|
Name |
Accession |
Description |
Interval |
E-value |
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-254 |
7.85e-133 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 375.93 E-value: 7.85e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivSDI 80
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGE---ILVDGQDVTALRG--RAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMPWLRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:COG3638 76 RRLRRRIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALT 240
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELT 235
|
250
....*....|....
gi 518255160 241 PALLRDLYGMQADE 254
Cdd:COG3638 236 DAVLREIYGGEAEE 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-248 |
2.02e-114 |
|
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: 329.14 E-value: 2.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivSDIRS 82
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSG---SVLIDGTDINKLKG--KALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMPWLRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALTPA 242
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
....*.
gi 518255160 243 LLRDLY 248
Cdd:cd03256 236 VLDEIY 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-249 |
1.85e-106 |
|
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: 308.84 E-value: 1.85e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivSDIRS 82
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGS---ILLEGTDITKLRG--KKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMPWLRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALTPA 242
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
....*..
gi 518255160 243 LLRDLYG 249
Cdd:TIGR02315 237 VLRHIYG 243
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-248 |
6.70e-96 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 283.06 E-value: 6.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREGRIVSDIRS 82
Cdd:PRK09984 5 IRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMPWLRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALTPA 242
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
|
....*.
gi 518255160 243 LLRDLY 248
Cdd:PRK09984 244 RFDHLY 249
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-230 |
2.63e-73 |
|
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: 223.91 E-value: 2.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGK---HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREG-RIVS 78
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE---VRVDGTDISKLSeKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 DIRsiRSQVGFVFQQFNLVDRLPVLTNVLVGRLhtmpwLRGVmgwFNAQERSAALAALERVGILDCHKQRASTLSGGQQQ 158
Cdd:cd03255 78 AFR--RRHIGFVFQSFNLLPDLTALENVELPLL-----LAGV---PKKERRERAEELLERVGLGDRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAiRYCPRVIALNQGQV 230
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-233 |
4.22e-73 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 223.77 E-value: 4.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGK---HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRI-V 77
Cdd:COG1136 4 LLELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSG---EVLIDGQDISSLSEReL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 SDIRsiRSQVGFVFQQFNLVDRLPVLTNVLvgrlhtMPWLrgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQ 157
Cdd:COG1136 81 ARLR--RRHIGFVFQFFNLLPELTALENVA------LPLL--LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAiRYCPRVIALNQGQVIYD 233
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-253 |
1.48e-71 |
|
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: 220.69 E-value: 1.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivsdiR 81
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSG---EVLLDGRDLASLSR-----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNLVDRLPVLTNVLVGRLhtmPWlRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:COG1120 72 ELARRIAYVPQEPPAPFGLTVRELVALGRY---PH-LGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG-PAAALT 240
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGpPEEVLT 227
|
250
....*....|...
gi 518255160 241 PALLRDLYGMQAD 253
Cdd:COG1120 228 PELLEEVYGVEAR 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-255 |
1.45e-66 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 207.63 E-value: 1.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgrivsdi 80
Cdd:COG1121 5 PAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSG---TVRLFGKPPRRA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 rsiRSQVGFVFQQFNLVDRLP--VLTNVLVGRLHTMPWLRgvmgWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQ 158
Cdd:COG1121 74 ---RRRIGYVPQRAEVDWDFPitVRDVVLMGRYGRRGLFR----RPSRADREAVDEALERVGLEDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAA 238
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEV 225
|
250
....*....|....*..
gi 518255160 239 LTPALLRDLYGMQADEF 255
Cdd:COG1121 226 LTPENLSRAYGGPVALL 242
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-248 |
4.21e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 203.37 E-value: 4.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregRIVSDIRS 82
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSG---EVRVLGE------DVARDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNV-LVGRLHTMPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:COG1131 71 VRRRIGYVPQEPALYPDLTVRENLrFFARLYGLP---------RKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALTP 241
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
....*..
gi 518255160 242 ALLRDLY 248
Cdd:COG1131 221 RLLEDVF 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-239 |
4.02e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 200.99 E-value: 4.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivsDIRS 82
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSG---TITVDGEDLTDSKK---DINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGrlhtmpwLRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:COG1126 75 LRRKVGMVFQQFNLFPHLTVLENVTLA-------PIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPdssRKVMEILSTIQR--EDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDP---ELVGEVLDVMRDlaKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-238 |
2.28e-62 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 196.04 E-value: 2.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivSDIRS 82
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSG---QVLVNGQDLSRLKR--REIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNV-LVgrlhtmpwLRgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:COG2884 77 LRRRIGVVFQDFRLLPDRTVYENVaLP--------LR-VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMaIRYCP-RVIALNQGQVIYDGPAAA 238
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLEL-VDRMPkRVLELEDGRLVRDEARGV 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-239 |
1.75e-59 |
|
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: 189.08 E-value: 1.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgrivsDIRS 82
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG---EVLVDGKDITKK-----NLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQ-----FNLVdrlpVLTNVLVGRLHtmpwlrgvMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQ 157
Cdd:COG1122 73 LRRKVGLVFQNpddqlFAPT----VEEDVAFGPEN--------LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAA 237
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
..
gi 518255160 238 AL 239
Cdd:COG1122 220 EV 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-230 |
2.41e-58 |
|
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: 185.43 E-value: 2.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivsDIRS 82
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSG---TIIIDGLKLTDDKK---NINE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGrlhtmpwLRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:cd03262 74 LRQKVGMVFQQFNLFPHLTVLENITLA-------PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSsrkVMEILSTIQR--EDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPEL---VGEVLDVMKDlaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-234 |
4.80e-58 |
|
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: 184.66 E-value: 4.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 4 RIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsdirsi 83
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGS---IRVFGKPLEKE---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 84 RSQVGFVFQQFNlVDR---LPVLTNVLVGRLHTMPWLRgvmgWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:cd03235 67 RKRIGYVPQRRS-IDRdfpISVRDVVLMGLYGHKGLFR----RLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGqVIYDG 234
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-239 |
1.20e-55 |
|
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: 179.40 E-value: 1.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivSDIR 81
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSG---EILVDGQDITGLSE--KELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNLVDRLPVLTNVLVG-RLHT-MPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSLTVFENVAFPlREHTdLS---------EAEIRELVLEKLELVGLPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
6.89e-55 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 178.36 E-value: 6.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFANGK---HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRiv 77
Cdd:COG1116 6 PALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSG---EVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 sdirsirsQVGFVFQQFNLVDRLPVLTNVLVGrlhtmpwLRgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQ 157
Cdd:COG1116 81 --------DRGVVFQEPALLPWLTVLDNVALG-------LE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIAL 225
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-229 |
1.09e-54 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 175.07 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRIvsdIRS 82
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSG---SILIDGEDLTDLEDE---LPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGrlhtmpwlrgvmgwfnaqersaalaalervgildchkqrastLSGGQQQRAAI 162
Cdd:cd03229 74 LRRRIGMVFQDFALFPHLTVLENIALG------------------------------------------LSGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQ 229
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-234 |
1.98e-54 |
|
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: 175.40 E-value: 1.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGqcvqregRIVSDIRS 82
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE---ILIDG-------RDVTGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGrlhtmpwLRgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:cd03259 70 ERRNIGMVFQDYALFPHLTVAENIAFG-------LK-LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-269 |
2.18e-53 |
|
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: 173.89 E-value: 2.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRIVsdirs 82
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSG---SILIDGEDVRKEPREA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 iRSQVGFVFQQFNLVDRLPVLTNV-LVGRLHTMpwlrgvmgwFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:COG4555 73 -RRQIGVLPDERGLYDRLTVRENIrYFAELYGL---------FDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGpaaalTP 241
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG-----SL 216
|
250 260 270
....*....|....*....|....*....|
gi 518255160 242 ALLRDLYGMQ--ADEFLsgsELLQSAQAQI 269
Cdd:COG4555 217 DELREEIGEEnlEDAFV---ALIGSEEGEA 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-239 |
5.47e-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: 180.10 E-value: 5.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHF----ANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivS 78
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSG---SILFDGKDLTKLSR--R 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 DIRSIRSQVGFVFQ----QFNlvdrlPVLTnvlVGRLHTMPwLRgVMGWFNAQERSA-ALAALERVGILDCHKQR-ASTL 152
Cdd:COG1123 336 SLRELRRRVQMVFQdpysSLN-----PRMT---VGDIIAEP-LR-LHGLLSRAERRErVAELLERVGLPPDLADRyPHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIY 232
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
....*..
gi 518255160 233 DGPAAAL 239
Cdd:COG1123 486 DGPTEEV 492
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-231 |
9.66e-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: 171.50 E-value: 9.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANG---KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivsd 79
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSG---EVLVDGEPVTGPGP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 irsirsQVGFVFQQFNLVDRLPVLTNVLVGrlhtmpwLRgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:cd03293 74 ------DRGYVFQQDALLPWLTVLDNVALG-------LE-LQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQ--GQVI 231
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-235 |
1.02e-52 |
|
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: 171.61 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGK---HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivSD 79
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS---VLVDGTDLTLLSG--KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQQFNLVDRLPVLTNVlvgrlhTMPwLRgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:cd03258 77 LRKARRRIGMIFQHFNLLSSRTVFENV------ALP-LE-IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGP 235
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-239 |
4.20e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 167.96 E-value: 4.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 6 QNLNKHFanGKHA-LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgSLIeVNGQCVqREGRIvsDIRSIR 84
Cdd:PRK09493 5 KNVSKHF--GPTQvLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG--DLI-VDGLKV-NDPKV--DERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 85 SQVGFVFQQFNLVDRLPVLTNVLVGRLHtmpwlrgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIAR 164
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGPLR-------VRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 165 TLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-229 |
1.36e-50 |
|
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: 165.72 E-value: 1.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 4 RIQNLNKHFANG-KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQRegrivSDIRS 82
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSG---EVLVDGKDLTK-----LSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQ-----FNLVdrlpVLTNVLVGRLHtmpwlrgvMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQ 157
Cdd:cd03225 73 LRRKVGLVFQNpddqfFGPT----VEEEVAFGLEN--------LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQ 229
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-250 |
2.14e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 165.70 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFanGKHALRdIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregrivsDIRS 82
Cdd:COG3840 2 LRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSG---RILWNGQ----------DLTA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQ---VGFVFQQFNLVDRLPVLTNVLVGrLHtmPWLRgvmgwFNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:COG3840 66 LPPAerpVSMLFQENNLFPHLTVAQNIGLG-LR--PGLK-----LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
250
....*....|....*
gi 518255160 240 T----PALLRDLYGM 250
Cdd:COG3840 218 LdgepPPALAAYLGI 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-239 |
7.21e-50 |
|
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: 164.60 E-value: 7.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivSDIRS 82
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSG---EVLIDGEDISGLSE--AELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVG-RLHTMpwlrgvmgwFNAQE-RSAALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:cd03261 75 LRRRMGMLFQSGALFDSLTVFENVAFPlREHTR---------LSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-225 |
2.50e-49 |
|
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: 162.01 E-value: 2.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 5 IQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRI-VSDIRsi 83
Cdd:TIGR03608 1 LKNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQ---VYLNGQETPPLNSKkASKFR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 84 RSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMPWLRgvmgwfnaQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIA 163
Cdd:TIGR03608 75 REKLGYLFQNFALIENETVEENLDLGLKYKKLSKK--------EKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 164 RTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHqvDMAI-RYCPRVIAL 225
Cdd:TIGR03608 147 RAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTH--DPEVaKQADRVIEL 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-238 |
5.00e-49 |
|
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: 162.22 E-value: 5.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregrivsDIRS 82
Cdd:cd03219 1 LEVRGLTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSG---SVLFDGE----------DITG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQ------VGFVFQQFNLVDRLPVLTNVLVGRLHTMP--WLRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSG 154
Cdd:cd03219 67 LPPHeiarlgIGRTFQIPRLFPELTVLENVMVAAQARTGsgLLLARARREEREARERAEELLERVGLADLADRPAGELSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 155 GQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
....
gi 518255160 235 PAAA 238
Cdd:cd03219 226 TPDE 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-238 |
5.13e-49 |
|
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: 162.90 E-value: 5.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREG--RIVs 78
Cdd:COG0411 3 PLLEVRGLTKRFG-GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSG---RILFDGRDITGLPphRIA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 dirsiRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMP--WLRGVMGWFN--AQERSA---ALAALERVGILDCHKQRAST 151
Cdd:COG0411 78 -----RLGIARTFQNPRLFPELTVLENVLVAAHARLGrgLLAALLRLPRarREEREArerAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 152 LSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVI 231
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
....*..
gi 518255160 232 YDGPAAA 238
Cdd:COG0411 233 AEGTPAE 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-239 |
6.53e-48 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 160.35 E-value: 6.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFanGKH-ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQ----REG-R 75
Cdd:COG4598 8 ALEVRDLHKSF--GDLeVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGE---IRVGGEEIRlkpdRDGeL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 76 IVSD---IRSIRSQVGFVFQQFNLVDRLPVLTNVLVGRLHtmpwlrgVMGWFNAQERSAALAALERVGILDCHKQRASTL 152
Cdd:COG4598 83 VPADrrqLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVH-------VLGRPKAEAIERAEALLAKVGLADKRDAYPAHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDssrKVMEILSTIQR--EDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDPE---LVGEVLKVMRDlaEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
....*....
gi 518255160 231 IYDGPAAAL 239
Cdd:COG4598 233 EEQGPPAEV 241
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-238 |
1.01e-47 |
|
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: 158.75 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKHA---LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQ---REGR 75
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGT---VRLAGQDLFaldEDAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 76 ivSDIRsiRSQVGFVFQQFNLVDRLPVLTNVLvgrlhtMP-WLRGVMgwfNAQERsaALAALERVGILDCHKQRASTLSG 154
Cdd:COG4181 85 --ARLR--ARHVGFVFQSFQLLPTLTALENVM------LPlELAGRR---DARAR--ARALLERVGLGHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 155 GQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRyCPRVIALNQGQVIYDG 234
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
....
gi 518255160 235 PAAA 238
Cdd:COG4181 229 AATA 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-256 |
1.03e-47 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 162.17 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGK---HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivSD 79
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGS---VLVDGVDLTALSE--RE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQQFNLVDRLPVLTNVLvgrlhtMPwLRgVMGWFNAQ--ERSAALaaLERVGILDCHKQRASTLSGGQQ 157
Cdd:COG1135 77 LRAARRKIGMIFQHFNLLSSRTVAENVA------LP-LE-IAGVPKAEirKRVAEL--LELVGLSDKADAYPSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG--- 234
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGpvl 226
|
250 260
....*....|....*....|....*..
gi 518255160 235 -----PAAALTPALLRDLYGMQADEFL 256
Cdd:COG1135 227 dvfanPQSELTRRFLPTVLNDELPEEL 253
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-239 |
1.85e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 161.47 E-value: 1.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVqregriVSDI 80
Cdd:COG1118 1 MSIEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSG---RIVLNGRDL------FTNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRLPVLTNVLVGrlhtmpwLRgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:COG1118 71 PPRERRVGFVFQHYALFPHMTVAENIAFG-------LR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDpDSSRKVMEI-LSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALD-AKVRKELRRwLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-234 |
4.35e-47 |
|
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: 155.67 E-value: 4.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 4 RIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivsdiRSI 83
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG---EILLDGKDLASLSP-----KEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 84 RSQVGFVFQqfnlvdrlpvltnvlvgrlhtmpwlrgvmgwfnaqersaalaALERVGILDCHKQRASTLSGGQQQRAAIA 163
Cdd:cd03214 72 ARKIAYVPQ------------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLA 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518255160 164 RTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03214 110 RALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-229 |
4.28e-46 |
|
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: 153.94 E-value: 4.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivSDIRS 82
Cdd:TIGR02673 2 IEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRG---QVRIAGEDVNRLRG--RQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVlvgrlhTMPwLRgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPDRTVYENV------ALP-LE-VRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQ 229
Cdd:TIGR02673 149 ARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-230 |
4.81e-46 |
|
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: 152.55 E-value: 4.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregRIVSDIRS 82
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG---EIKVLGK------DIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVlvgrlhtmpwlrgvmgwfnaqersaalaalervgildchkqrasTLSGGQQQRAAI 162
Cdd:cd03230 71 VKRRIGYLPEEPSLYENLTVRENL--------------------------------------------KLSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-274 |
1.77e-45 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 160.07 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANG-KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQRegrivSDI 80
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLE-----LSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQqfnlvDRLPVLTNVLVGRLHTMPWLRGVMGWFNAQERsaALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:COG1123 79 ALRGRRIGMVFQ-----DPMTQLNPVTVGDQIAEALENLGLSRAEARAR--VLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAalt 240
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE--- 228
|
250 260 270
....*....|....*....|....*....|....
gi 518255160 241 pALLRDLYGMQADEFLSGSELLQSAQAQIPSPVL 274
Cdd:COG1123 229 -EILAAPQALAAVPRLGAARGRAAPAAAAAEPLL 261
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-235 |
2.07e-45 |
|
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: 154.15 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 9 NKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRIvsDIRSIRSQVG 88
Cdd:TIGR04521 11 QPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGT---VTIDGRDITAKKKK--KLKDLRKKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 89 FVFQQfnlvdrlP--------VLTNVLVGRLHtmpwlrgvMGwFNAQE-RSAALAALERVGILDCHKQRAS-TLSGGQQQ 158
Cdd:TIGR04521 86 LVFQF-------PehqlfeetVYKDIAFGPKN--------LG-LSEEEaEERVKEALELVGLDEEYLERSPfELSGGQMR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGP 235
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-236 |
2.96e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 153.33 E-value: 2.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNgqcvqreGRIVSDIR 81
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSG---RILLD-------GRDVTGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNLVDRLPVLTNVLVGrlhtmpwLRgvMGWFNAQERSA-ALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:COG3842 74 PEKRNVGMVFQDYALFPHLTVAENVAFG-------LR--MRGVPKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPdSSRKVMEI-LSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV--------I 231
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDA-KLREEMREeLRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIeqvgtpeeI 223
|
....*
gi 518255160 232 YDGPA 236
Cdd:COG3842 224 YERPA 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-249 |
4.27e-44 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 150.31 E-value: 4.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQR-EGRIVSD 79
Cdd:PRK13548 1 AMLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSG---EVRLNGRPLADwSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQ---VGFVFqqfnlvdrlPVLTNVLVGRlhtMPWLRGvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQ 156
Cdd:PRK13548 77 RRAVLPQhssLSFPF---------TVEEVVAMGR---APHGLS-----RAEDDALVAAALAQVDLAHLAGRDYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 157 QQRAAIARTLVQ------GAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:PRK13548 140 QQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
250 260
....*....|....*....|
gi 518255160 231 IYDG-PAAALTPALLRDLYG 249
Cdd:PRK13548 220 VADGtPAEVLTPETLRRVYG 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-234 |
6.65e-44 |
|
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: 148.81 E-value: 6.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGK---HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivSD 79
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSG---SIIFDGKDLLKLSR--RL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQQ----FNlvdrlPVLTnvlVGRLHTMPWLRGVMGWFNAQERSAALAALERVGIL-DCHKQRASTLSG 154
Cdd:cd03257 77 RKIRRKEIQMVFQDpmssLN-----PRMT---IGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeEVLNRYPHELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 155 GQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-240 |
1.20e-43 |
|
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: 148.04 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANG-KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqregRIVSDIR 81
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT---AYINGY------SIRTDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNLVDRLPVLTNVlvgRLHTMpwLRGVmgwFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:cd03263 72 AARQSLGYCPQFDALFDELTVREHL---RFYAR--LKGL---PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALT 240
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-250 |
1.31e-43 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 148.69 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 4 RIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregrivsDIRSI 83
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSG---EVLVDGL----------DVATT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 84 RS-----QVGFVFQQFNLVDRLPVLTNVLVGRLhtmPWLRGVMgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQ 158
Cdd:COG4604 69 PSrelakRLAILRQENHINSRLTVRELVAFGRF---PYSKGRL---TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAA 238
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
250
....*....|...
