236
Cdd:PTZ00243 1462 KKgSGFILMDEATANIDPALDRQIQATVMSAFSAyTVITIAHRLHTV----AQYDKIIVMDHGAVAEMGS 1527
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-215 |
2.01e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksvGSHIELLGRTVQREGRLARDIR- 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--------REDYEVTGGTVEFKGKDLLELSp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 83 KSRAHTGyIFQQFN-------LVNR--LSVLENVLIGALGSTPFWRTCFSWFTgEQKQRALQA----LTRVGMVHFahqr 149
Cdd:PRK09580 73 EDRAGEG-IFMAFQypveipgVSNQffLQTALNAVRSYRGQEPLDRFDFQDLM-EEKIALLKMpedlLTRSVNVGF---- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 985002877 150 vstlSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIV---MDTLRDINQNdgiTVVVTLHQ--VDY 215
Cdd:PRK09580 147 ----SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVadgVNSLRDGKRS---FIIVTHYQriLDY 210
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-209 |
5.85e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSVGSHIElLGRTVQREGRLARD 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELapvSGEIGLAKGIK-LGYFAQHQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 81 IRKSRAHTGYIFQQfnlvnrlsVLENVLIGALGSTPFwrtcfswftgeQKQRALQALTRvgmvhfahqrvstLSGGQQQR 160
Cdd:PRK10636 391 DESPLQHLARLAPQ--------ELEQKLRDYLGGFGF-----------QGDKVTEETRR-------------FSGGEKAR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 985002877 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVT 209
Cdd:PRK10636 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVS 484
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-214 |
5.92e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 132 RALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQAK---VILADEPIASLDPESARIVMDTLRDINQNdGITVV 207
Cdd:TIGR00630 808 RKLQTLCDVGLGYIRlGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDK-GNTVV 886
|
....*..
gi 985002877 208 VTLHQVD 214
Cdd:TIGR00630 887 VIEHNLD 893
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-57 |
8.04e-04 |
|
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: 39.69 E-value: 8.04e-04
10 20 30
....*....|....*....|....*....|..
gi 985002877 29 HGEMVALLGPSGSGKSTLLRHLSG---LITGD 57
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPelvLATGE 115
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
147-184 |
8.16e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 8.16e-04
10 20 30
....*....|....*....|....*....|....*...
gi 985002877 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-211 |
1.01e-03 |
|
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: 38.51 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 29 HGEMVALLGPSGSGKSTLLRHLSGLItgdksvgshiellgrtvqregrlardirkSRAHTGYIFqqfnlvnrlsvlenvl 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAREL-----------------------------GPPGGGVIY---------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 109 igalgstpfwrtcfswFTGEQKQRALQALTRVGMVHFahqRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESA 188
Cdd:smart00382 36 ----------------IDGEDILEEVLDQLLLIIVGG---KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
|
170 180
....*....|....*....|....*...
gi 985002877 189 RIVMDTLRD-----INQNDGITVVVTLH 211
Cdd:smart00382 97 ALLLLLEELrllllLKSEKNLTVILTTN 124
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1-46 |
1.50e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 1.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 985002877 1 MQTIIRVeKLAKTFNqhqaLHAVDLNIHHGEMVALLGPSGSGKSTL 46
Cdd:COG0178 2 MMDKIRI-RGAREHN----LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
154-251 |
1.55e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDinQNDGITVVVTLHQVDYALRyCERIVALRQGHVF- 232
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVe 1452
|
90 100
....*....|....*....|.
gi 985002877 233 YDGSSQQFDNER--FDHLYRS 251
Cdd:PLN03130 1453 FDTPENLLSNEGsaFSKMVQS 1473
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
147-184 |
1.59e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|....*...
gi 985002877 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
147-184 |
1.66e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.33 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|....*...
gi 985002877 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-231 |
1.92e-03 |
|
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: 39.04 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdKSVGShIELLGRTVQREGrLARDIRKSRAHTGYIFQQFNLVNRLS 102
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG-KFEGN-VFINGKPVDIRN-PAQAIRAGIAMVPEDRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985002877 103 VLENVLIGALGSTPFwrtcFSWFTGEQKQRALQALTRVGMVHFAHQ--RVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
Cdd:TIGR02633 356 VGKNITLSVLKSFCF----KMRIDAAAELQIIGSAIQRLKVKTASPflPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 985002877 181 ASLDPESArivMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQGHV 231
Cdd:TIGR02633 432 RGVDVGAK---YEIYKLINQlaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
33-58 |
3.25e-03 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 36.89 E-value: 3.25e-03
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
29-59 |
3.97e-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: 37.14 E-value: 3.97e-03
10 20 30
....*....|....*....|....*....|....
gi 985002877 29 HGEMVALLGPSGSGKSTLLRHLSG---LITGDKS 59
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPeldLRTGEIS 138
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
147-197 |
5.81e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.29 E-value: 5.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985002877 147 HQRVSTLSGGQQQR---VAIARALMQQ-----------AKVILaDEPIASLDPESARIVMDTLRD 197
Cdd:pfam13558 27 YRRSGGLSGGEKQLlayLPLAAALAAQygsaegrppapRLVFL-DEAFAKLDEENIRTALELLRA 90
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
30-52 |
6.08e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.61 E-value: 6.08e-03
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
32-50 |
7.64e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 35.97 E-value: 7.64e-03
|
| |