gi 518255160 239 -LTPALLRDLYGM 250
Cdd:COG4604 223 iITPEVLSDIYDT 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-234 |
1.41e-43 |
|
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: 147.34 E-value: 1.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANgKHALRDIDLNIADGeMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregRIVSDIRS 82
Cdd:cd03264 1 LQLENLTKRYGK-KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSG---TIRIDGQ------DVLKQPQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVltnvlVGRLHTMPWLRGVMgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:cd03264 70 LRRRIGYLPQEFGVYPNFTV-----REFLDYIAWLKGIP---SKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdgRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-239 |
9.80e-43 |
|
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: 146.49 E-value: 9.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANG---KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivs 78
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGE---VTFDGRPVTRRRR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 diRSIRSQVGFVFQQ----FNlvdrlPVLTnvlVGRLHTMPwLRgVMGWFNAQERsaALAALERVGiLDCH--KQRASTL 152
Cdd:COG1124 75 --KAFRRRVQMVFQDpyasLH-----PRHT---VDRILAEP-LR-IHGLPDREER--IAELLEQVG-LPPSflDRYPHQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIY 232
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVE 219
|
....*..
gi 518255160 233 DGPAAAL 239
Cdd:COG1124 220 ELTVADL 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-230 |
1.31e-42 |
|
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: 145.24 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 6 QNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRivSDIRSIRS 85
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSG---TIRVNGQDVSDLRG--RAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 86 QVGFVFQQFNLVDRLPVLTNVLVGrlhtmpwLRgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIART 165
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFA-------LE-VTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 166 LVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-234 |
1.32e-42 |
|
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: 144.94 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 8 LNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREGRIVSdirsirsqv 87
Cdd:cd03298 3 LDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVS--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 88 gFVFQQFNLVDRLPVLTNVLVGRlhtMPWLRgvmgwFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLV 167
Cdd:cd03298 74 -MLFQENNLFAHLTVEQNVGLGL---SPGLK-----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 168 QGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-235 |
3.31e-42 |
|
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: 144.63 E-value: 3.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLvaDAGPGSLIEvnGQcVQREGRIVSDIR- 81
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLN--DLIPGAPDE--GE-VLLDGKDIYDLDv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 ---SIRSQVGFVFQQFNLVdRLPVLTNVLVGrlhtmPWLRGVmgWFNAQERSAALAALERVGILDCHKQR--ASTLSGGQ 156
Cdd:cd03260 75 dvlELRRRVGMVFQKPNPF-PGSIYDNVAYG-----LRLHGI--KLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 157 QQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdgRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGP 235
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-236 |
7.07e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 147.14 E-value: 7.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MA-LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNgqcvqreGRIVSD 79
Cdd:COG3839 1 MAsLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG---EILIG-------GRDVTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQQFNLVDRLPVLTNVLVG-RLHTMPwlrgvmgwfnAQERSAALA-ALERVGILDCHKQRASTLSGGQQ 157
Cdd:COG3839 70 LPPKDRNIAMVFQSYALYPHMTVYENIAFPlKLRKVP----------KAEIDRRVReAAELLGLEDLLDRKPKQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPdSSRKVMEI-LSTIQREDGRTVIVSLH-QVD---MAirycPRVIALNQGQV-- 230
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDA-KLRVEMRAeIKRLHRRLGTTTIYVTHdQVEamtLA----DRIAVMNDGRIqq 214
|
250
....*....|..
gi 518255160 231 ------IYDGPA 236
Cdd:COG3839 215 vgtpeeLYDRPA 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-230 |
5.03e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.72 E-value: 5.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHaLRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQRegrivSDIRS 82
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG---EIYLDGKPLSA-----MPPPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRlPVLTNvlvgrlhtmpwLRGVMGWFNAQ-ERSAALAALERVGI-LDCHKQRASTLSGGQQQRA 160
Cdd:COG4619 72 WRRQVAYVPQEPALWGG-TVRDN-----------LPFPFQLRERKfDRERALELLERLGLpPDILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-242 |
6.19e-41 |
|
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: 141.67 E-value: 6.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsDIRS 82
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGE---IFIDGEDIREQ-----DPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNV-LVGRLhtmpwlrgvMGWFNAQERSAALAALERVGILDCH-KQR-ASTLSGGQQQR 159
Cdd:cd03295 73 LRRKIGYVIQQIGLFPHMTVEENIaLVPKL---------LKWPKEKIRERADELLALVGLDPAEfADRyPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVI-YDGPAAA 238
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVqVGTPDEI 223
|
....*
gi 518255160 239 LT-PA 242
Cdd:cd03295 224 LRsPA 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-240 |
1.70e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 140.53 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFanGKH-ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgSLIEVNGQCVQREGRIVSD 79
Cdd:COG4161 1 MSIQLKNINCFY--GSHqALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSG--QLNIAGHQFDFSQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQQFNLVDRLPVLTNVLVGRLHtmpwlrgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:COG4161 77 IRLLRQKVGMVFQQYNLWPHLTVMENLIEAPCK-------VLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF 228
|
.
gi 518255160 240 T 240
Cdd:COG4161 229 T 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-235 |
2.23e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 143.02 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 4 RIQNLNKHFANGK---HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivSDI 80
Cdd:PRK11153 3 ELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGR---VLVDGQDLTALSE--KEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRLPVLTNVlvgrlhTMPwLRgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:PRK11153 78 RKARRQIGMIFQHFNLLSSRTVFDNV------ALP-LE-LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGP 235
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-239 |
2.39e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 140.27 E-value: 2.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSL--IEVNGQ--CVQREGRIv 77
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgdITIDTArsLSQQKGLI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 sdiRSIRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMPWLRGvmgwfNAQERSAALaaLERVGILDCHKQRASTLSGGQQ 157
Cdd:PRK11264 81 ---RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKE-----EATARAREL--LAKVGLAGKETSYPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDssrKVMEILSTIQR--EDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGP 235
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPE---LVGEVLNTIRQlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
....
gi 518255160 236 AAAL 239
Cdd:PRK11264 228 AKAL 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-227 |
5.43e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 138.00 E-value: 5.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregRIVSDI 80
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAG---EVLWNGE------PIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRLPVLTNV-LVGRLHTMPwlrgvmgwfnaQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:COG4133 71 EDYRRRLAYLGHADGLKPELTVRENLrFWAALYGLR-----------ADREAIDEALEAVGLAGLADLPVRQLSAGQKRR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTiQREDGRTVIVSLHQvDMAIRYCpRVIALNQ 227
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ-PLELAAA-RVLDLGD 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-234 |
8.11e-40 |
|
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: 137.88 E-value: 8.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGK---HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregRIVSD 79
Cdd:cd03266 2 ITADALTKRFRDVKktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG---FATVDGF------DVVKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQQFNLVDRLPVLTNVL-VGRLHTMpwlrgvmgwfnaqERSAALAALE----RVGILDCHKQRASTLSG 154
Cdd:cd03266 73 PAEARRRLGFVSDSTGLYDRLTARENLEyFAGLYGL-------------KGDELTARLEeladRLGMEELLDRRVGGFST 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 155 GQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTiQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03266 140 GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-240 |
1.10e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 138.61 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFanGKH-ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgSLIEVNGQCVQREGRIVSD 79
Cdd:PRK11124 1 MSIQLNGINCFY--GAHqALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSG--TLNIAGNHFDFSKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQQFNLVDRLPVLTNVLVGRLHtmpwlrgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPHLTVQQNLIEAPCR-------VLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCF 228
|
.
gi 518255160 240 T 240
Cdd:PRK11124 229 T 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-273 |
2.45e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 138.33 E-value: 2.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANG-KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgrivSDIR 81
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSG---KVTVDGLDTLDE----ENLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQ----QF--NLV--DrlpV---LTNvlvgrlhtmpwlRGVmgwfNAQE-RSAALAALERVGILDcHKQRA 149
Cdd:TIGR04520 74 EIRKKVGMVFQnpdnQFvgATVedD---VafgLEN------------LGV----PREEmRKRVDEALKLVGMED-FRDRE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 150 -STLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRyCPRVIALNQG 228
Cdd:TIGR04520 134 pHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKG 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 518255160 229 QVIYDGpaaalTPAllrdlygmqadEFLSGSELLQSAQAQIPSPV 273
Cdd:TIGR04520 213 KIVAEG-----TPR-----------EIFSQVELLKEIGLDVPFIT 241
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-229 |
4.35e-39 |
|
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: 134.29 E-value: 4.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 4 RIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgrivsDIRSI 83
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG---EILIDGKDIAKL-----PLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 84 RSQVGFVFQqfnlvdrlpvltnvlvgrlhtmpwlrgvmgwfnaqersaalaalervgildchkqrastLSGGQQQRAAIA 163
Cdd:cd00267 72 RRRIGYVPQ-----------------------------------------------------------LSGGQRQRVALA 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 164 RTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQ 229
Cdd:cd00267 93 RALLLNPDLLLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-242 |
4.46e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 142.46 E-value: 4.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVqregRIVSDI 80
Cdd:COG1129 3 PLLEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSG---EILLDGEPV----RFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRLPVLTNVLVGRLhtmPWLRGVMGWfnAQERSAALAALERVGI-LDcHKQRASTLSGGQQQR 159
Cdd:COG1129 75 DAQAAGIAIIHQELNLVPNLSVAENIFLGRE---PRRGGLIDW--RAMRRRARELLARLGLdID-PDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVI-VS--LHQVdMAIryCPRVIALNQGQVIYDGPA 236
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIyIShrLDEV-FEI--ADRVTVLRDGRLVGTGPV 224
|
....*.
gi 518255160 237 AALTPA 242
Cdd:COG1129 225 AELTED 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-180 |
1.34e-38 |
|
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: 132.77 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgrivsDIRSIRSQVGFVFQQFNLVD 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEG---TILLDGQDLTDD-----ERKSLRKEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 RLPVLTNVLVGRLhtmpwlrgVMGWFNAQERSAALAALERVGILDCHKQRA----STLSGGQQQRAAIARTLVQGAKLVL 174
Cdd:pfam00005 73 RLTVRENLRLGLL--------LKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLL 144
|
....*.
gi 518255160 175 ADEPIA 180
Cdd:pfam00005 145 LDEPTA 150
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-251 |
1.64e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 135.63 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHfANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQR-EGRIVSDIR 81
Cdd:COG4559 2 LEAENLSVR-LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSG---EVRLNGRPLAAwSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SI---RSQVGFVFqqfnlvdrlPVLTNVLVGRlhtMPWLRGvmgwfNAQERSAALAALERVGILDcHKQRA-STLSGGQQ 157
Cdd:COG4559 78 AVlpqHSSLAFPF---------TVEEVVALGR---APHGSS-----AAQDRQIVREALALVGLAH-LAGRSyQTLSGGEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 158 QRAAIARTLVQ-------GAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:COG4559 140 QRVQLARVLAQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
250 260
....*....|....*....|..
gi 518255160 231 IYDG-PAAALTPALLRDLYGMQ 251
Cdd:COG4559 219 VAQGtPEEVLTDELLERVYGAD 240
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-238 |
4.56e-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: 137.09 E-value: 4.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKhALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGqcvqregRIVSDIRS 82
Cdd:TIGR03265 5 LSIDNIRKRFGAFT-ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGT---IYQGG-------RDITRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGrLHTmpwlRGvMGwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:TIGR03265 74 QKRDYGIVFQSYALFPNLTVADNIAYG-LKN----RG-MG--RAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV--------IYDG 234
Cdd:TIGR03265 146 ARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIeqvgtpqeIYRH 225
|
....
gi 518255160 235 PAAA 238
Cdd:TIGR03265 226 PATP 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-236 |
5.69e-38 |
|
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: 133.52 E-value: 5.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqregrIVSDIRS 82
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGE---ILLDGK-------DITNLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVG-RLHTMPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:cd03300 70 HKRPVNTVFQNYALFPHLTVFENIAFGlRLKKLP---------KAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPdSSRKVMEI-LSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV--------IY 232
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDL-KLRKDMQLeLKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIqqigtpeeIY 219
|
....
gi 518255160 233 DGPA 236
Cdd:cd03300 220 EEPA 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-252 |
1.12e-37 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 140.74 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFA-NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregrivsDI 80
Cdd:COG2274 473 DIELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG---RILIDGI----------DL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSI-----RSQVGFVFQQFNLVDRlPVLTNVLVGRLHTmpwlrgvmgwfnaqERSAALAALERVGILD---CHKQ----- 147
Cdd:COG2274 540 RQIdpaslRRQIGVVLQDVFLFSG-TIRENITLGDPDA--------------TDEEIIEAARLAGLHDfieALPMgydtv 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 148 ---RASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDMaIRYCPRVIA 224
Cdd:COG2274 605 vgeGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLST-IRLADRIIV 681
|
250 260 270
....*....|....*....|....*....|
gi 518255160 225 LNQGQVIYDGPAAALTPA--LLRDLYGMQA 252
Cdd:COG2274 682 LDKGRIVEDGTHEELLARkgLYAELVQQQL 711
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-275 |
1.19e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.47 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsdir 81
Cdd:COG4152 1 MLELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE---VLWDGEPLDPE-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 sIRSQVGFV------FQQFNLVDRLpvltnVLVGRLHTMPWlrgvmgwfnAQERSAALAALERVGILDCHKQRASTLSGG 155
Cdd:COG4152 69 -DRRRIGYLpeerglYPKMKVGEQL-----VYLARLKGLSK---------AEAKRRADEWLERLGLGDRANKKVEELSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 156 QQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTiQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGP 235
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 236 AAAL---------------TPALLRDLYGMQADEFLSGSELLQSAQAQIPSPVLA 275
Cdd:COG4152 213 VDEIrrqfgrntlrleadgDAGWLRALPGVTVVEEDGDGAELKLEDGADAQELLR 267
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-231 |
1.98e-37 |
|
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: 133.15 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 18 ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivSDIRSIRSQ-VGFVFQQFNL 96
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK---VLIDGQDIAAMSR--KELRELRRKkISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 97 VDRLPVLTNVLVGrLHtmpwLRGVmgwfNAQERSA-ALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLA 175
Cdd:cd03294 114 LPHRTVLENVAFG-LE----VQGV----PRAEREErAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 176 DEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVI 231
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-252 |
3.84e-37 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 132.06 E-value: 3.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegriVSDi 80
Cdd:PRK11231 1 MTLRTENLTVGYGT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGT---VFLGDKPISM----LSS- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRLPVLTNVLVGRlhtMPWLrGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:PRK11231 72 RQLARRLALLPQHHLTPEGITVRELVAYGR---SPWL-SLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG-PAAAL 239
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGtPEEVM 226
|
250
....*....|...
gi 518255160 240 TPALLRDLYGMQA 252
Cdd:PRK11231 227 TPGLLRTVFDVEA 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-238 |
1.35e-36 |
|
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: 130.15 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFANGKhALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslievngqcVQREGRIVSDI 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGT----------ILFGGEDATDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRLPVLTNVLVGrLHTMPwlrgVMGWFNAQERSAALAALERVGILDCHKQR-ASTLSGGQQQR 159
Cdd:cd03296 70 PVQERNVGFVFQHYALFRHMTVFDNVAFG-LRVKP----RSERPPEAEIRAKVHELLKLVQLDWLADRyPAQLSGGQRQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV--------I 231
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIeqvgtpdeV 224
|
....*..
gi 518255160 232 YDGPAAA 238
Cdd:cd03296 225 YDHPASP 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-239 |
4.23e-36 |
|
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: 128.32 E-value: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFanGK-HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqregrivsDIR 81
Cdd:cd03224 1 LEVENLNAGY--GKsQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGS---IRFDGR----------DIT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQ------VGFVFQQFNLVDRLPVLTNVLVGRLhtmpwlrgvmgwfnAQERSAALAALERV----GIL-DCHKQRAS 150
Cdd:cd03224 66 GLPPHeraragIGYVPEGRRIFPELTVEENLLLGAY--------------ARRRAKRKARLERVyelfPRLkERRKQLAG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 151 TLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:cd03224 132 TLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
....*....
gi 518255160 231 IYDGPAAAL 239
Cdd:cd03224 211 VLEGTAAEL 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-235 |
8.01e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.61 E-value: 8.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCvqregriVSDIRS 82
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR---IMLDGQD-------ITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVG-RLHTMPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:PRK09452 84 ENRHVNTVFQSYALFPHMTVFENVAFGlRMQKTP---------AAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPdSSRKVMEI-LSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGP 235
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDY-KLRKQMQNeLKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-234 |
1.15e-35 |
|
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: 127.01 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsdirs 82
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE---VLFDGKPLDIA--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVL-VGRLHTMPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:cd03269 68 ARNRIGYLPEERGLYPKMKVIDQLVyLAQLKGLK---------KEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-245 |
1.38e-35 |
|
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: 129.79 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGK---HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREGRivSD 79
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSE--KE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIR-SQVGFVFQQ----FNlvdrlPVLTnvlVGRLHTMP-WLRGVMGWFNAQERsaALAALERVGILDcHKQRAS--- 150
Cdd:COG0444 80 LRKIRgREIQMIFQDpmtsLN-----PVMT---VGDQIAEPlRIHGGLSKAEARER--AIELLERVGLPD-PERRLDryp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 151 -TLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVI-VSlHqvDMA-IRY-CPRVIALN 226
Cdd:COG0444 149 hELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILfIT-H--DLGvVAEiADRVAVMY 225
|
250 260
....*....|....*....|....*..
gi 518255160 227 QGQVIYDGPAAAL--------TPALLR 245
Cdd:COG0444 226 AGRIVEEGPVEELfenprhpyTRALLS 252
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-239 |
1.47e-35 |
|
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: 127.10 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 5 IQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSlieVNGQcvqregRIVSDIRSIR 84
Cdd:cd03265 3 VENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT---VAGH------DVVREPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 85 SQVGFVFQQFNLVDRLPVLTNVLV-GRLHTMPWLRgvmgwfnAQERSAALaaLERVGILDCHKQRASTLSGGQQQRAAIA 163
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIhARLYGVPGAE-------RRERIDEL--LDFVGLLEAADRLVKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 164 RTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-264 |
1.66e-35 |
|
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: 129.05 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 10 KHFANGKhALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSlieVNGQCVQREGRIVsdirsiRSQVGF 89
Cdd:TIGR01188 1 KVYGDFK-AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTAR---VAGYDVVREPRKV------RRSIGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 90 VFQQFNLVDRLPVLTN-VLVGRLHTMPWLRgvmgwfnAQERSAALaaLERVGILDCHKQRASTLSGGQQQRAAIARTLVQ 168
Cdd:TIGR01188 71 VPQYASVDEDLTGRENlEMMGRLYGLPKDE-------AEERAEEL--LELFELGEAADRPVGTYSGGMRRRLDIAASLIH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 169 GAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALTPAL----- 243
Cdd:TIGR01188 142 QPDVLFLDEPTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLgkdtl 220
|
250 260
....*....|....*....|....
gi 518255160 244 ---LRDLYGMQADEFLSGSELLQS 264
Cdd:TIGR01188 221 esrPRDIQSLKVEVSMLIAELGET 244
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-235 |
1.68e-35 |
|
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: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAglLVADAGPGSLIEvnGQCVQREGRIVS--- 78
Cdd:TIGR00972 1 AIEIENLNLFY-GEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLN--RMNDLVPGVRIE--GKVLFDGQDIYDkki 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 DIRSIRSQVGFVFQQFNLVDrLPVLTNVLVG-RLHtmpwlrGVMGwfNAQERSAALAALERVGILDCHKQRAST----LS 153
Cdd:TIGR00972 76 DVVELRRRVGMVFQKPNPFP-MSIYDNIAYGpRLH------GIKD--KKELDEIVEESLKKAALWDEVKDRLHDsalgLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILstIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYD 233
Cdd:TIGR00972 147 GGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELI--QELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEY 224
|
..
gi 518255160 234 GP 235
Cdd:TIGR00972 225 GP 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-259 |
2.60e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 127.39 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFanGKH-ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQ----REGRI- 76
Cdd:PRK10619 6 LNVIDLHKRY--GEHeVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGS---IVVNGQTINlvrdKDGQLk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 77 VSD---IRSIRSQVGFVFQQFNLVDRLPVLTNVLVGRLHtmpwlrgVMGWFNAQERSAALAALERVGILDCHKQR-ASTL 152
Cdd:PRK10619 81 VADknqLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQ-------VLGLSKQEARERAVKYLAKVGIDERAQGKyPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIY 232
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
250 260
....*....|....*....|....*....
gi 518255160 233 DGPAAAL--TPALLRdlygmqADEFLSGS 259
Cdd:PRK10619 233 EGAPEQLfgNPQSPR------LQQFLKGS 255
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-223 |
4.29e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 125.04 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 14 NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslievngQCVQREGRivsdirsirsQVGFVFQQ 93
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG---------TVRRAGGA----------RVAYVPQR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 FNLVDRLP--VLTNVLVGRlhtmpW-LRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGA 170
Cdd:NF040873 64 SEVPDSLPltVRDLVAMGR-----WaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518255160 171 KLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVI 223
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVL 190
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-239 |
5.15e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.85 E-value: 5.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 23 DLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregrivsDIRSI---RSQVGFVFQQFNLVDR 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASG---SLTLNGQ----------DHTTTppsRRPVSMLFQENNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 100 LPVLTNVLVGrLHtmPWLRgvmgwFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADEPI 179
Cdd:PRK10771 86 LTVAQNIGLG-LN--PGLK-----LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 180 ASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-236 |
1.15e-34 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 132.16 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHA---LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLlvaDAGPGSLIEVNGQCV-QREGRIVS 78
Cdd:PRK10535 5 LELKDIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCL---DKPTSGTYRVAGQDVaTLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 DIRsiRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTmpwlrgvmGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQ 158
Cdd:PRK10535 82 QLR--REHFGFIFQRYHLLSHLTAAQNVEVPAVYA--------GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRyCPRVIALNQGQVIYDGPA 236
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-247 |
1.35e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.53 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQregrivsdI 80
Cdd:COG3845 4 PALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG---EILIDGKPVR--------I 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RS----IRSQVGFVFQQFNLVDRLPVLTNVLVGRlhtMPWLRGVMGWFNAQERSAALAalERVGI-LDCHKqRASTLSGG 155
Cdd:COG3845 72 RSprdaIALGIGMVHQHFMLVPNLTVAENIVLGL---EPTKGGRLDRKAARARIRELS--ERYGLdVDPDA-KVEDLSVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 156 QQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVI-VS--LHQVdMAIryCPRVIALNQGQVIY 232
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIfIThkLREV-MAI--ADRVTVLRRGKVVG 221
|
250
....*....|....*
gi 518255160 233 DGPAAALTPALLRDL 247
Cdd:COG3845 222 TVDTAETSEEELAEL 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-230 |
2.00e-34 |
|
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: 123.90 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNgqcvqreGRIVSDIRS 82
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGR---IYIG-------GRDVTDLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVG-RLHTMPwlRGVMgwfNAQERSAAlAALERVGILDchkQRASTLSGGQQQRAA 161
Cdd:cd03301 70 KDRDIAMVFQNYALYPHMTVYDNIAFGlKLRKVP--KDEI---DERVREVA-ELLQIEHLLD---RKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-229 |
2.13e-34 |
|
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: 122.49 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKH-ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQRegrivSDIR 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG---EILIDGVDLRD-----LDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNLVDRlPVLTNVLvgrlhtmpwlrgvmgwfnaqersaalaalervgildchkqrastlSGGQQQRAA 161
Cdd:cd03228 73 SLRKNIAYVPQDPFLFSG-TIRENIL---------------------------------------------SGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILStiQREDGRTVIVSLHQVDMaIRYCPRVIALNQGQ 229
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALR--ALAKGKTVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-262 |
2.99e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 124.81 E-value: 2.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANG----KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgrivS 78
Cdd:COG1101 2 LELKNLSKTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSG---SILIDGKDVTKL----P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 DIRsiRSQ-VGFVFQqfnlvD-------RLPVLTNVLV--GRLHTMPWLRGVmgwfNAQERSAALAALERVGI-LDCH-K 146
Cdd:COG1101 75 EYK--RAKyIGRVFQ-----DpmmgtapSMTIEENLALayRRGKRRGLRRGL----TKKRRELFRELLATLGLgLENRlD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 147 QRASTLSGGQQQraaiARTLV----QGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRV 222
Cdd:COG1101 144 TKVGLLSGGQRQ----ALSLLmatlTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 518255160 223 IALNQGQVIYD--GPA-AALTPAllrDLYGM----QADEFLSGSELL 262
Cdd:COG1101 220 IMMHEGRIILDvsGEEkKKLTVE---DLLELfeeiRGEELADDRLLL 263
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-246 |
3.87e-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: 126.75 E-value: 3.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 21 DIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRIVsDIRSIRSQVGFVFQQFNLVDRL 100
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSG---RIRLGGEVLQDSARGI-FLPPHRRRIGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 101 PVLTNVLVGRlhtmpwlrgvmgWFN-AQERSAALAAL-ERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADEP 178
Cdd:COG4148 93 SVRGNLLYGR------------KRApRAERRISFDEVvELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 179 IASLDPDSSRKVMEILSTIQRE-DGRTVIVSlHQVDMAIRYCPRVIALNQGQVIYDGPAA------ALTPALLRD 246
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDElDIPILYVS-HSLDEVARLADHVVLLEQGRVVASGPLAevlsrpDLLPLAGGE 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-239 |
3.89e-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: 129.88 E-value: 3.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgrivsDIR 81
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG---SILINGVDLSDL-----DPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQfnlvdrlPVL---T---NVLVGRlhtmpwlrgvmgwFNAQErSAALAALERVGILDCHKQ-------- 147
Cdd:COG4988 408 SWRRQIAWVPQN-------PYLfagTireNLRLGR-------------PDASD-EELEAALEAAGLDEFVAAlpdgldtp 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 148 ---RASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDMaIRYCPRVIA 224
Cdd:COG4988 467 lgeGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL-LAQADRILV 543
|
250
....*....|....*
gi 518255160 225 LNQGQVIYDGPAAAL 239
Cdd:COG4988 544 LDDGRIVEQGTHEEL 558
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
14-250 |
4.43e-34 |
|
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: 124.04 E-value: 4.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 14 NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGslIEVNGQcvqREGRIvsDIRSIRSQVGFV--F 91
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGND--VRLFGE---RRGGE--DVWELRKRIGLVspA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 92 QQFNLVDRLPVLTNVLVGrlhtmpwLRGVMGWFN---AQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQ 168
Cdd:COG1119 87 LQLRFPRDETVLDVVLSG-------FFDSIGLYReptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 169 GAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVI-VSlHQVDMAIRYCPRVIALNQGQVIYDGPAAA-LTPALLRD 246
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVT-HHVEEIPPGITHVLLLKDGRVVAAGPKEEvLTSENLSE 238
|
....
gi 518255160 247 LYGM 250
Cdd:COG1119 239 AFGL 242
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
1.31e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.80 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCV--QREGrivsdI 80
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGR---ILFDGKPIdySRKG-----L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQ-FNLVDRLPVLTNVLVGRLHtmpwlrgvMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:PRK13636 78 MKLRESVGMVFQDpDNQLFSASVYQDVSFGAVN--------LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-252 |
3.74e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 124.95 E-value: 3.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivSDI 80
Cdd:PRK09536 2 PMIDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT---VLVAGDDVEA-----LSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRLPVLTNVLVGRL-HtmpwlRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:PRK09536 73 RAASRRVASVPQDTSLSFEFDVRQVVEMGRTpH-----RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG-PAAA 238
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGpPADV 226
|
250
....*....|....
gi 518255160 239 LTPALLRDLYGMQA 252
Cdd:PRK09536 227 LTADTLRAAFDART 240
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-234 |
3.83e-33 |
|
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: 120.48 E-value: 3.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIA---DGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQrEGRIVSDIRSIRSQVGFVFQQFN 95
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGG---TIVLNGTVLF-DSRKKINLPPQQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 LVDRLPVLTNVLVGrlhtMPWLRgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLA 175
Cdd:cd03297 86 LFPHLNVRENLAFG----LKRKR------NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 176 DEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-228 |
7.10e-33 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 119.82 E-value: 7.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANG---KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREGRIVsd 79
Cdd:NF038007 2 LNMQNAEKCYITKtikTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKII-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRsiRSQVGFVFQQFNLVDRLPVLTNVlvgrlhTMPW-LRGVmgwfNAQERSAALA-ALERVGILDCHKQRASTLSGGQQ 157
Cdd:NF038007 80 LR--RELIGYIFQSFNLIPHLSIFDNV------ALPLkYRGV----AKKERIERVNqVLNLFGIDNRRNHKPMQLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIVSLHQVDmAIRYCPRVIALNQG 228
Cdd:NF038007 148 QRVAIARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYIN-QKGTTIIMVTHSDE-ASTYGNRIINMKDG 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-230 |
7.89e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 120.27 E-value: 7.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHA---LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREGRIvsd 79
Cdd:PRK10584 7 VEVHHLKKSVGQGEHElsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 irSIRSQ-VGFVFQQFNLVDRLPVLTNVLVGRLhtmpwLRGVMgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQ 158
Cdd:PRK10584 84 --KLRAKhVGFVFQSFMLIPTLNALENVELPAL-----LRGES---SRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRyCPRVIALNQGQV 230
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-239 |
1.26e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 119.70 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREG--RIVs 78
Cdd:COG0410 2 PMLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGS---IRFDGEDITGLPphRIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 dirsiRSQVGFVFQQFNLVDRLPVLTNvlvgrlhtmpwLRgvMGWFNAQERSAALAALERVG----IL-DCHKQRASTLS 153
Cdd:COG0410 77 -----RLGIGYVPEGRRIFPSLTVEEN-----------LL--LGAYARRDRAEVRADLERVYelfpRLkERRRQRAGTLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYD 233
Cdd:COG0410 139 GGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
....*.
gi 518255160 234 GPAAAL 239
Cdd:COG0410 218 GTAAEL 223
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-268 |
2.83e-32 |
|
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: 121.88 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 15 GKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRIvsDIRSI-RSQVGFVFQQ 93
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQ---IFIDGENIMKQSPV--ELREVrRKKIGMVFQQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 FNLVDRLPVLTNVLVGrlhtmPWLRGVmgwfNAQER-SAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKL 172
Cdd:TIGR01186 80 FALFPHMTILQNTSLG-----PELLGW----PEQERkEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 173 VLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGpaaalTP-ALLRDLYGMQ 251
Cdd:TIGR01186 151 LLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVG-----TPdEILRNPANEY 225
|
250
....*....|....*..
gi 518255160 252 ADEFLSGSELLQSAQAQ 268
Cdd:TIGR01186 226 VEEFIGKVDLSQVFDAE 242
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-262 |
3.23e-32 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 119.71 E-value: 3.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivsdiRS 82
Cdd:PRK10253 8 LRGEQLTLGYGK-YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGH---VWLDGEHIQHYAS-----KE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMPwlrgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:PRK10253 79 VARRIGLLAQNATTPGDITVQELVARGRYPHQP----LFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG-PAAALTP 241
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGaPKEIVTA 234
|
250 260
....*....|....*....|....
gi 518255160 242 ALLRDLYGMQA---DEFLSGSELL 262
Cdd:PRK10253 235 ELIERIYGLRCmiiDDPVAGTPLV 258
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-233 |
4.26e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 116.37 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGkHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqrEGRIVSDIRS 82
Cdd:cd03216 1 LELRGITKRFGGV-KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE---ILVDGK----EVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQqfnlvdrlpvltnvlvgrlhtmpwlrgvmgwfnaqersaalaalervgildchkqrastLSGGQQQRAAI 162
Cdd:cd03216 73 RRAGIAMVYQ-----------------------------------------------------------LSVGERQMVEI 93
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVI-VSlHQVDMAIRYCPRVIALNQGQVIYD 233
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIfIS-HRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-234 |
6.92e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 117.82 E-value: 6.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKhaLRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLievngqcvqrEGRIVSDIRS 82
Cdd:cd03299 1 LKVENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL----------NGKDITNLPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVG-RLHTMPWLrgvmgwfNAQERSAALAalERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:cd03299 69 EKRDISYVPQNYALFPHMTVYKNIAYGlKKRKVDKK-------EIERKVLEIA--EMLGIDHLLNRKPETLSGGEQQRVA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-234 |
8.16e-32 |
|
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: 116.93 E-value: 8.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsdiRS 82
Cdd:cd03268 1 LKTNDLTKTYG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE---ITFDGKSYQKN-------IE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGfvfqqfNLVDRlPVLTNVLVGRLHTMPWLRGVMGWFNAQERsaalaALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:cd03268 70 ALRRIG------ALIEA-PGFYPNLTARENLRLLARLLGIRKKRIDE-----VLDVVGLKDSAKKKVKGFSLGMKQRLGI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-216 |
1.09e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 118.04 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFANG---KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGriv 77
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGE---ITLDGVPVTGPG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 sdirsirSQVGFVFQQFNLVDRLPVLTNVLVG-RLHTMPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQ 156
Cdd:COG4525 76 -------ADRGVVFQKDALLPWLNVLDNVAFGlRLRGVP---------KAERRARAEELLALVGLADFARRRIWQLSGGM 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 157 QQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAI 216
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEAL 199
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-254 |
1.59e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 122.58 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLvaDAGPGSlIEVNGQcvqregrivsDIR 81
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY--DPTSGR-ILIDGV----------DIR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 -----SIRSQVGFVFQQFNLVDRlPVLTNVLVGRLH-TMPWLrgvmgwfnaqERSAALAALE------------RVGild 143
Cdd:COG1132 406 dltleSLRRQIGVVPQDTFLFSG-TIRENIRYGRPDaTDEEV----------EEAAKAAQAHefiealpdgydtVVG--- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 144 chkQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDmAIRYCPRVI 223
Cdd:COG1132 472 ---ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRIL 545
|
250 260 270
....*....|....*....|....*....|...
gi 518255160 224 ALNQGQVIYDGPAAAL--TPALLRDLYGMQADE 254
Cdd:COG1132 546 VLDDGRIVEQGTHEELlaRGGLYARLYRLQFGE 578
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-240 |
1.73e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.91 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsDIR 81
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGR---VKVMGREVNAE-----NEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNlvDRL---PVLTNVLVGRLHtmpwlrgvMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQ 158
Cdd:PRK13647 76 WVRSKVGLVFQDPD--DQVfssTVWDDVAFGPVN--------MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAA 238
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSL 224
|
..
gi 518255160 239 LT 240
Cdd:PRK13647 225 LT 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
15-239 |
2.36e-31 |
|
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: 119.45 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 15 GKHALrDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQrEGRIVSDIRSIRSQVGFVFQQF 94
Cdd:TIGR02142 10 GDFSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGE---IVLNGRTLF-DSRKGIFLPPEKRRIGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 95 NLVDRLPVLTNVLVGRLHTMPWLRGVmgwfnaqeRSAALAALerVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVL 174
Cdd:TIGR02142 85 RLFPHLSVRGNLRYGMKRARPSERRI--------SFERVIEL--LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 175 ADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
2.65e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 118.26 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFaNGK-----HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREGR 75
Cdd:PRK13651 1 MQIKVKNIVKIF-NKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 76 I----------------VSDIRSIRSQVGFVFQ--QFNLVDRlPVLTNVLVGRLHtmpwlrgvMGWFNAQERSAALAALE 137
Cdd:PRK13651 80 KekvleklviqktrfkkIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVS--------MGVSKEEAKKRAAKYIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 138 RVGILDCHKQRAS-TLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAI 216
Cdd:PRK13651 151 LVGLDESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVL 229
|
250
....*....|....*...
gi 518255160 217 RYCPRVIALNQGQVIYDG 234
Cdd:PRK13651 230 EWTKRTIFFKDGKIIKDG 247
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
8-230 |
3.96e-31 |
|
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: 115.34 E-value: 3.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 8 LNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGrivsdirSIRSQV 87
Cdd:TIGR01277 3 LDKVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGS---IKVNDQSHTGLA-------PYQRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 88 GFVFQQFNLVDRLPVLTNVLVGrLHtmPWLRgvmgwFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLV 167
Cdd:TIGR01277 73 SMLFQENNLFAHLTVRQNIGLG-LH--PGLK-----LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 168 QGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:TIGR01277 145 RPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-234 |
4.00e-31 |
|
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: 114.57 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSlIEVNGqcvqregrIVSDIRSIRSQVGFVFQQFNLVD 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGE-VLING--------RPLDKRSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 RLPVLTNVlvgrlhtmpwlrgvmgWFNAQERSaalaalervgildchkqrastLSGGQQQRAAIARTLVQGAKLVLADEP 178
Cdd:cd03213 96 TLTVRETL----------------MFAAKLRG---------------------LSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 179 IASLDPDSSRKVMEILSTIqREDGRTVIVSLHQV-DMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-250 |
5.24e-31 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 116.43 E-value: 5.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 15 GKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivSDIRSIRSQVGFVFQQF 94
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGE---ILLDAQPLES-----WSSKAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 95 NLVDRLPVLTNVLVGRlhtMPWlRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVL 174
Cdd:PRK10575 95 PAAEGMTVRELVAIGR---YPW-HGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 175 ADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALT-PALLRDLYGM 250
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMrGETLEQIYGI 247
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-235 |
8.19e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.27 E-value: 8.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANG-KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgrivsDIR 81
Cdd:PRK13635 6 IRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAG---TITVGGMVLSEE-----TVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQ----QFnlvdrlpVLTNV---LVGRL--HTMPwlRGVMgwfnaQERSAAlaALERVGILDCHKQRASTL 152
Cdd:PRK13635 78 DVRRQVGMVFQnpdnQF-------VGATVqddVAFGLenIGVP--REEM-----VERVDQ--ALRQVGMEDFLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRyCPRVIALNQGQVIY 232
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
...
gi 518255160 233 DGP 235
Cdd:PRK13635 221 EGT 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-270 |
1.51e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.56 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGrivSDIRS 82
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGE---VLIKGEPIKYDK---KSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQqfNLVDRL---PVLTNVLVGRLHtmpwlrgvMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:PRK13639 76 VRKTVGIVFQ--NPDDQLfapTVEEDVAFGPLN--------LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGpaaal 239
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEG----- 219
|
250 260 270
....*....|....*....|....*....|.
gi 518255160 240 TPallrdlygmqaDEFLSGSELLQSAQAQIP 270
Cdd:PRK13639 220 TP-----------KEVFSDIETIRKANLRLP 239
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-217 |
2.40e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 113.76 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGK---HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLlvaDAGPGSLIEVNGQCV-QREGRIVS 78
Cdd:PRK11629 6 LQCDNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQPMsKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 DIRSirSQVGFVFQQFNLVDRLPVLTNVlvgrlhTMPWLRGVMGWFNAQERsaALAALERVGILDCHKQRASTLSGGQQQ 158
Cdd:PRK11629 83 ELRN--QKLGFIYQFHHLLPDFTALENV------AMPLLIGKKKPAEINSR--ALEMLAAVGLEHRANHRPSELSGGERQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIR 217
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-248 |
2.51e-30 |
|
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: 119.10 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKH-ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgrivsDI 80
Cdd:COG4987 333 SLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG---SITLGGVDLRDL-----DE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRlPVLTNVLVGRLhtmpwlrgvmgwfNAQERsAALAALERVGI----------LDCH-KQRA 149
Cdd:COG4987 405 DDLRRRIAVVPQRPHLFDT-TLRENLRLARP-------------DATDE-ELWAALERVGLgdwlaalpdgLDTWlGEGG 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 150 STLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDmAIRYCPRVIALNQGQ 229
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLEDGR 546
|
250 260
....*....|....*....|.
gi 518255160 230 VIYDGPAAAL--TPALLRDLY 248
Cdd:COG4987 547 IVEQGTHEELlaQNGRYRQLY 567
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-230 |
2.77e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 116.34 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFANGKhALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivsdI 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH---IRFHGTDVSR-------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRLPVLTNVLVGrLHTMPwlrgvmgwfnAQER--SAALAA-----LERVGILDCHKQRASTLS 153
Cdd:PRK10851 70 HARDRKVGFVFQHYALFRHMTVFDNIAFG-LTVLP----------RRERpnAAAIKAkvtqlLEMVQLAHLADRYPAQLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:PRK10851 139 GGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-270 |
2.82e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.70 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLN-KHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsDI 80
Cdd:PRK13632 7 MIKVENVSfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGE---IKIDGITISKE-----NL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQ----QF---NLVDRLPV-LTNVLVGRlhtmpwlrGVMgwfnaqeRSAALAALERVGILDCHKQRASTL 152
Cdd:PRK13632 79 KEIRKKIGIIFQnpdnQFigaTVEDDIAFgLENKKVPP--------KKM-------KDIIDDLAKKVGMEDYLDKEPQNL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRyCPRVIALNQGQVIY 232
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIA 222
|
250 260 270
....*....|....*....|....*....|....*...
gi 518255160 233 DGpaaalTPallrdlygmqaDEFLSGSELLQSAQAQIP 270
Cdd:PRK13632 223 QG-----KP-----------KEILNNKEILEKAKIDSP 244
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-233 |
2.90e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 114.39 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVAD-----AGPGSLIEVngqcvqREgriv 77
Cdd:PRK11247 13 LLLNAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSagellAGTAPLAEA------RE---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 sDIRsirsqvgFVFQQFNLVDRLPVLTNVLVGrlhtmpwLRGvmGWfnaqeRSAALAALERVGILDCHKQRASTLSGGQQ 157
Cdd:PRK11247 82 -DTR-------LMFQDARLLPWKKVIDNVGLG-------LKG--QW-----RDAALQALAAVGLADRANEWPAALSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYD 233
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-235 |
3.91e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.98 E-value: 3.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLR-------MVAGLLVAdagpGSlIEVNGQCVQREG 74
Cdd:COG1117 11 KIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARVE----GE-ILLDGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 75 RivsDIRSIRSQVGFVFQQFNLvdrLP--VLTNVLVG-RLHtmpwlrgvmGWFNAQERSAAL-AALERVGIL----DCHK 146
Cdd:COG1117 85 V---DVVELRRRVGMVFQKPNP---FPksIYDNVAYGlRLH---------GIKSKSELDEIVeESLRKAALWdevkDRLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 147 QRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILS------TIqredgrtVIV--SLHQvdmAIRY 218
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILelkkdyTI-------VIVthNMQQ---AARV 219
|
250
....*....|....*..
gi 518255160 219 CPRVIALNQGQVIYDGP 235
Cdd:COG1117 220 SDYTAFFYLGELVEFGP 236
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-239 |
4.12e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 115.18 E-value: 4.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgRivsdiRSIRSQVGFVFQQfn 95
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSG---EVRVLGYVPFKR-R-----KEFARRIGVVFGQ-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 lvdR------LPVL-TNVLVGRLHTMPWLRgvmgwfnAQERSAALAALERVG-ILDchkQRASTLSGGQQQRAAIARTLV 167
Cdd:COG4586 104 ---RsqlwwdLPAIdSFRLLKAIYRIPDAE-------YKKRLDELVELLDLGeLLD---TPVRQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518255160 168 QGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHqvDMA--IRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSH--DMDdiEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-230 |
6.45e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 112.28 E-value: 6.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivSDIRS 82
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGK---IWFSGHDITRLKN--REVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVlvgrlhTMPWLrgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNV------AIPLI--IAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-235 |
6.48e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.99 E-value: 6.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFANG----KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRI 76
Cdd:PRK13637 1 MSIKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGK---IIIDGVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 77 VSDirsIRSQVGFVFQ--QFNLVDRlPVLTNVLVGRLHtmpwlrgvMGWFNAQERSAALAALERVGI-LDCHKQRAS-TL 152
Cdd:PRK13637 78 LSD---IRKKVGLVFQypEYQLFEE-TIEKDIAFGPIN--------LGLSEEEIENRVKRAMNIVGLdYEDYKDKSPfEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIY 232
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCEL 225
|
...
gi 518255160 233 DGP 235
Cdd:PRK13637 226 QGT 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-270 |
1.08e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREgrivsDIRSIRSQVGFVFQ--- 92
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAK-----TVWDIREKVGIVFQnpd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 93 -QF---NLVDRLPV-LTNVLVGRLHTMPWLRGVmgwfnaqersaalaaLERVGILDCHKQRASTLSGGQQQRAAIARTLV 167
Cdd:PRK13640 95 nQFvgaTVGDDVAFgLENRAVPRPEMIKIVRDV---------------LADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 168 QGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIrYCPRVIALNQGQVIYDGpaaalTPAllrdl 247
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQG-----SPV----- 228
|
250 260
....*....|....*....|...
gi 518255160 248 ygmqadEFLSGSELLQSAQAQIP 270
Cdd:PRK13640 229 ------EIFSKVEMLKEIGLDIP 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-234 |
1.29e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.19 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLievnGQCVQREGRIVSDIRSIRSQVGFVFQ--Q 93
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI----GERVITAGKKNKKLKPLRKKVGIVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 FNLVDRlPVLTNVLVGRLHtmpwlrgvmgwFNAQERSA---ALAALERVGILDCHKQRAS-TLSGGQQQRAAIARTL-VQ 168
Cdd:PRK13634 96 HQLFEE-TVEKDICFGPMN-----------FGVSEEDAkqkAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLaME 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 169 GAKLVLaDEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:PRK13634 164 PEVLVL-DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-229 |
2.17e-29 |
|
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: 110.99 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFA----NGK--HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAG------PGSLIEVngqcV 70
Cdd:COG4778 5 LEVENLSKTFTlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsilvrhDGGWVDL----A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 71 QREGRIVSDIRsiRSQVGFVFQQFNLVDRLPVLTNVlvgrlhTMPWLRgvMGWFNAQERSAALAALERVGIldchKQR-- 148
Cdd:COG4778 81 QASPREILALR--RRTIGYVSQFLRVIPRVSALDVV------AEPLLE--RGVDREEARARARELLARLNL----PERlw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 149 ---ASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIAL 225
Cdd:COG4778 147 dlpPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDV 225
|
....
gi 518255160 226 NQGQ 229
Cdd:COG4778 226 TPFS 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-234 |
3.31e-29 |
|
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: 110.88 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 10 KHFANGKH----ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGqcvqregrIVSDIRSIR- 84
Cdd:cd03267 24 KSLFKRKYreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE---VRVAG--------LVPWKRRKKf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 85 -SQVGFVFQQFN-LVDRLPVL-TNVLVGRLHTMPWLRgvmgwfnAQERSAALAALERVG-ILDchkQRASTLSGGQQQRA 160
Cdd:cd03267 93 lRRIGVVFGQKTqLWWDLPVIdSFYLLAAIYDLPPAR-------FKKRLDELSELLDLEeLLD---TPVRQLSLGQRMRA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-234 |
9.61e-29 |
|
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: 109.55 E-value: 9.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqregRIVSDIRS 82
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGK---ILLDGQ------DITKLPMH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVF--QQFNLVDRLPVLTNVLVGrLHTMPWLRgvmgwfnAQERSAALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:cd03218 71 KRARLGIGYlpQEASIFRKLTVEENILAV-LEIRGLSK-------KEREEKLEELLEEFHITHLRKSKASSLSGGERRRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSsrkVMEILSTIQ--REDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDPIA---VQDIQKIIKilKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEG 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-215 |
9.95e-29 |
|
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: 108.28 E-value: 9.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 12 FANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslievngqcVQREGRIV----SDIRSIRSQV 87
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGA----------VLIDGEPLdysrKGLLERRQRV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 88 GFVFQqfNLVDRL---PVLTNVLVGRLHtmpwlrgvMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIAR 164
Cdd:TIGR01166 71 GLVFQ--DPDDQLfaaDVDQDVAFGPLN--------LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518255160 165 TLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMA 215
Cdd:TIGR01166 141 AVAMRPDVLLLDEPTAGLDPAGREQMLAILRRL-RAEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-234 |
1.04e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.60 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFANGK----HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGRi 76
Cdd:PRK13649 1 MGINLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQG---SVRVDDTLITSTSK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 77 VSDIRSIRSQVGFVFQ--QFNLVDRlPVLTNVLVGrlhtmPWLRGVmgwfnAQERSAALA--ALERVGIL-DCHKQRAST 151
Cdd:PRK13649 77 NKDIKQIRKKVGLVFQfpESQLFEE-TVLKDVAFG-----PQNFGV-----SQEEAEALAreKLALVGISeSLFEKNPFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 152 LSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIVSLHQVDMAIRYCPRVIALNQGQVI 231
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
...
gi 518255160 232 YDG 234
Cdd:PRK13649 225 LSG 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-235 |
2.99e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.53 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFANG----KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRi 76
Cdd:PRK13641 1 MSIKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGT---ITIAGYHITPETG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 77 VSDIRSIRSQVGFVFQ--QFNLVDRlPVLTNVLVGRLHtmpwlrgvMGWFNAQERSAALAALERVGI-LDCHKQRASTLS 153
Cdd:PRK13641 77 NKNLKKLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKN--------FGFSEDEAKEKALKWLKKVGLsEDLISKSPFELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVI-Y 232
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIkH 226
|
...
gi 518255160 233 DGP 235
Cdd:PRK13641 227 ASP 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-234 |
1.94e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.15 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLievngqcvqrEGRIVSDIRS 82
Cdd:PRK11607 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML----------DGVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVG-RLHTMPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFGlKQDKLP---------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPD-SSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERV-GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-260 |
2.16e-27 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 106.89 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivsdir 81
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGK---ISILGQPTRQALQ------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 siRSQVGFVFQQFNLVDRLPVLTN--VLVGRLHTMPWLRGVmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:PRK15056 77 --KNLVAYVPQSEEVDWSFPVLVEdvVMMGRYGHMGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALnQGQVIYDGPAAAL 239
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETT 228
|
250 260
....*....|....*....|...
gi 518255160 240 TPA--LLRDLYGMQADEFLSGSE 260
Cdd:PRK15056 229 FTAenLELAFSGVLRHVALNGSE 251
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-217 |
2.78e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 109.04 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 18 ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQ----CVQREGRivsDIRsiRSQVGFVFQQ 93
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGE---VLIDGEditkLSKKELR---ELR--RKKMSMVFQH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 FNLvdrLP---VLTNVLVGrLHtmpwLRGVmgwfNAQERSA-ALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQG 169
Cdd:COG4175 114 FAL---LPhrtVLENVAFG-LE----IQGV----PKAERRErAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518255160 170 AKLVLADEPIASLDPdSSRKVM--EILStIQREDGRTVI-VSlHQVDMAIR 217
Cdd:COG4175 182 PDILLMDEAFSALDP-LIRREMqdELLE-LQAKLKKTIVfIT-HDLDEALR 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-237 |
3.51e-27 |
|
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: 105.24 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLlvADAGPGSLIeVNGQCVQREG--RIVsdirsirsqvgfVFQQFNL 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL--AQPTSGGVI-LEGKQITEPGpdRMV------------VFQNYSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 97 VDRLPVLTNVLVGRLHTMPWLRgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLAD 176
Cdd:TIGR01184 66 LPWLTVRENIALAVDRVLPDLS------KSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518255160 177 EPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNqgqviyDGPAA 237
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLT------NGPAA 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-239 |
6.57e-27 |
|
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: 109.39 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANG---KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLvadagPGSLIEVNGQcVQREGRIV-- 77
Cdd:COG4172 7 LSVEDLSVAFGQGggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-----PDPAAHPSGS-ILFDGQDLlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 ---SDIRSIR-SQVGFVFQQ----FNlvdrlPVLTnvlVG-------RLHTMpwLRGvmgwfnAQERSAALAALERVGIL 142
Cdd:COG4172 81 lseRELRRIRgNRIAMIFQEpmtsLN-----PLHT---IGkqiaevlRLHRG--LSG------AAARARALELLERVGIP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 143 DcHKQRAST----LSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHqvDMAI-- 216
Cdd:COG4172 145 D-PERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH--DLGVvr 221
|
250 260
....*....|....*....|...
gi 518255160 217 RYCPRVIALNQGQVIYDGPAAAL 239
Cdd:COG4172 222 RFADRVAVMRQGEIVEQGPTAEL 244
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-216 |
8.31e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.17 E-value: 8.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGrivsdir 81
Cdd:PRK11248 1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS---ITLDGKPVEGPG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 sirSQVGFVFQQFNLVDRLPVLTNVLVGRlhtmpWLRGVMgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:PRK11248 70 ---AERGVVFQNEGLLPWRNVQDNVAFGL-----QLAGVE---KMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAI 216
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAV 193
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-258 |
1.10e-26 |
|
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: 106.04 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 34 LIGASGSGKSTLLRMVAGLLVADAGPgslievngqcVQREGRIVSDIRSIRSQVGFVFQQFNLVDRLPVLTNVLVG-RLH 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGS----------IMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGlKMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 113 TMPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDpDSSRKVME 192
Cdd:TIGR01187 71 KVP---------RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD-KKLRDQMQ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 193 I-LSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGpaaalTPallRDLYGMQADEFLSG 258
Cdd:TIGR01187 141 LeLKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIG-----TP---EEIYEEPANLFVAR 199
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-235 |
2.30e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.84 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKhALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGL--LVADAGPGSLIEVNGQCVQRegrivSDI 80
Cdd:PRK14247 4 IEIRDLKVSFGQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVSGEVYLDGQDIFK-----MDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQFNLVDRLPVLTNVLVG-RLHtmpwlRGVMGWFNAQERsaALAALERVGILDCHKQR----ASTLSGG 155
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNLSIFENVALGlKLN-----RLVKSKKELQER--VRWALEKAQLWDEVKDRldapAGKLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 156 QQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdgRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGP 235
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-225 |
2.40e-26 |
|
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: 107.76 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivSDIR 81
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS---IAVNGVPLAD-----ADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNLVDRlPVLTNVLVGRlhtmpwlrgvmgwfNAQERSAALAALERVGILDCHK-----------QRAS 150
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAG-TIAENIRLAR--------------PDASDAEIREALERAGLDEFVAalpqgldtpigEGGA 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 151 TLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDMAIRyCPRVIAL 225
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-245 |
2.72e-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: 102.99 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegriVSDIRS 82
Cdd:TIGR03410 1 LEVSNLNVYYG-QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGS---IRLDGEDITK----LPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGrlhtmpwlrgvMGWFNAQERSAALAALERVGIL-DCHKQRASTLSGGQQQRAA 161
Cdd:TIGR03410 73 ARAGIAYVPQGREIFPRLTVEENLLTG-----------LAALPRRSRKIPDEIYELFPVLkEMLGRRGGDLSGGQQQQLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALTP 241
Cdd:TIGR03410 142 IARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDE 221
|
....
gi 518255160 242 ALLR 245
Cdd:TIGR03410 222 DKVR 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-231 |
4.92e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.93 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLlvADAGPGslIEVNGQCVQREGRIVS---D 79
Cdd:PRK14239 6 LQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM--NDLNPE--VTITGSIVYNGHNIYSprtD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQQFNLVDrLPVLTNVLVGrlhtmpwLRgVMGWFNAQERSAAL-AALERVGILDCHKQR----ASTLSG 154
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYG-------LR-LKGIKDKQVLDEAVeKSLKGASIWDEVKDRlhdsALGLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 155 GQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQreDGRTVIVSLHQVDMAIRYCPRVIALNQGQVI 231
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-231 |
7.40e-26 |
|
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: 101.18 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 4 RIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivsdirsi 83
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGS---ILLNGKPIKAKER-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 84 RSQVGFVFQQfnlVDRlpVLTNVLVGRlhtmPWLRGVMGWFNAQERSAALaaLERVGILDCHKQRASTLSGGQQQRAAIA 163
Cdd:cd03226 70 RKSIGYVMQD---VDY--QLFTDSVRE----ELLLGLKELDAGNEQAETV--LKDLDLYALKERHPLSLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 164 RTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVI 231
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-251 |
1.38e-25 |
|
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: 101.41 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 13 ANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQregriVSDIRSIRSQVGFVFQ 92
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGR---VLVDGHDLA-----LADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 93 QFNLVDRlPVLTNVLVGRlhTMPWLRGVmgwfnaqERSAALAALE------RVGILDCHKQRASTLSGGQQQRAAIARTL 166
Cdd:cd03252 84 ENVLFNR-SIRDNIALAD--PGMSMERV-------IEAAKLAGAHdfiselPEGYDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 167 VQGAKLVLADEPIASLDPDSSRKVMEILSTIQreDGRTVIVSLHQVDmAIRYCPRVIALNQGQVIYDGPAAALTPA--LL 244
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEngLY 230
|
....*..
gi 518255160 245 RDLYGMQ 251
Cdd:cd03252 231 AYLYQLQ 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-234 |
1.42e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.47 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 14 NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGrivsDIRSIRSQVGFVFQQ 93
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGK---VYVDGLDTSDEE----NLWDIRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 -FNLVDRLPVLTNVLVGrlhtmPWLRGVmgwfNAQE-RSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAK 171
Cdd:PRK13633 94 pDNQIVATIVEEDVAFG-----PENLGI----PPEEiRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 172 LVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRyCPRVIALNQGQVIYDG 234
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-239 |
1.49e-25 |
|
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: 101.15 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 15 GKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVqregRIVSdIRSIRSQVGFVFQQF 94
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGR---ILIDGHDV----RDYT-LASLRRQIGLVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 95 NLVDRlPVLTNVLVGRLhtmpwlrgvmGWFNAQERSAALAALERVGILDCHK-------QRASTLSGGQQQRAAIARTLV 167
Cdd:cd03251 86 FLFND-TVAENIAYGRP----------GATREEVEEAARAANAHEFIMELPEgydtvigERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 168 QGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDmAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEEL 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-254 |
2.79e-25 |
|
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: 104.80 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 15 GKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivSDIRSIRSQVGFVFQQF 94
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQ---ILLDGHDLAD-----YTLASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 95 NLVDRlPVLTNVLVGRLHTMPwlrgvmgwfNAQERSAALAA--LERV-----GILDCHKQRASTLSGGQQQRAAIARTLV 167
Cdd:TIGR02203 416 VLFND-TIANNIAYGRTEQAD---------RAEIERALAAAyaQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 168 QGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDmAIRYCPRVIALNQGQVIYDGPAAALTPA--LLR 245
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLARngLYA 562
|
....*....
gi 518255160 246 DLYGMQADE 254
Cdd:TIGR02203 563 QLHNMQFRE 571
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-257 |
3.15e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.88 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFanGKHALRD-IDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivsdiR 81
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDnLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQ---IFIDGEDVTH--------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQ-VGFVFQQFNLVDRLPVLTNVLVGrlhtmpwLRgVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:PRK11432 74 SIQQRdICMVFQSYALFPHMSLGENVGYG-------LK-MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAaalt 240
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP---- 221
|
250
....*....|....*..
gi 518255160 241 pallRDLYGMQADEFLS 257
Cdd:PRK11432 222 ----QELYRQPASRFMA 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-239 |
3.67e-25 |
|
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: 100.00 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 9 NKHFA--NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVagLLVADAGPGSlIEVNGQcvqregrivsDIR----- 81
Cdd:cd03253 5 NVTFAydPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL--FRFYDVSSGS-ILIDGQ----------DIRevtld 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQ---FNLVdrlpVLTNVLVGRLhtmpwlrgvmgwfNAQE---RSAALAAL-------------ERVGil 142
Cdd:cd03253 72 SLRRAIGVVPQDtvlFNDT----IGYNIRYGRP-------------DATDeevIEAAKAAQihdkimrfpdgydTIVG-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 143 dchkQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDmAIRYCPRV 222
Cdd:cd03253 133 ----ERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLS-TIVNADKI 205
|
250
....*....|....*..
gi 518255160 223 IALNQGQVIYDGPAAAL 239
Cdd:cd03253 206 IVLKDGRIVERGTHEEL 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-249 |
4.09e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRIvSDIRSIRSQVGFVFQ--- 92
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGT---VTVDDITITHKTKD-KYIRPVRKRIGMVFQfpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 93 -QF--NLVDRlpvltNVLVGrlhtmPWLRGvMGWFNAQERSAALaaLERVGI-LDCHKQRASTLSGGQQQRAAIARTLVQ 168
Cdd:PRK13646 96 sQLfeDTVER-----EIIFG-----PKNFK-MNLDEVKNYAHRL--LMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 169 GAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGpaaalTPallRDLY 248
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT-----SP---KELF 234
|
.
gi 518255160 249 G 249
Cdd:PRK13646 235 K 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-234 |
4.41e-25 |
|
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: 99.61 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 4 RIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqrEGRIVSdIRSI 83
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQ---ILIDGI----DIRDIS-RKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 84 RSQVGFVFQQFNLVDRlPVLTNVLVGRLhtmpwlrgvmgwfNAQERSAALAAlERVGILDCHKQ-----------RASTL 152
Cdd:cd03254 76 RSMIGVVLQDTFLFSG-TIMENIRLGRP-------------NATDEEVIEAA-KEAGAHDFIMKlpngydtvlgeNGGNL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQreDGRTVIVSLHQVDmAIRYCPRVIALNQGQVIY 232
Cdd:cd03254 141 SQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKIIE 217
|
..
gi 518255160 233 DG 234
Cdd:cd03254 218 EG 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-230 |
5.80e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.42 E-value: 5.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MA-LRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLlvADAGPGSLIEVNgqcvQRegriVSD 79
Cdd:PRK11000 1 MAsVTLRNVTKAYGD-VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGDLFIGE----KR----MND 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQQFNLVDRLPVLTNVLVGRLhtmpwLRGVMGWFNAQERSAALAALERVGILDchkQRASTLSGGQQQR 159
Cdd:PRK11000 70 VPPAERGVGMVFQSYALYPHLSVAENMSFGLK-----LAGAKKEEINQRVNQVAEVLQLAHLLD---RKPKALSGGQRQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPdSSRKVMEI-LSTIQREDGRTVIVSLH-QVDmAIRYCPRVIALNQGQV 230
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDA-ALRVQMRIeISRLHKRLGRTMIYVTHdQVE-AMTLADKIVVLDAGRV 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-240 |
6.62e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.15 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAN----GKHA----LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREG 74
Cdd:PRK10419 4 LNVSGLSHHYAHgglsGKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGN---VSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 75 RivSDIRSIRSQVGFVFQQ-FNLVDrlPVLTnvlVGRLHTMPwLRGVMGWFNAQERSAALAALERVGILDCHKQR-ASTL 152
Cdd:PRK10419 81 R--AQRKAFRRDIQMVFQDsISAVN--PRKT---VREIIREP-LRHLLSLDKAERLARASEMLRAVDLDDSVLDKrPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIY 232
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
....*...
gi 518255160 233 DGPAAALT 240
Cdd:PRK10419 233 TQPVGDKL 240
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
8.22e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.53 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVagllvadagpGSLIEVNGQC-VQREGRIVS-- 78
Cdd:PRK14267 4 AIETVNLRVYYGS-NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF----------NRLLELNEEArVEGEVRLFGrn 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 ------DIRSIRSQVGFVFQQFNLVDRLPVLTNVLVG-RLHTMPWLRG----VMGWfnaqersaalaALERVGILDCHKQ 147
Cdd:PRK14267 73 iyspdvDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGvKLNGLVKSKKeldeRVEW-----------ALKKAALWDEVKD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 148 R----ASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdgRTVIVSLHQVDMAIRYCPRVI 223
Cdd:PRK14267 142 RlndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVA 219
|
250
....*....|...
gi 518255160 224 ALNQGQVIYDGPA 236
Cdd:PRK14267 220 FLYLGKLIEVGPT 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-217 |
8.32e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.86 E-value: 8.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFanGKH-ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLlvADAGPGSLIEvnGQCVQREGRIVS--- 78
Cdd:PRK14243 11 LRTENLNVYY--GSFlAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRL--NDLIPGFRVE--GKVTFHGKNLYApdv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 DIRSIRSQVGFVFQQFNLVDRlPVLTNVLVGrlhtmPWLRGVMGWFNAQ-ERSAALAAL-ERVGilDCHKQRASTLSGGQ 156
Cdd:PRK14243 85 DPVEVRRRIGMVFQKPNPFPK-SIYDNIAYG-----ARINGYKGDMDELvERSLRQAALwDEVK--DKLKQSGLSLSGGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518255160 157 QQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdgRTVIVSLHQVDMAIR 217
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-244 |
8.71e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 100.96 E-value: 8.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGK----------HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQR 72
Cdd:COG4608 8 LEVRDLKKHFPVRGglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGE---ILFDGQDITG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 73 EGRivSDIRSIRSQVGFVFQ----QFNlvdrlPVLTnvlVGRLHTMPWLrgVMGWFNAQERSA-ALAALERVGILDCHKQ 147
Cdd:COG4608 85 LSG--RELRPLRRRMQMVFQdpyaSLN-----PRMT---VGDIIAEPLR--IHGLASKAERRErVAELLELVGLRPEHAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 148 R-ASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHqvDMA-IRY-CPRVIA 224
Cdd:COG4608 153 RyPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISH--DLSvVRHiSDRVAV 230
|
250 260
....*....|....*....|....*...
gi 518255160 225 LNQGQVIYDGPAAAL--------TPALL 244
Cdd:COG4608 231 MYLGKIVEIAPRDELyarplhpyTQALL 258
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-243 |
1.21e-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: 103.41 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 14 NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGqcvqregrivSDIRSI-----RSQVG 88
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEG---SVLLDG----------VDIRQIdpadlRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 89 FVFQQfnlvdrlPVL------TNVLVGRLHTmpwlrgvmgwfnaqERSAALAALERVGILDC---HKQ--------RAST 151
Cdd:TIGR03375 543 YVPQD-------PRLfygtlrDNIALGAPYA--------------DDEEILRAAELAGVTEFvrrHPDgldmqigeRGRS 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 152 LSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDMaIRYCPRVIALNQGQVI 231
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSL-LDLVDRIIVMDNGRIV 678
|
250
....*....|..
gi 518255160 232 YDGPAAALTPAL 243
Cdd:TIGR03375 679 ADGPKDQVLEAL 690
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
9-261 |
1.26e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.81 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 9 NKHFANgkHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSL--IEVNGQCVQREgrivsdIRSIRSQ 86
Cdd:PRK13643 14 NSPFAS--RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdIVVSSTSKQKE------IKPVRKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 87 VGFVFQ--QFNLVDRlPVLTNVLVGrlhtmPWLRGVmgwfnAQERSAALAA--LERVGILDCHKQRAS-TLSGGQQQRAA 161
Cdd:PRK13643 86 VGVVFQfpESQLFEE-TVLKDVAFG-----PQNFGI-----PKEKAEKIAAekLEMVGLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGpaaalTP 241
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG-----TP 228
|
250 260
....*....|....*....|
gi 518255160 242 AllrDLYgmQADEFLSGSEL 261
Cdd:PRK13643 229 S---DVF--QEVDFLKAHEL 243
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-280 |
1.40e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.31 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNL----NKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLL--------VADAGPGSLIEVNGQCV 70
Cdd:PRK13631 22 LRVKNLycvfDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkskygtiqVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 71 QREGRIVSDIRSIRSQVGFVFQ--QFNLVdRLPVLTNVLVGrlhtmPWLRGVmgwfnAQERSAALAA--LERVGILDCHK 146
Cdd:PRK13631 102 NPYSKKIKNFKELRRRVSMVFQfpEYQLF-KDTIEKDIMFG-----PVALGV-----KKSEAKKLAKfyLNKMGLDDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 147 QRAS-TLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIAL 225
Cdd:PRK13631 171 ERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVM 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 226 NQGQVIYDGpaaalTPallrdlYgmqadEFLSGSELLQSAQAQIPsPVLAWSNNL 280
Cdd:PRK13631 250 DKGKILKTG-----TP------Y-----EIFTDQHIINSTSIQVP-RVIQVINDL 287
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-246 |
2.04e-24 |
|
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: 98.75 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKhALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREGRIVSDIRS 82
Cdd:TIGR02323 4 LQVSGLSKSYGGGK-GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 I-RSQVGFVFQQFNLVDRLPVLTNVLVG-RLHTMpwlrGVMGWFNAqeRSAALAALERVGI-LDCHKQRASTLSGGQQQR 159
Cdd:TIGR02323 83 LmRTEWGFVHQNPRDGLRMRVSAGANIGeRLMAI----GARHYGNI--RATAQDWLEEVEIdPTRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGpaaaL 239
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG----L 232
|
....*..
gi 518255160 240 TPALLRD 246
Cdd:TIGR02323 233 TDQVLDD 239
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-234 |
2.04e-24 |
|
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: 97.66 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVqregrivsDIRSIRSQVGFVFQQFN 95
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL--------DPADLRRNIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 LVDRlPVLTNVLVGRLHTmpwlrgvmgwfnaqERSAALAALERVGILDC---HKQ--------RASTLSGGQQQRAAIAR 164
Cdd:cd03245 89 LFYG-TLRDNITLGAPLA--------------DDERILRAAELAGVTDFvnkHPNgldlqigeRGRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 165 TLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDMaIRYCPRVIALNQGQVIYDG 234
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-234 |
3.63e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.40 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegriVSDIRS 82
Cdd:PRK09700 6 ISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGT---ITINNINYNK----LDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTmpwlRGVMG-----WFNAQERSAALaaLERVGILDCHKQRASTLSGGQQ 157
Cdd:PRK09700 78 AQLGIGIIYQELSVIDELTVLENLYIGRHLT----KKVCGvniidWREMRVRAAMM--LLRVGLKVDLDEKVANLSISHK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-251 |
4.77e-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: 97.23 E-value: 4.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqregrivsDIRSI-----RSQVGFVFQQ 93
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGE---ILLDGV----------DIRDLnlrwlRSQIGLVSQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 FNLVDRlPVLTNVLVGRlhtmpwlrgvmgwFNAQ----ERSAALAAL------------ERVGildchkQRASTLSGGQQ 157
Cdd:cd03249 86 PVLFDG-TIAENIRYGK-------------PDATdeevEEAAKKANIhdfimslpdgydTLVG------ERGSQLSGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDmAIRYCPRVIALNQGQVIYDGPAA 237
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHD 222
|
250
....*....|....*.
gi 518255160 238 AL--TPALLRDLYGMQ 251
Cdd:cd03249 223 ELmaQKGVYAKLVKAQ 238
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-236 |
5.04e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.53 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MA-LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNgqcvqreGRIVSD 79
Cdd:PRK11650 1 MAgLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE---IWIG-------GRVVNE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 I----RSIrsqvGFVFQQFNLVDRLPVLTNvlvgrlhtMPW---LRGvMGWFNAQERSAALA-ALERVGILDcHKQRAst 151
Cdd:PRK11650 71 LepadRDI----AMVFQNYALYPHMSVREN--------MAYglkIRG-MPKAEIEERVAEAArILELEPLLD-RKPRE-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 152 LSGGQQQRAAIARTLVQGAKLVLADEPIASLDPdSSRKVMEI-LSTIQREDGRTVIVSLH-QVDmAIRYCPRVIALNQGQ 229
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA-KLRVQMRLeIQRLHRRLKTTSLYVTHdQVE-AMTLADRVVVMNGGV 212
|
250
....*....|....*
gi 518255160 230 V--------IYDGPA 236
Cdd:PRK11650 213 AeqigtpveVYEKPA 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-234 |
7.21e-24 |
|
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: 95.07 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLN-KHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREgrivsdir 81
Cdd:cd03247 1 LSINNVSfSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 sIRSQVGFVFQQfnlvdrlpvltnvlvgrlhtmPWLrgvmgwFNAQERsaalaalERVGIldchkqrasTLSGGQQQRAA 161
Cdd:cd03247 73 -LSSLISVLNQR---------------------PYL------FDTTLR-------NNLGR---------RFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdgRTVIVSLHQVdMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-239 |
7.97e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.64 E-value: 7.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregrivsDI 80
Cdd:COG1137 2 MTLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG---RIFLDGE----------DI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSI----RSQVGF--------VFQqfnlvdRLPVLTNVL-VGRLHTMPwlrgvmgwfnAQERSAALAAL-ERVGILDCHK 146
Cdd:COG1137 68 THLpmhkRARLGIgylpqeasIFR------KLTVEDNILaVLELRKLS----------KKEREERLEELlEEFGITHLRK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 147 QRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSsrkVMEILSTIQ--REDGRTVIVSLHQVDMAIRYCPRVIA 224
Cdd:COG1137 132 SKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIA---VADIQKIIRhlKERGIGVLITDHNVRETLGICDRAYI 208
|
250
....*....|....*
gi 518255160 225 LNQGQVIYDGPAAAL 239
Cdd:COG1137 209 ISEGKVLAEGTPEEI 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-246 |
1.15e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.53 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKhALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREGRIVSDIRS 82
Cdd:PRK11701 7 LSVRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 I-RSQVGFVFQqfNLVD--RLPVLTNVLVG-RLhtMpwlrgVMGWFNAQE-RSAALAALERVGI----LDchkQRASTLS 153
Cdd:PRK11701 86 LlRTEWGFVHQ--HPRDglRMQVSAGGNIGeRL--M-----AVGARHYGDiRATAGDWLERVEIdaarID---DLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYD 233
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
250
....*....|...
gi 518255160 234 GpaaaLTPALLRD 246
Cdd:PRK11701 234 G----LTDQVLDD 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-239 |
1.54e-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: 99.76 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGK----------HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGlLVADAGPgslIEVNGQCVQR 72
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGE---IRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 73 EGRivSDIRSIRSQVGFVFQqfnlvD-------RLPVLTNVLVG-RLHTMPWlrgvmgwfNAQERSA-ALAALERVGILD 143
Cdd:COG4172 352 LSR--RALRPLRRRMQVVFQ-----DpfgslspRMTVGQIIAEGlRVHGPGL--------SAAERRArVAEALEEVGLDP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 144 CHKQR-ASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHqvDMA-IRY-CP 220
Cdd:COG4172 417 AARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISH--DLAvVRAlAH 494
|
250
....*....|....*....
gi 518255160 221 RVIALNQGQVIYDGPAAAL 239
Cdd:COG4172 495 RVMVMKDGKVVEQGPTEQV 513
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-249 |
1.71e-23 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 96.43 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSL-----IEVNGQCVQR-EGRIVSDIRSI---RSQVGF 89
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGArvtgdVTLNGEPLAAiDAPRLARLRAVlpqAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 90 VFQqfnlVDRLpvltnVLVGRLhtmPWLRGVmGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQ- 168
Cdd:PRK13547 97 AFS----AREI-----VLLGRY---PHARRA-GALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 169 --------GAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG-PAAAL 239
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGaPADVL 243
|
250
....*....|
gi 518255160 240 TPALLRDLYG 249
Cdd:PRK13547 244 TPAHIARCYG 253
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
2.57e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRIVsdi 80
Cdd:PRK13536 40 VAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGK---ITVLGVPVPARARLA--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 rsiRSQVGFVFQQFNLVDRLPVLTNVLV-GRLHTMpwlrgvmgwfNAQERSAALAALERVGILDCHKQ-RASTLSGGQQQ 158
Cdd:PRK13536 113 ---RARIGVVPQFDNLDLEFTVRENLLVfGRYFGM----------STREIEAVIPSLLEFARLESKADaRVSDLSGGMKR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAA 238
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
.
gi 518255160 239 L 239
Cdd:PRK13536 259 L 259
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-234 |
5.00e-23 |
|
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: 94.26 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREgrivsdirSIRSQVGFVFQQFNLVD 98
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPD--------QFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 RLPVLTNvlvgrLHTMPWLRgvMGWFNAQERSAALAalERVGILDCHKQRA-----STLSGGQQQRAAIARTLVQGAKLV 173
Cdd:cd03234 95 GLTVRET-----LTYTAILR--LPRKSSDAIRKKRV--EDVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 174 LADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAI-RYCPRVIALNQGQVIYDG 234
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPRSDLfRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-278 |
1.24e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.28 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqrEGRIVSDIRS 82
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGK---VLVSGI----DTGDFSKLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQ--QFNLVDRlPVLTNVLVG--RLHTMPwlrgvmgwfnAQERSAALAALERVGILDCHKQRASTLSGGQQQ 158
Cdd:PRK13644 75 IRKLVGIVFQnpETQFVGR-TVEEDLAFGpeNLCLPP----------IEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDmAIRYCPRVIALNQGQVIYDG-PAA 237
Cdd:PRK13644 144 CVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGePEN 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 518255160 238 ALTPALLRDLyGMQADEFLSGSELLQSAQAQIPspvlaWSN 278
Cdd:PRK13644 222 VLSDVSLQTL-GLTPPSLIELAENLKMHGVVIP-----WEN 256
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-211 |
1.37e-22 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 97.05 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivSDIRS 82
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE---VTLDGVPVSS-----LDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRlPVLTNVLVGRLhtmpwlrgvmgwfNAQErSAALAALERVGILDCHK-----------QRAST 151
Cdd:TIGR02868 407 VRRRVSVCAQDAHLFDT-TVRENLRLARP-------------DATD-EELWAALERVGLADWLRalpdgldtvlgEGGAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 152 LSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILstIQREDGRTVIVSLHQ 211
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-234 |
1.41e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 94.30 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 18 ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRIVSDIRSIRSQVGFVFQ--QFN 95
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ---TIVGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 LVDRlPVLTNVLVGRLHtmpwlrgvMGWfNAQERSAALAALERVGIL--DCHKQRASTLSGGQQQRAAIARTLVQGAKLV 173
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVN--------LGE-NKQEAYKKVPELLKLVQLpeDYVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518255160 174 LADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-248 |
1.75e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.03 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAgpgslievngqcvqreGRIVSDIRS 82
Cdd:PRK10895 4 LTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA----------------GNIIIDDED 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 I---------RSQVGFVFQQFNLVDRLPVLTNvLVGRLHtmpwLRGVMGWFNAQERSAALaaLERVGILDCHKQRASTLS 153
Cdd:PRK10895 67 IsllplharaRRGIGYLPQEASIFRRLSVYDN-LMAVLQ----IRDDLSAEQREDRANEL--MEEFHIEHLRDSMGQSLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSsrkVMEILSTIQ--REDGRTVIVSLHQVDMAIRYCPRVIALNQGQVI 231
Cdd:PRK10895 140 GGERRRVEIARALAANPKFILLDEPFAGVDPIS---VIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
250
....*....|....*...
gi 518255160 232 YDG-PAAALTPALLRDLY 248
Cdd:PRK10895 217 AHGtPTEILQDEHVKRVY 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
16-263 |
2.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 93.26 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsDIRSIRSQVGFVFQQFN 95
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQ---IIIDGDLLTEE-----NVWDIRHKIGMVFQNPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 lvdrlpvltNVLVGRLHTMPWLRGV--MGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLV 173
Cdd:PRK13650 92 ---------NQFVGATVEDDVAFGLenKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 174 LADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDmAIRYCPRVIALNQGQViydgpAAALTPallRDLygmqad 253
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNGQV-----ESTSTP---REL------ 227
|
250
....*....|
gi 518255160 254 eFLSGSELLQ 263
Cdd:PRK13650 228 -FSRGNDLLQ 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-185 |
1.44e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHfANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADagpgslIEVNGQcVQREGRIVSDIRS 82
Cdd:COG4136 2 LSLENLTIT-LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPA------FSASGE-VLLNGRRLTALPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGrlhtMPwlRGVMGwfnAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:COG4136 74 EQRRIGILFQDDLLFPHLSVGENLAFA----LP--PTIGR---AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVAL 144
|
170 180
....*....|....*....|...
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPD 185
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAA 167
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-249 |
1.81e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 94.31 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 5 IQNLNKHF-ANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQregrivSDIRSI 83
Cdd:TIGR01257 931 VKNLVKIFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT---VLVGGKDIE------TNLDAV 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 84 RSQVGFVFQQFNLVDRLPVLTNVLVgrlhtMPWLRGvMGWFNAQERSAALaaLERVGILDCHKQRASTLSGGQQQRAAIA 163
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHILF-----YAQLKG-RSWEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVA 1073
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 164 RTLVQGAKLVLADEPIASLDPDSSRKVMEILstIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGpaaalTPAL 243
Cdd:TIGR01257 1074 IAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG-----TPLF 1146
|
....*.
gi 518255160 244 LRDLYG 249
Cdd:TIGR01257 1147 LKNCFG 1152
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
2.43e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.93 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslIEVNGQcVQREGRIVSDIR 81
Cdd:PRK14271 21 AMAAVNLTLGFA-GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG----YRYSGD-VLLGGRSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SI---RSQVGFVFQQFNLVDrLPVLTNVLVG-RLHTM-PwlrgvmgwfNAQERSAALAALERVGILDCHKQRAST----L 152
Cdd:PRK14271 95 DVlefRRRVGMLFQRPNPFP-MSIMDNVLAGvRAHKLvP---------RKEFRGVAQARLTEVGLWDAVKDRLSDspfrL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQreDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIY 232
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
....*..
gi 518255160 233 DGPAAAL 239
Cdd:PRK14271 243 EGPTEQL 249
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-239 |
3.02e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLvadagP--GSLiEVNGQcvqrEGRiVSDI 80
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-----PyqGSL-KINGI----ELR-ELDP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQQfnlvDRLP---VLTNVLvgrlhtmpwlrgvMGWFNAQErSAALAALERVGILDCHKQ---------- 147
Cdd:PRK11174 419 ESWRKHLSWVGQN----PQLPhgtLRDNVL-------------LGNPDASD-EQLQQALENAWVSEFLPLlpqgldtpig 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 148 -RASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDmAIRYCPRVIALN 226
Cdd:PRK11174 481 dQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLE-DLAQWDQIWVMQ 557
|
250
....*....|...
gi 518255160 227 QGQVIYDGPAAAL 239
Cdd:PRK11174 558 DGQIVQQGDYAEL 570
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-245 |
3.20e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKST----LLRmvaglLVADAGPgslIEVNGQCVQREGRivSDIRSIRSQVGFVF 91
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLR-----LINSQGE---IWFDGQPLHNLNR--RQLLPVRHRIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 92 QQFN--LVDRLPVLTNVLVG-RLHtMPWLrgvmgwfNAQERSAA-LAALERVGILDCHKQR-ASTLSGGQQQRAAIARTL 166
Cdd:PRK15134 369 QDPNssLNPRLNVLQIIEEGlRVH-QPTL-------SAAQREQQvIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 167 VQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG--------PAAA 238
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGdcervfaaPQQE 520
|
....*..
gi 518255160 239 LTPALLR 245
Cdd:PRK15134 521 YTRQLLA 527
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-229 |
3.96e-21 |
|
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: 88.68 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 18 ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQ---CVQrEGRIVSDirSIRSqvgfvfqqf 94
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG---SVSVPGSiayVSQ-EPWIQNG--TIRE--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 95 nlvdrlpvltNVLVGRLHTMPWLRGVMgwfnaqeRSAAL----AALE-----RVGildchkQRASTLSGGQQQRAAIART 165
Cdd:cd03250 85 ----------NILFGKPFDEERYEKVI-------KACALepdlEILPdgdltEIG------EKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 166 LVQGAKLVLADEPIASLDPDSSRKVME--ILSTIQreDGRTVIVSLHQVDmAIRYCPRVIALNQGQ 229
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLL--NNKTRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-246 |
4.86e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.66 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGP----GSLIE-VNGQCVQREGrIV 77
Cdd:PRK11300 6 LSVSGLMMRFG-GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTillrGQHIEgLPGHQIARMG-VV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 SDIRSIRsqvgfVFQQFNLVDRLPVL------TNVLVGRLHTMPWLRGVMgwfNAQERSAALaaLERVGILDCHKQRAST 151
Cdd:PRK11300 84 RTFQHVR-----LFREMTVIENLLVAqhqqlkTGLFSGLLKTPAFRRAES---EALDRAATW--LERVGLLEHANRQAGN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 152 LSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVI 231
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
250
....*....|....*
gi 518255160 232 YDGpaaalTPALLRD 246
Cdd:PRK11300 234 ANG-----TPEEIRN 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-242 |
7.96e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.62 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 14 NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQcvqregriVSDIRSIRSQVGFVFQQ 93
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAG---TIKLDGG--------DIDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 FNLVDRLPVLTNVLVgrlhtmpWLRgvmgwFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLV 173
Cdd:PRK13539 82 NAMKPALTVAENLEF-------WAA-----FLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 174 LADEPIASLDPDSSRKVMEILSTiQREDGRTVIVSLHQvDMAIrYCPRVIALnqgqviydGPAAALTPA 242
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATHI-PLGL-PGARELDL--------GPFAAEDPA 207
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-210 |
1.34e-20 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 87.45 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivSDIRS 82
Cdd:TIGR03740 1 LETKNLSKRFGK-QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGE---IIFDGHPWTR-----KDLHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IrsqvGFVFQQFNLVDRLPVLTNVLVgrlHTMpwLRGVmgwfnaqERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:TIGR03740 72 I----GSLIESPPLYENLTARENLKV---HTT--LLGL-------PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGI 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIVSLH 210
Cdd:TIGR03740 136 AIALLNHPKLLILDEPTNGLDPIGIQELRELIRSFP-EQGITVILSSH 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-213 |
1.68e-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: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVadagpgslievngqCVQREGRIVSDIRSIRSQVgfvfqqfN 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK--------------GTPVAGCVDVPDNQFGREA-------S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 LVDRLPVLTNVLvgrlhtmpwlrgvmgwfnaqersAALAALERVGILDC--HKQRASTLSGGQQQRAAIARTLVQGAKLV 173
Cdd:COG2401 102 LIDAIGRKGDFK-----------------------DAVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518255160 174 LADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVD 213
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-249 |
3.68e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 4 RIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslievngqCVQREGRIVSDIrsi 83
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG----------RVEVNGRVSALL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 84 rsQVGFVFQqfnlvdrlPVLT---NV-LVGRLhtmpwlrgvMGWFNAQERS-----AALAALERVgiLDchkQRASTLSG 154
Cdd:COG1134 94 --ELGAGFH--------PELTgreNIyLNGRL---------LGLSRKEIDEkfdeiVEFAELGDF--ID---QPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 155 GQQQR-A-AIArTLVQgAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVI-VSlHQVDMAIRYCPRVIALNQGQVI 231
Cdd:COG1134 150 GMRARlAfAVA-TAVD-PDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIfVS-HSMGAVRRLCDRAIWLEKGRLV 225
|
250
....*....|....*...
gi 518255160 232 YDGPAAALTPALLRDLYG 249
Cdd:COG1134 226 MDGDPEEVIAAYEALLAG 243
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-251 |
3.89e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.82 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLvadAGPGSlIEVNGQCVQRegrivSDIRSIRSQVGFVFQQFNLVD 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL---PGQGE-ILLNGRPLSD-----WSAAELARHRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 RLPV---LTnvlvgrLHTMPWLrgvmgwfNAQERSAALAAL-ERVGILDCHKQRASTLSGGQQQRAAIARTLVQ------ 168
Cdd:COG4138 83 AMPVfqyLA------LHQPAGA-------SSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptin 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 169 -GAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAA-LTPALLRD 246
Cdd:COG4138 150 pEGQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEvMTPENLSE 228
|
....*
gi 518255160 247 LYGMQ 251
Cdd:COG4138 229 VFGVK 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-234 |
4.09e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.11 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 18 ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsDIRSIRSQVGFVFQ----Q 93
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE---IFYNNQAITDD-----NFEKLRKHIGIVFQnpdnQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 FnlVDRLpVLTNVLVG-RLHTMPWLrgvmgwfNAQERSAAlaALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKL 172
Cdd:PRK13648 96 F--VGSI-VKYDVAFGlENHAVPYD-------EMHRRVSE--ALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 173 VLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRyCPRVIALNQGQVIYDG 234
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-254 |
5.34e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNkhfanGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVqregRIVSDIR 81
Cdd:COG1129 256 VLEVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE---IRLDGKPV----RIRSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFV---FQQFNLVDRLPVLTNVlvgrlhTMPWLRGV--MGWFN-AQERSAALAALERVGI----LDchkQRAST 151
Cdd:COG1129 324 AIRAGIAYVpedRKGEGLVLDLSIRENI------TLASLDRLsrGGLLDrRRERALAEEYIKRLRIktpsPE---QPVGN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 152 LSGGQQQRAAIARTLVQGAKLVLADEPiasldpdsSRKV-----MEILSTIQR--EDGRTVIV--SlhqvDM--AIRYCP 220
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEP--------TRGIdvgakAEIYRLIRElaAEGKAVIVisS----ELpeLLGLSD 462
|
250 260 270
....*....|....*....|....*....|....*
gi 518255160 221 RVIALNQGQVIYDGPAAALTP-ALLRDLYGMQADE 254
Cdd:COG1129 463 RILVMREGRIVGELDREEATEeAIMAAATGGAAAA 497
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-235 |
5.44e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.34 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVqregrivsDIRSIRSQVGFVfQQFN 95
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPI--------DAKEMRAISAYV-QQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 LVdrLPVLTnvlvGRLHTMPWLRGVMG--WFNAQERSAALAALERVGILDCHKQRAST------LSGGQQQRAAIARTLV 167
Cdd:TIGR00955 109 LF--IPTLT----VREHLMFQAHLRMPrrVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518255160 168 QGAKLVLADEPIASLDPDSSRKVMEILSTI-QRedGRTVIVSLHQVDMAIrYC--PRVIALNQGQVIYDGP 235
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQK--GKTIICTIHQPSSEL-FElfDKIILMAEGRVAYLGS 250
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-248 |
6.45e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.09 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFanGK-HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivSDIR 81
Cdd:PRK11614 6 LSFDKVSAHY--GKiQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGR---IVFDGKDITDW----QTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNLVDRLPVLTNVlvgrlhtmpwlrgVMGWFNAqERSAALAALERV-----GILDCHKQRASTLSGGQ 156
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEENL-------------AMGGFFA-ERDQFQERIKWVyelfpRLHERRIQRAGTMSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 157 QQRAAIARTLVQGAKLVLADEPIASLDPDSsrkVMEILSTIQ--REDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIY-D 233
Cdd:PRK11614 143 QQMLAIGRALMSQPRLLLLDEPSLGLAPII---IQQIFDTIEqlREQGMTIFLVEQNANQALKLADRGYVLENGHVVLeD 219
|
250
....*....|....*
gi 518255160 234 GPAAALTPALLRDLY 248
Cdd:PRK11614 220 TGDALLANEAVRSAY 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-234 |
6.61e-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: 89.09 E-value: 6.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQC-----VQREGRI- 76
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCekcgyVERPSKVg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 77 -------------VSDI--------RSIRSQVGFVFQQ-FNLVDRLPVLTNVLvgrlHTMPWLrgvmGWFNAQERSAALA 134
Cdd:TIGR03269 80 epcpvcggtlepeEVDFwnlsdklrRRIRKRIAIMLQRtFALYGDDTVLDNVL----EALEEI----GYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 135 ALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDM 214
Cdd:TIGR03269 152 LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|
gi 518255160 215 AIRYCPRVIALNQGQVIYDG 234
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEG 251
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-234 |
8.38e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.17 E-value: 8.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 18 ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegriVSD--IRSIR-SQVGFVFQQF 94
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ---VLIDGVDIAK----ISDaeLREVRrKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 95 NLVDRLPVLTNVLVGRlhtmpWLRGVMGwfnAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVL 174
Cdd:PRK10070 116 ALMPHMTVLDNTAFGM-----ELAGINA---EERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 175 ADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-211 |
1.40e-19 |
|
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: 84.33 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 14 NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslievngqcvqregRIVSDIRSIRSQVGFVFQQ 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSG----------------EVRWNGTPLAEQRDEPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 FNLVDRLPVLTNVLVGRLHTMPWLRgvmgwFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLV 173
Cdd:TIGR01189 75 ILYLGHLPGLKPELSALENLHFWAA-----IHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 518255160 174 LADEPIASLDPDSSRKVMEIL-STIQRedGRTVIVSLHQ 211
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLrAHLAR--GGIVLLTTHQ 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-231 |
1.41e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.04 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqrEGRIVSDIRS 82
Cdd:PRK11288 5 LSFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS---ILIDGQ----EMRFASTTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMpwlrgvMGWFNAQE-RSAALAALERVGI-LDCHkQRASTLSGGQQQRA 160
Cdd:PRK11288 77 LAAGVAIIYQELHLVPEMTVAENLYLGQLPHK------GGIVNRRLlNYEAREQLEHLGVdIDPD-TPLKYLSIGQRQMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 161 AIARTLVQGAKLVLADEPIASLdpdSSRKVMEILSTIQ--REDGRTVIVSLHQVDMAIRYCPRVIALNQGQVI 231
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSL---SAREIEQLFRVIRelRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-234 |
1.66e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 5 IQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsliEVngqcvqregRIVSDIRsir 84
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-----EV---------SIPKGLR--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 85 sqVGFVFQQFNLVDRLPVLTNVLVGRLHTMPWLR--------------GVMGWFNAQERSAAL----------AALERVG 140
Cdd:COG0488 63 --IGYLPQEPPLDDDLTVLDTVLDGDAELRALEAeleeleaklaepdeDLERLAELQEEFEALggweaearaeEILSGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 141 ILDC-HKQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSsrkvmeIL---STIQREDGRTVIVSlHqvDmai 216
Cdd:COG0488 141 FPEEdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES------IEwleEFLKNYPGTVLVVS-H--D--- 208
|
250 260
....*....|....*....|....
gi 518255160 217 RY-----CPRVIALNQGQVI-YDG 234
Cdd:COG0488 209 RYfldrvATRILELDRGKLTlYPG 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-244 |
1.99e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.77 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREGriVSDIR 81
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASG---SIRLDGEDITGLS--PRERR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 siRSQVGFV---FQQFNLVDRLPVLTNVLVGRLHTMPWLRGvmGWFNAQE-RSAALAALERVGI----LDchkQRASTLS 153
Cdd:COG3845 332 --RLGVAYIpedRLGRGLVPDMSVAENLILGRYRRPPFSRG--GFLDRKAiRAFAEELIEEFDVrtpgPD---TPARSLS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILsTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYD 233
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL-LELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
250
....*....|.
gi 518255160 234 GPAAALTPALL 244
Cdd:COG3845 484 VPAAEATREEI 494
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-245 |
2.03e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsDIRS 82
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGS---VLIRGEPITKE-----NIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQqfNLVDRL---PVLTNVLVGRLHtmpwlrgvMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQR 159
Cdd:PRK13652 76 VRKFVGLVFQ--NPDDQIfspTVEQDIAFGPIN--------LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAA- 238
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEi 225
|
....*...
gi 518255160 239 -LTPALLR 245
Cdd:PRK13652 226 fLQPDLLA 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-239 |
2.12e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.01 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRIVsdir 81
Cdd:PRK13537 7 PIDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGS---ISLCGEPVPSRARHA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 siRSQVGFVFQQFNLVDRLPVLTNVLV-GRLHTMPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRA 160
Cdd:PRK13537 79 --RQRVGVVPQFDNLDPDFTVRENLLVfGRYFGLS---------AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEIL-STIQRedGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLrSLLAR--GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-231 |
2.18e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 12 FANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLL-VADagpgSLIEVNGQcVQREGRIVSDIRSI--RSQVG 88
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeIYD----SKIKVDGK-VLYFGKDIFQIDAIklRKEVG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 89 FVFQQFNLVDRLPVLTNVLVG-RLHTMPWLRGVmgwfnaqeRSAALAALERVG----ILDCHKQRASTLSGGQQQRAAIA 163
Cdd:PRK14246 94 MVFQQPNPFPHLSIYDNIAYPlKSHGIKEKREI--------KKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 164 RTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdgRTVIVSLHQVDMAIRYCPRVIALNQGQVI 231
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-230 |
2.76e-19 |
|
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: 82.87 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNkhfanGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGqcvqREGRIVSDIR 81
Cdd:cd03215 4 VLEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGE---ITLDG----KPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFV---FQQFNLVDRLPVLTNVLVGRLhtmpwlrgvmgwfnaqersaalaalervgildchkqrastLSGGQQQ 158
Cdd:cd03215 72 AIRAGIAYVpedRKREGLVLDLSVAENIALSSL----------------------------------------LSGGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-234 |
3.00e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.32 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLrmvaGLL--VADAGPGSlIEVNGQcvqregrivsD 79
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLqrVFDPQSGR-ILIDGT----------D 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IR-----SIRSQVGFVFQQFNLVDRlPVLTNVLVGRLH-TMPWLRGvmgwfnAQERSAALAALER--------VGildch 145
Cdd:PRK13657 399 IRtvtraSLRRNIAVVFQDAGLFNR-SIEDNIRVGRPDaTDEEMRA------AAERAQAHDFIERkpdgydtvVG----- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 146 kQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVDmAIRYCPRVIAL 225
Cdd:PRK13657 467 -ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLS-TVRNADRILVF 542
|
....*....
gi 518255160 226 NQGQVIYDG 234
Cdd:PRK13657 543 DNGRVVESG 551
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-230 |
3.52e-19 |
|
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: 82.65 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHA-LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivsdiR 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGR---VRLDGADISQWDP-----N 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNLVDrlpvltnvlvGRLhtmpwlrgvmgwfnaqersaalaalervgildchkqRASTLSGGQQQRAA 161
Cdd:cd03246 73 ELGDHVGYLPQDDELFS----------GSI------------------------------------AENILSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDmAIRYCPRVIALNQGQV 230
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-240 |
5.36e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.21 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRIVSDIRS 82
Cdd:PRK10762 5 LQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGS---ILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IrsqvGFVFQQFNLVDRLPVLTNVLVGRLHTMPWlrGVMGWFNAQERSAALaaLERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:PRK10762 81 I----GIIHQELNLIPQLTIAENIFLGREFVNRF--GRIDWKKMYAEADKL--LARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 163 ARTLVQGAKLVLADEPIASL---DPDSSRKVMEILstiqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALtdtETESLFRVIREL----KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
.
gi 518255160 240 T 240
Cdd:PRK10762 229 T 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-237 |
9.87e-19 |
|
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: 85.62 E-value: 9.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKH----ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgSLIEVNGQCVQREGRIVS 78
Cdd:TIGR03269 280 IKVRNVSKRYISVDRgvvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE-VNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 DIRSIRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMPWLRGVMgwfnaqersAALAALERVG--------ILDchkQRAS 150
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARM---------KAVITLKMVGfdeekaeeILD---KYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 151 TLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
....*..
gi 518255160 231 IYDGPAA 237
Cdd:TIGR03269 507 VKIGDPE 513
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-212 |
1.18e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.16 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKhALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGL--LVADAGPGSLIEVNGQCVQrEGRIvsD 79
Cdd:PRK14258 7 AIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMneLESEVRVEGRVEFFNQNIY-ERRV--N 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQQFNLVDrLPVLTNVLVGRlhtmpwlrGVMGWFNAQERSAAL-AALERVGILDCHKQR----ASTLSG 154
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFP-MSVYDNVAYGV--------KIVGWRPKLEIDDIVeSALKDADLWDEIKHKihksALDLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518255160 155 GQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQ-REDGRTVIVS--LHQV 212
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVShnLHQV 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-239 |
1.21e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 17 HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqregRI----VSDIRSIRSQVGFVFQ 92
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGE---IIFNGQ------RIdtlsPGKLQALRRDIQFIFQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 93 Q--FNLVDRLPVLTNVLVG-RLHtmpwlrGVMGWFNAQERSAALaaLERVGILDCHKQR-ASTLSGGQQQRAAIARTLVQ 168
Cdd:PRK10261 409 DpyASLDPRQTVGDSIMEPlRVH------GLLPGKAAAARVAWL--LERVGLLPEHAWRyPHEFSGGQRQRICIARALAL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 169 GAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHqvDMAI--RYCPRVIALNQGQVIYDGPAAAL 239
Cdd:PRK10261 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISH--DMAVveRISHRVAVMYLGQIVEIGPRRAV 551
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-235 |
3.26e-18 |
|
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: 81.00 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLN-KHFANGKHALRDIDLNIADGEMVALIGASGSGKST----LLRMVagllvaDAGPGSlIEVNGQcvqregriv 77
Cdd:cd03244 3 IEFKNVSlRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV------ELSSGS-ILIDGV--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 sDIRSI-----RSQVGFVFQQfnlvdrlPVL---TnvlvgrlhtmpwLRGVMGWFNAQERSAALAALERVGILDCHKQRA 149
Cdd:cd03244 67 -DISKIglhdlRSRISIIPQD-------PVLfsgT------------IRSNLDPFGEYSDEELWQALERVGLKEFVESLP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 150 -----------STLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEilsTIQRE-DGRTVIVSLHQVDmAIR 217
Cdd:cd03244 127 ggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQK---TIREAfKDCTVLTIAHRLD-TII 202
|
250
....*....|....*....
gi 518255160 218 YCPRVIALNQGQVI-YDGP 235
Cdd:cd03244 203 DSDRILVLDKGRVVeFDSP 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-227 |
3.27e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.62 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 20 RDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsliEV--NGQCVQREGRivsdirSIRSQVGFVFQQFNLV 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAG-----EVlwQGEPIRRQRD------EYHQDLLYLGHQPGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 98 DRLPVLTNvlvgrlhtmpwLRGVMGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADE 177
Cdd:PRK13538 87 TELTALEN-----------LRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518255160 178 PIASLDPDSsrkVMEILSTIQR--EDGRTVIVSLHQvDMAIRYCP-RVIALNQ 227
Cdd:PRK13538 156 PFTAIDKQG---VARLEALLAQhaEQGGMVILTTHQ-DLPVASDKvRKLRLGQ 204
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-273 |
4.20e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.83 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHF--ANGKH----------ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCV 70
Cdd:PRK15079 9 LEVADLKVHFdiKDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGE---VAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 71 QREGRivSDIRSIRSQVGFVFQqfnlvDRL----PVLTnvlVGRLHTMPwLRGVMGWFNAQE-RSAALAALERVGILDCH 145
Cdd:PRK15079 86 LGMKD--DEWRAVRSDIQMIFQ-----DPLaslnPRMT---IGEIIAEP-LRTYHPKLSRQEvKDRVKAMMLKVGLLPNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 146 KQR-ASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHqvDMAI-------- 216
Cdd:PRK15079 155 INRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAH--DLAVvkhisdrv 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 217 --RYCPRVIALNQGQVIYDGPAAALTPALlrdlygMQA----DEFLSGSELLQSAQAQIPSPV 273
Cdd:PRK15079 233 lvMYLGHAVELGTYDEVYHNPLHPYTKAL------MSAvpipDPDLERNKTIQLLEGELPSPI 289
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-234 |
4.64e-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: 80.65 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslievngqcVQREGRIVSdirSIRSQVGFvfqqfn 95
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT----------VTVRGRVSS---LLGLGGGF------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 lvdrLPVLT---NV-LVGRLhtmpwlrgvMGWFNAQERS-----AALAALErvgilDCHKQRASTLSGGQQQRAAIARTL 166
Cdd:cd03220 96 ----NPELTgreNIyLNGRL---------LGLSRKEIDEkideiIEFSELG-----DFIDLPVKTYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 167 VQGAKLVLADEPIASLDPDSSRKVMEILSTiQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-240 |
5.01e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 5.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSlIEVNGQCVQregriVSDIR- 81
Cdd:PRK13549 6 LEMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGE-IIFEGEELQ-----ASNIRd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNLVDRLPVLTNVLVGRlhtmPWLR-GVMGWFNAQERSAALaaLERVGILDCHKQRASTLSGGQQQRA 160
Cdd:PRK13549 79 TERAGIAIIHQELALVKELSVLENIFLGN----EITPgGIMDYDAMYLRAQKL--LAQLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSlHQVDMAIRYCPRVIALNQGQVIYDGPAAALT 240
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYIS-HKLNEVKAISDTICVIRDGRHIGTRPAAGMT 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
15-235 |
5.92e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 15 GKHALrDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGqcvqregRIVSDIRS-I-----RSQVG 88
Cdd:PRK11144 11 GDLCL-TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKG---RIVLNG-------RVLFDAEKgIclppeKRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 89 FVFQQFNLVDRLPVLTNVLVGRLHTMPwlrgvmGWFNAqersaaLAALerVGILDCHKQRASTLSGGQQQRAAIARTLVQ 168
Cdd:PRK11144 80 YVFQDARLFPHYKVRGNLRYGMAKSMV------AQFDK------IVAL--LGIEPLLDRYPGSLSGGEKQRVAIGRALLT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 169 GAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGP 235
Cdd:PRK11144 146 APELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-242 |
6.15e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.32 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLvaDAGpgslievngqcvqrEGRIvsdir 81
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW--PYG--------------SGRI----- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 sirsqvgfvfqqfnlvdRLPVLTNVLVgrlhtMPW--------LRGVMGWFNAQER---SAALAALERVGI------LDC 144
Cdd:COG4178 421 -----------------ARPAGARVLF-----LPQrpylplgtLREALLYPATAEAfsdAELREALEAVGLghlaerLDE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 145 HKQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILstiQREDGRTVIVSL-HQVDMAiRYCPRVI 223
Cdd:COG4178 479 EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL---REELPGTTVISVgHRSTLA-AFHDRVL 554
|
250
....*....|....*....
gi 518255160 224 ALNqgqviyDGPAAALTPA 242
Cdd:COG4178 555 ELT------GDGSWQLLPA 567
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-270 |
1.03e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 81.33 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MAL-RIQNLNKHFANGKHALRDID---LNIADGEMVALIGASGSGKSTLLRMVAGLLvadAGPGSL----IEVNGQCVQR 72
Cdd:PRK11022 1 MALlNVDKLSVHFGDESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLI---DYPGRVmaekLEFNGQDLQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 73 ----EGRivsdiRSIRSQVGFVFQqfnlvDRLPVLTNVLVGRLHTMPWLRGVMGWFNAQERSAALAALERVGI------L 142
Cdd:PRK11022 78 isekERR-----NLVGAEVAMIFQ-----DPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpasrL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 143 DCHKQRastLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRV 222
Cdd:PRK11022 148 DVYPHQ---LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 223 IALNQGQVIYDGPAAAL--------TPALLRDLygmqaDEFLSGSELLQSAQAQIP 270
Cdd:PRK11022 225 IVMYAGQVVETGKAHDIfraprhpyTQALLRAL-----PEFAQDKARLASLPGVVP 275
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-240 |
4.75e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.64 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKhALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIeVNGQCVQREGriVSDIRs 82
Cdd:TIGR02633 2 LEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIY-WSGSPLKASN--IRDTE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 iRSQVGFVFQQFNLVDRLPVLTNVLVGRLHTMPwlRGVMGWFNAQERSAALAALERVGILDCHKQrASTLSGGQQQRAAI 162
Cdd:TIGR02633 77 -RAGIVIIHQELTLVPELSVAENIFLGNEITLP--GGRMAYNAMYLRAKNLLRELQLDADNVTRP-VGDYGGGQQQLVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSlHQVDMAIRYCPRVIALNQGQVIYDGPAAALT 240
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAVCDTICVIRDGQHVATKDMSTMS 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-258 |
8.48e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 78.27 E-value: 8.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 21 DIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivSDIRSIRSQVGFVFQQFNLVDRL 100
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGE---ILFDGENIPAMSR--SRLYTVRKRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 101 PVLTNVLVG-RLHT-MPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADEP 178
Cdd:PRK11831 100 NVFDNVAYPlREHTqLP---------APLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 179 IASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGpaaalTPALLRDLYGMQADEFLSG 258
Cdd:PRK11831 171 FVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG-----SAQALQANPDPRVRQFLDG 245
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-225 |
9.72e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.06 E-value: 9.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 13 ANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslievngqcVQREGRIVSDI--RSIRSQVGFV 90
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGT----------LLFEGEDISTLkpEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 91 FQQfnlvdrlPVLTNVLVGRLHTMPW-LRGvmgwfNAQERSAALAALERVGI-LDCHKQRASTLSGGQQQRAAIARTLVQ 168
Cdd:PRK10247 87 AQT-------PTLFGDTVYDNLIFPWqIRN-----QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 169 GAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDmAIRYCPRVIAL 225
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKVITL 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-234 |
1.15e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsliEVngqcvqREGRIVsdirs 82
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG-----TV------KLGETV----- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 irsQVGFVFQ-QFNLVDRLPVLTNVL-----VGRLHtmpwLRGVMGWFN-AQERsaalaalervgildcHKQRASTLSGG 155
Cdd:COG0488 379 ---KIGYFDQhQEELDPDKTVLDELRdgapgGTEQE----VRGYLGRFLfSGDD---------------AFKPVGVLSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 156 QQQRAAIARTLVQGAKLVLADEPIASLDPDsSRKVMEILstIQREDGrTVIVSLHqvDmaiRY-----CPRVIALNQGQV 230
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDIE-TLEALEEA--LDDFPG-TVLLVSH--D---RYfldrvATRILEFEDGGV 507
|
....*
gi 518255160 231 I-YDG 234
Cdd:COG0488 508 ReYPG 512
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-239 |
5.01e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.28 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQREgrivsDIRSIRSQVGFVFQQFNlvd 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG---KVKIDGELLTAE-----NVWNLRRKIGMVFQNPD--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 rlpvltNVLVGRLHTMPWLRGVMGWFNAQERSAALA--ALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLAD 176
Cdd:PRK13642 92 ------NQFVGATVEDDVAFGMENQGIPREEMIKRVdeALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 177 EPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRyCPRVIALNQGQVIYDGPAAAL 239
Cdd:PRK13642 166 ESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-244 |
6.61e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.54 E-value: 6.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 17 HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAglLVADAGPGSLIeVNGQCVQREGRivSDIRSIRSQVGFVFQqfNL 96
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLT--MIETPTGGELY-YQGQDLLKADP--EAQKLLRQKIQIVFQ--NP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 97 VDRL------------PVLTNVLVGRlhtmpwlrgvmgwfnAQERSAALAALERVGILDCHKQR-ASTLSGGQQQRAAIA 163
Cdd:PRK11308 102 YGSLnprkkvgqileePLLINTSLSA---------------AERREKALAMMAKVGLRPEHYDRyPHMFSGGQRQRIAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 164 RTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQV--------DMAIRYCPRVIALNQGQVIYDGP 235
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLsvvehiadEVMVMYLGRCVEKGTKEQIFNNP 246
|
....*....
gi 518255160 236 AAALTPALL 244
Cdd:PRK11308 247 RHPYTQALL 255
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-239 |
6.95e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.37 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 18 ALRDIDLNIADGEMVALIGASGSGKSTllrmVAGLLVA--DAGPGSlIEVNGQCVQRegrivSDIRSIRSQVGFVFQQFN 95
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfyDIDEGE-ILLDGHDLRD-----YTLASLRNQVALVSQNVH 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 LVDRlPVLTNVLVGRLHTmpwlrgvmgWFNAQ-ERSAALA-ALERVGILD-----CHKQRASTLSGGQQQRAAIARTLVQ 168
Cdd:PRK11176 428 LFND-TIANNIAYARTEQ---------YSREQiEEAARMAyAMDFINKMDngldtVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518255160 169 GAKLVLADEPIASLDPDSSRKVMEILSTIQREdgRTVIVSLHQVDmAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-211 |
9.99e-16 |
|
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: 73.68 E-value: 9.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 22 IDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLievngqcvqrEGRIVSDIR-SIRSQVGFVFQQFNLVDRL 100
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL----------NGGPLDFQRdSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 101 PVLTNvlvgrlhtMPWLRGVMGwfnaqeRSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIA 180
Cdd:cd03231 89 SVLEN--------LRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|.
gi 518255160 181 SLDPDSSRKVMEILSTiQREDGRTVIVSLHQ 211
Cdd:cd03231 155 ALDKAGVARFAEAMAG-HCARGGMVVLTTHQ 184
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-234 |
2.10e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.27 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivsDIRSIRSQVGFVFQQfnlVD 98
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGA---VLWQGKPLDYSKR---GLLALRQQVATVFQD---PE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 RLPVLTNVLVGRLHTMPWLrGVMGWFNAQERSAALAALERVGIldcHKQRASTLSGGQQQRAAIARTLVQGAKLVLADEP 178
Cdd:PRK13638 88 QQIFYTDIDSDIAFSLRNL-GVPEAEITRRVDEALTLVDAQHF---RHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 179 IASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDG 234
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-239 |
2.35e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 75.63 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKH-ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEVNGQCVQRegrivSDI 80
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQG---EILLNGQPIAD-----YSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 RSIRSQVGFVFQqfnlvdRLPVLTNVLVGRLhtmpwlrgVMGWFNAQErSAALAALERVGiLDCHKQRAS---------- 150
Cdd:PRK11160 410 AALRQAISVVSQ------RVHLFSATLRDNL--------LLAAPNASD-EALIEVLQQVG-LEKLLEDDKglnawlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 151 -TLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLHQVdMAIRYCPRVIALNQGQ 229
Cdd:PRK11160 474 rQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRL-TGLEQFDRICVMDNGQ 550
|
250
....*....|
gi 518255160 230 VIYDGPAAAL 239
Cdd:PRK11160 551 IIEQGTHQEL 560
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-239 |
3.45e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALR---DIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAG--PGSLIEVNGQCVQREGRiv 77
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTvvnDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVvyPSGDIRFHGESLLHASE-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 SDIRSIR-SQVGFVFQQfnlvdrlPVltnVLVGRLHTM-PWLRGVMGWFNAQERSAA----LAALERVGILDCHKQRAS- 150
Cdd:PRK15134 84 QTLRGVRgNKIAMIFQE-------PM---VSLNPLHTLeKQLYEVLSLHRGMRREAArgeiLNCLDRVGIRQAAKRLTDy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 151 --TLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQG 228
Cdd:PRK15134 154 phQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
250
....*....|.
gi 518255160 229 QVIYDGPAAAL 239
Cdd:PRK15134 234 RCVEQNRAATL 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-240 |
6.31e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 7 NLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQregrIVSDIRSIRSQ 86
Cdd:PRK10982 3 NISKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS---ILFQGKEID----FKSSKEALENG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 87 VGFVFQQFNLVDRLPVLTNVLVGRLHTmpwlrgvMGWFNAQER--SAALAALERVGILDCHKQRASTLSGGQQQRAAIAR 164
Cdd:PRK10982 75 ISMVHQELNLVLQRSVMDNMWLGRYPT-------KGMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 165 TLVQGAKLVLADEPIASLdpdSSRKVMEILSTIQ--REDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALT 240
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSL---TEKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLT 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-228 |
8.75e-15 |
|
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: 74.66 E-value: 8.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFA-NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSlieVNGQcvqregRIVSDIR 81
Cdd:TIGR01257 1938 LRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAT---VAGK------SILTNIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVfQQFNLVDRLpvltnvLVGRLHTMPW--LRGVmgwfNAQE-RSAALAALERVGILDCHKQRASTLSGGQQQ 158
Cdd:TIGR01257 2009 DVHQNMGYC-PQFDAIDDL------LTGREHLYLYarLRGV----PAEEiEKVANWSIQSLGLSLYADRLAGTYSGGNKR 2077
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 159 RAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQG 228
Cdd:TIGR01257 2078 KLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-210 |
1.37e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.29 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGllVADAGpgslievngqcvQREGRIVSD--- 79
Cdd:NF040905 2 LEMRGITKTFP-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG--VYPHG------------SYEGEILFDgev 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 --IRSIRS--QVGFVF--QQFNLVDRLPVLTNVLVGRLHTMpwlRGVMGWFNAQERSAALaaLERVGILDCHKQRASTLS 153
Cdd:NF040905 67 crFKDIRDseALGIVIihQELALIPYLSIAENIFLGNERAK---RGVIDWNETNRRAREL--LAKVGLDESPDTLVTDIG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLH 210
Cdd:NF040905 142 VGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-227 |
1.50e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANgKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslievngqCVQREGRIvsdirs 82
Cdd:PRK09544 5 VSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKL------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 irsQVGFVFQQFNLVDRLPvLTnvlVGRLhtMPWLRGVmgwfnaqERSAALAALERVGILDCHKQRASTLSGGQQQRAAI 162
Cdd:PRK09544 68 ---RIGYVPQKLYLDTTLP-LT---VNRF--LRLRPGT-------KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLL 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQ 227
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-247 |
1.52e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.74 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 18 ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQregriVSDIrSIRSQ-VGFVFQ---- 92
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE---LLIDDHPLH-----FGDY-SYRSQrIRMIFQdpst 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 93 QFNLVDRLPVLTNVLVgRLHTMpwlrgvmgwFNAQERSAAL-AALERVGILDCHKQR-ASTLSGGQQQRAAIARTLVQGA 170
Cdd:PRK15112 99 SLNPRQRISQILDFPL-RLNTD---------LEPEQREKQIiETLRQVGLLPDHASYyPHMLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 171 KLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAALTPALLRDL 247
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHEL 245
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-251 |
1.84e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 26 IADGEMVALIGASGSGKSTLLRMVAGLLvadAGPGSlIEVNGQCV-QREGRIVSDIRsirsqvGFVFQQFNLVDRLPV-- 102
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL---PGSGS-IQFAGQPLeAWSAAELARHR------AYLSQQQTPPFAMPVfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 103 -LTnvlvgrLHtMPwlrgvmgwfnAQERSAALAAL-----ERVGILDCHKQRASTLSGGQQQRAAIARTLVQ-------G 169
Cdd:PRK03695 89 yLT------LH-QP----------DKTRTEAVASAlnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 170 AKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAA-ALTPALLRDLY 248
Cdd:PRK03695 152 GQLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDeVLTPENLAQVF 230
|
...
gi 518255160 249 GMQ 251
Cdd:PRK03695 231 GVN 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-210 |
1.89e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 72.93 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqregrivsDIR-----SIRSQVGFVFQQ 93
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGR---ILIDGQ----------DIRdvtqaSLRAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 ---FNlvDRLpvLTNVLVGRLHTMPwlrgvmgwfnAQERSAA-LAALE------------RVGildchkQRASTLSGGQQ 157
Cdd:COG5265 441 tvlFN--DTI--AYNIAYGRPDASE----------EEVEAAArAAQIHdfieslpdgydtRVG------ERGLKLSGGEK 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRedGRTVIVSLH 210
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH 551
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
5-234 |
3.65e-14 |
|
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: 69.60 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 5 IQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREGRivsdirSIR 84
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFAE------KYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 85 SQVGFVFQQfnlvDR-LPVLTnvlVGrlHTMpwlrgvmgwfnaqERSAALAALERV-GIldchkqrastlSGGQQQRAAI 162
Cdd:cd03233 83 GEIIYVSEE----DVhFPTLT---VR--ETL-------------DFALRCKGNEFVrGI-----------SGGERKRVSI 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSSrkvMEILSTIQ---REDGRTVIVSLHQVDMAIRYC-PRVIALNQGQVIYDG 234
Cdd:cd03233 130 AEALVSRASVLCWDNSTRGLDSSTA---LEILKCIRtmaDVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQIYYG 202
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-257 |
4.62e-14 |
|
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: 70.13 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 25 NIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslievngqcvqregrivsDIRSIRSQVGFVFQQfnlvdrlpvLT 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG--------------------DIEIELDTVSYKPQY---------IK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 105 NVLVGRLHTMpwLRGVMGWF--NAQERSAALAALERVGILDchkQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASL 182
Cdd:cd03237 72 ADYEGTVRDL--LSSITKDFytHPYFKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 183 DPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIalnqgqvIYDGPAA----ALTPALLRDlyGMqaDEFLS 257
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI-------VFEGEPSvngvANPPQSLRS--GM--NRFLK 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-208 |
4.81e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 22 IDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRIvsdirsirsqvgfvfQQFNLVDRLP 101
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQ---IQIDGKTATRGDRS---------------RFMAYLGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 102 VLTNVLvGRLHTMPWLRGVMGWFNAQERSAALAAlerVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIAS 181
Cdd:PRK13543 92 GLKADL-STLENLHFLCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180
....*....|....*....|....*..
gi 518255160 182 LDPDSSRKVMEILSTIQREDGRTVIVS 208
Cdd:PRK13543 168 LDLEGITLVNRMISAHLRGGGAALVTT 194
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-239 |
4.94e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.06 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivSDIRSIRSQVGFVFQQFNLVD 98
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQ---VLLDGVPLVQ-----YDHHYLHRQVALVGQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 RlPVLTNVLVGRLHTMpwlrgvmgwfNAQERSAALAALERVGILDCHK-------QRASTLSGGQQQRAAIARTLVQGAK 171
Cdd:TIGR00958 569 G-SVRENIAYGLTDTP----------DEEIMAAAKAANAHDFIMEFPNgydtevgEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 172 LVLADEPIASLDPDSSRKVMEILStiqrEDGRTVIVSLHQVDMaIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQESRS----RASRTVLLIAHRLST-VERADQILVLKKGSVVEMGTHKQL 700
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-251 |
7.52e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.73 E-value: 7.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 20 RDIDLNIADGEMVALIGASGSGKSTL-----------LRMVAGLLVADAGPGSLIEVNGQCVqreGRIVSDIRSirsqvg 88
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTcaaalgilpagVRQTAGRVLLDGKPVAPCALRGRKI---ATIMQNPRS------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 89 fvfqQFNlvdrlPVLTNvlvgRLHTMPWLRGVMGwfnAQERSAALAALERVGILDCH---KQRASTLSGGQQQRAAIART 165
Cdd:PRK10418 91 ----AFN-----PLHTM----HTHARETCLALGK---PADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 166 LVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAAAL------ 239
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLfnapkh 234
|
250
....*....|....*..
gi 518255160 240 --TPALL---RDLYGMQ 251
Cdd:PRK10418 235 avTRSLVsahLALYGME 251
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-248 |
1.61e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.55 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLnkHFA-NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLlvadagPGSLIEvngqcvqrEGRIVSDIR 81
Cdd:cd03217 1 LEIKDL--HVSvGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH------PKYEVT--------EGEILFKGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SI-------RSQVGfVFQQFNLVDRLPVLTNvlvgrlhtMPWLRGVmgwfnaqersaalaaleRVGildchkqrastLSG 154
Cdd:cd03217 65 DItdlppeeRARLG-IFLAFQYPPEIPGVKN--------ADFLRYV-----------------NEG-----------FSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 155 GQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCP-RVIALNQGQVIYD 233
Cdd:cd03217 108 GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIKPdRVHVLYDGRIVKS 186
|
250
....*....|....*
gi 518255160 234 GPaaaltPALLRDLY 248
Cdd:cd03217 187 GD-----KELALEIE 196
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-234 |
1.66e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 26 IADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVqregrivsdiRSIRSQVGFVFQQFNLVDRLPVLTN 105
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPT----------KQILKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 106 VLVGRLHTMPwlrgvmGWFNAQER-SAALAALERVGILDCHKQRAST-----LSGGQQQRAAIARTLVQGAKLVLADEPI 179
Cdd:PLN03211 161 LVFCSLLRLP------KSLTKQEKiLVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 180 ASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAI-RYCPRVIALNQGQVIYDG 234
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFG 289
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-211 |
2.42e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivsDIRSIRSQVGFVFQQFNLVD 98
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE---ILFERQSIKK------DLCTYQKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 RLPVLTNVLVGrLHTMPWLRGVmgwfnaqERSAALAALERVGILDChkqraSTLSGGQQQRAAIARTLVQGAKLVLADEP 178
Cdd:PRK13540 88 YLTLRENCLYD-IHFSPGAVGI-------TELCRLFSLEHLIDYPC-----GLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|....*
gi 518255160 179 IASLDpdsSRKVMEILSTIQ--REDGRTVIVSLHQ 211
Cdd:PRK13540 155 LVALD---ELSLLTIITKIQehRAKGGAVLLTSHQ 186
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-228 |
2.44e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 67.74 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRIVSDIRSiRSQVGFVFQQFNLVD 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK---VHWSNKNESEPSFEATRSRN-RYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 RlPVLTNVLVGRlhtmPwlrgvmgwFNAQERSAALAALE---RVGILDCHKQ-----RASTLSGGQQQRAAIARTLVQGA 170
Cdd:cd03290 93 A-TVEENITFGS----P--------FNKQRYKAVTDACSlqpDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 171 KLVLADEPIASLDPDSSRKVME--ILSTIQrEDGRTVIVSLHQvdmaIRYCPR---VIALNQG 228
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQegILKFLQ-DDKRTLVLVTHK----LQYLPHadwIIAMKDG 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-267 |
3.79e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.36 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 5 IQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslievngqcVQREGRIVSDI--RS 82
Cdd:PRK10790 343 IDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE----------IRLDGRPLSSLshSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVfQQFNLVDRLPVLTNVLVGRLHTMPWLRGVMgwfnaqeRSAALAALERV---GILDCHKQRASTLSGGQQQR 159
Cdd:PRK10790 413 LRQGVAMV-QQDPVVLADTFLANVTLGRDISEEQVWQAL-------ETVQLAELARSlpdGLYTPLGEQGNNLSVGQKQL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDgrTVIVSLHQVDmAIRYCPRVIALNQGQVIYDGPAAAL 239
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLS-TIVEADTILVLHRGQAVEQGTHQQL 561
|
250 260 270
....*....|....*....|....*....|
gi 518255160 240 TPALLR--DLYGMQadefLSGSELLQSAQA 267
Cdd:PRK10790 562 LAAQGRywQMYQLQ----LAGEELAASVRE 587
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-251 |
3.95e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 13 ANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslievngqcVQREGRIVSDIR--SIRSQVGFV 90
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD----------IRFHDIPLTKLQldSWRSRLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 91 FQQ-FNLVDRlpVLTNVLVGRLHTMPwlrgvmgwfNAQERSAALAALE------------RVGildchkQRASTLSGGQQ 157
Cdd:PRK10789 395 SQTpFLFSDT--VANNIALGRPDATQ---------QEIEHVARLASVHddilrlpqgydtEVG------ERGVMLSGGQK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILStiQREDGRTVIVSLHQVDmAIRYCPRVIALNQGQVIYDGPAA 237
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHD 534
|
250
....*....|....*.
gi 518255160 238 ALT--PALLRDLYGMQ 251
Cdd:PRK10789 535 QLAqqSGWYRDMYRYQ 550
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-242 |
5.73e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegriVSDIRS 82
Cdd:PRK15439 12 LCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT---LEIGGNPCAR----LTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVGrlhtMPwlrgvmgwfNAQERSAALAALerVGILDCH---KQRASTLSGGQQQR 159
Cdd:PRK15439 84 HQLGIYLVPQEPLLFPNLSVKENILFG----LP---------KRQASMQKMKQL--LAALGCQldlDSSAGSLEVADRQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSlHQVDMAIRYCPRVIALNQGQVIYDGPAA-- 237
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFIS-HKLPEIRQLADRISVMRDGTIALSGKTAdl 227
|
250
....*....|..
gi 518255160 238 -------ALTPA 242
Cdd:PRK15439 228 stddiiqAITPA 239
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-229 |
7.79e-13 |
|
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: 64.39 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslievngqcvqregrIVSDIRS 82
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-----------------IVTWGST 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRsqVGFvFQQfnlvdrlpvltnvlvgrlhtmpwlrgvmgwfnaqersaalaalervgildchkqrastLSGGQQQRAAI 162
Cdd:cd03221 63 VK--IGY-FEQ----------------------------------------------------------LSGGEKMRLAL 81
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 163 ARTLVQGAKLVLADEPIASLDPDSsrkVMEILSTIQREDGRTVIVSlHQVDMAIRYCPRVIALNQGQ 229
Cdd:cd03221 82 AKLLLENPNLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVS-HDRYFLDQVATKIIELEDGK 144
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-236 |
1.32e-12 |
|
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: 67.37 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKH-ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQRegrivSDIR 81
Cdd:TIGR01842 317 LSVENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGS---VRLDGADLKQ-----WDRE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQFNLVDRlPVLTNVlvGRLHTMPWLRGVMgwfnaqerSAALAALERVGILDCHK-------QRASTLSG 154
Cdd:TIGR01842 389 TFGKHIGYLPQDVELFPG-TVAENI--ARFGENADPEKII--------EAAKLAGVHELILRLPDgydtvigPGGATLSG 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 155 GQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDmAIRYCPRVIALNQGQVIYDG 234
Cdd:TIGR01842 458 GQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPS-LLGCVDKILVLQDGRIARFG 535
|
..
gi 518255160 235 PA 236
Cdd:TIGR01842 536 ER 537
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-192 |
1.99e-12 |
|
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: 66.03 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslievngqcVQREGRIvsdirSIRSQVGFVfqqfnlvd 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK----------IKHSGRI-----SFSSQFSWI-------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 rLP--VLTNVLVGRLHTMPWLRGVMGWFNAQERSAALAALERVGIldchKQRASTLSGGQQQRAAIARTLVQGAKLVLAD 176
Cdd:cd03291 110 -MPgtIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVL----GEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170
....*....|....*.
gi 518255160 177 EPIASLDPDSSRKVME 192
Cdd:cd03291 185 SPFGYLDVFTEKEIFE 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-237 |
2.59e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 18 ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIevngqcvqreGRIV--SDIrSIRSQVGFVFQQFN 95
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLF----------GQPVdaGDI-ATRRRVGYMSQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 LVDRLPVLTN-VLVGRLHTMPwlrgvmgwfnAQERSAALAAL-ERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLV 173
Cdd:NF033858 350 LYGELTVRQNlELHARLFHLP----------AAEIAARVAEMlERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 174 LADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRyCPRVIALNQGQV-IYDGPAA 237
Cdd:NF033858 420 ILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVlASDTPAA 483
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-206 |
3.32e-12 |
|
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: 63.33 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 14 NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVAdagpgslievngqcvqREGRIvsdIRSIRSQVGFVFQQ 93
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPW----------------GSGRI---GMPEGEDLLFLPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 fnlvdrlPVLTnvlVGRLHTM---PWLRgvmgwfnaqersaalaalervgildchkqrasTLSGGQQQRAAIARTLVQGA 170
Cdd:cd03223 73 -------PYLP---LGTLREQliyPWDD--------------------------------VLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*.
gi 518255160 171 KLVLADEPIASLDPDSSRKVMEILstiqREDGRTVI 206
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLL----KELGITVI 142
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-210 |
3.67e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREgrivsDIRS 82
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE---ILLDGKPVTAE-----QPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLpvltnvlvgrlhtmpwlrgvMGWFNAQERSAALAA-LERVGI-----LDCHKQRASTLSGGQ 156
Cdd:PRK10522 395 YRKLFSAVFTDFHLFDQL--------------------LGPEGKPANPALVEKwLERLKMahkleLEDGRISNLKLSKGQ 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518255160 157 QQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLH 210
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-236 |
5.55e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.93 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLnkHFA-NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLlvadagPGslIEVNgqcvqrEGRIVSDIR 81
Cdd:COG0396 1 LEIKNL--HVSvEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH------PK--YEVT------SGSILLDGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SI-------RSQVG-FV-FQQfnlvdrlPV--------------LTNVLVGRLHTMPWLRGVmgwfnaqersaaLAALER 138
Cdd:COG0396 65 DIlelspdeRARAGiFLaFQY-------PVeipgvsvsnflrtaLNARRGEELSAREFLKLL------------KEKMKE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 139 VGILDCHKQRA--STLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQ----- 211
Cdd:COG0396 126 LGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHYqrild 204
|
250 260
....*....|....*....|....*...
gi 518255160 212 ---VDmairycpRVIALNQGQVIYDGPA 236
Cdd:COG0396 205 yikPD-------FVHVLVDGRIVKSGGK 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-246 |
8.19e-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: 65.35 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLrmvAGLLvadagpgslievnGQCVQREGRIvsdirSIRSQVGFVFQQfNLVD 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLL---SALL-------------AEMDKVEGHV-----HMKGSVAYVPQQ-AWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 RLPVLTNVLVGRLHTMPWLRGVMgwfnaqERSAALAALERVGILDCHK--QRASTLSGGQQQRAAIARTLVQGAKLVLAD 176
Cdd:TIGR00957 712 NDSLRENILFGKALNEKYYQQVL------EACALLPDLEILPSGDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518255160 177 EPIASLDPDSSRKVME-ILSTIQREDGRTVIVSLHqvdmAIRYCPRV---IALNQGQVIYDGPAAALtpaLLRD 246
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTH----GISYLPQVdviIVMSGGKISEMGSYQEL---LQRD 852
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-239 |
1.14e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFanGK-HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsLIEV-NGQCVQREGRivsd 79
Cdd:NF033858 1 VARLEGVSHRY--GKtVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQG---RVEVlGGDMADARHR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 iRSIRSQVGFVFQQF--NLVDRLPVLTNV-LVGRLhtmpwlrgvmgwF--NAQERSAALAALERVGILDCHKQR-ASTLS 153
Cdd:NF033858 72 -RAVCPRIAYMPQGLgkNLYPTLSVFENLdFFGRL------------FgqDAAERRRRIDELLRATGLAPFADRpAGKLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQRE-DGRTVIVSLHQVDMAIRYcPRVIALNQGQVIY 232
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErPGMSVLVATAYMEEAERF-DWLVAMDAGRVLA 217
|
....*..
gi 518255160 233 DGPAAAL 239
Cdd:NF033858 218 TGTPAEL 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-234 |
2.46e-11 |
|
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: 61.18 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 17 HALRDIDLNIADGEMVALIGASGSGKSTLLRmvagllvadagpgslievngQCVQREGRIvsdiRSIRSQVGFVFQQFNL 96
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--------------------EGLYASGKA----RLISFLPKFSRNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 97 VDRLPVLTNVLVGRLhtmpwlrgvmgwfnaqersaalaaleRVGildchkQRASTLSGGQQQRAAIARTLVQGAK--LVL 174
Cdd:cd03238 65 IDQLQFLIDVGLGYL--------------------------TLG------QKLSTLSGGELQRVKLASELFSEPPgtLFI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 175 ADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMaIRYCPRVIALNQGQVIYDG 234
Cdd:cd03238 113 LDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDV-LSSADWIIDFGPGSGKSGG 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-192 |
2.56e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.16 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslievngqcVQREGRIvsdirSIRSQVGFVfqqfnlvd 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK----------IKHSGRI-----SFSPQTSWI-------- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 rLP--VLTNVLVGRLHTMPWLRGVMGWFNAQERSAALAALERVGILDchkqRASTLSGGQQQRAAIARTLVQGAKLVLAD 176
Cdd:TIGR01271 499 -MPgtIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGE----GGITLSGGQRARISLARAVYKDADLYLLD 573
|
170
....*....|....*.
gi 518255160 177 EPIASLDPDSSRKVME 192
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFE 589
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
3-245 |
2.90e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.90 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALRDID---LNIADGEMVALIGASGSGKSTLLRMVAGL------LVADAGPGSLIEVNgQCVQRE 73
Cdd:PRK15093 4 LDIRNLTIEFKTSDGWVKAVDrvsMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrVTADRMRFDDIDLL-RLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 74 GRivsdiRSIRSQVGFVFQQ------------FNLVDRLPVLTnvLVGRLhtmpWLRgvmgwFNAQERSAaLAALERVGI 141
Cdd:PRK15093 83 RR-----KLVGHNVSMIFQEpqscldpservgRQLMQNIPGWT--YKGRW----WQR-----FGWRKRRA-IELLHRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 142 LDcHKQRAST----LSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIR 217
Cdd:PRK15093 146 KD-HKDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQ 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 518255160 218 YCPRVIALNQGQVIYDGPAAAL--------TPALLR 245
Cdd:PRK15093 225 WADKINVLYCGQTVETAPSKELvttphhpyTQALIR 260
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-238 |
2.96e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLrmvagllvadagpGSLIevnGQCVQREGRIVSDiRSIrsqvGFVFQQfn 95
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLL-------------QSLL---SQFEISEGRVWAE-RSI----AYVPQQ-- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 lvdrlPVLTNVLVgrlhtmpwlRGVMGWFNaQERSAALAALERVGILDCHKQRAS------------TLSGGQQQRAAIA 163
Cdd:PTZ00243 730 -----AWIMNATV---------RGNILFFD-EEDAARLADAVRVSQLEADLAQLGggleteigekgvNLSGGQKARVSLA 794
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 164 RTLVQGAKLVLADEPIASLDPDSSRKVME--ILSTIQredGRTVIVSLHQVDMAIRyCPRVIALNQGQVIYDGPAAA 238
Cdd:PTZ00243 795 RAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALA---GKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSAD 867
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-235 |
3.64e-11 |
|
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: 61.27 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFA-NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVqreGRIvsDIR 81
Cdd:cd03369 7 IEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGK---IEIDGIDI---STI--PLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQQfnlvdrlPVLTnvlvgrlhtMPWLRGVMGWFNAQERSAALAALeRVgildchKQRASTLSGGQQQRAA 161
Cdd:cd03369 79 DLRSSLTIIPQD-------PTLF---------SGTIRSNLDPFDEYSDEEIYGAL-RV------SEGGLNLSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDSSRKVMEilsTIQRE-DGRTVIVSLHQVDMAIRyCPRVIALNQGQVI-YDGP 235
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQK---TIREEfTNSTILTIAHRLRTIID-YDKILVMDAGEVKeYDHP 207
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-236 |
4.37e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.43 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 18 ALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCV----QREgriVSDIRSirSQVGFVFQ- 92
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREIlnlpEKE---LNKLRA--EQISMIFQd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 93 ---QFNLVDRL-PVLTNVLVgrLHtmpwlRGVmgwfnaqerSAALAALERVGILDCHK-----QRAST----LSGGQQQR 159
Cdd:PRK09473 106 pmtSLNPYMRVgEQLMEVLM--LH-----KGM---------SKAEAFEESVRMLDAVKmpearKRMKMypheFSGGMRQR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPA 236
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-230 |
4.81e-11 |
|
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: 61.33 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTllrmVAGLLVADAGP-GSLIEVNGQCVQRegrivSDIRSIRSQVGFVFQQFNLV 97
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKST----VVALLENFYQPqGGQVLLDGKPISQ-----YEHKYLHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 98 DRlPVLTNVLVGrLHTMPWLRGVmgwfNAQERSAA---LAALERvGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVL 174
Cdd:cd03248 101 AR-SLQDNIAYG-LQSCSFECVK----EAAQKAHAhsfISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 175 ADEPIASLDPDSSRKVMEILStiQREDGRTVIVSLHQVDMaIRYCPRVIALNQGQV 230
Cdd:cd03248 174 LDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLST-VERADQILVLDGGRI 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-230 |
4.85e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.26 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLL----RMVAGLlvadagpGSLIEVNGQCVQREGrivsdIRSIRsqvgfvfQQF 94
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMVEVC-------GGEIRVNGREIGAYG-----LRELR-------RQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 95 NLVDRLPVLTNVLVgRLHTMPWLRGvmgwfNAQERSAALAAL---ERV-----GILDCHKQRASTLSGGQQQRAAIARTL 166
Cdd:PTZ00243 1387 SMIPQDPVLFDGTV-RQNVDPFLEA-----SSAEVWAALELVglrERVaseseGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 167 VQ-GAKLVLADEPIASLDPDSSRK----VMEILStiqredGRTVIVSLHQVDMAIRYcPRVIALNQGQV 230
Cdd:PTZ00243 1461 LKkGSGFILMDEATANIDPALDRQiqatVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAV 1522
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-186 |
4.88e-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: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 5 IQNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLlvaDAgpgsliEVNGQCVQREGRivsdirsir 84
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DK------DFNGEARPQPGI--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 85 sQVGFVFQQFNLVDRLPVLTNVLVGrlhtMPWLRGVMGWFNaqERSAALAA--------LERVG----ILDCHK------ 146
Cdd:TIGR03719 69 -KVGYLPQEPQLDPTKTVRENVEEG----VAEIKDALDRFN--EISAKYAEpdadfdklAAEQAelqeIIDAADawdlds 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 147 ---------------QRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDS 186
Cdd:TIGR03719 142 qleiamdalrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-244 |
5.29e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.95 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKH---ALRDIDLNIADGEMVALIGASGSGKS----TLLRMVAGllvadagPGSLIEVNGQCVQREGR 75
Cdd:PRK10261 13 LAVENLNIAFMQEQQkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQ-------AGGLVQCDKMLLRRRSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 76 IV--------SDIRSIR-SQVGFVFQQfNLVDRLPVLTnvlVG-------RLHtmpwlrgvMGWFNAQERSAALAALERV 139
Cdd:PRK10261 86 QVielseqsaAQMRHVRgADMAMIFQE-PMTSLNPVFT---VGeqiaesiRLH--------QGASREEAMVEAKRMLDQV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 140 GILDCH---KQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAI 216
Cdd:PRK10261 154 RIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVA 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 518255160 217 RYCPRVIALNQGQV--------IYDGPAAALTPALL 244
Cdd:PRK10261 234 EIADRVLVMYQGEAvetgsveqIFHAPQHPYTRALL 269
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-242 |
1.47e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 61.35 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 22 IDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGRivsdiRSIRSQVGFVFQQFNLVDRLP 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE---ILLDGQPVTADNR-----EAYRQLFSAVFSDFHLFDRLL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 102 VLT-NVLVGRLHTMpwlrgvmgwfnaqersaaLAALErvgiLDcHK-----QRAST--LSGGQQQRAAIARTLVQGAKLV 173
Cdd:COG4615 423 GLDgEADPARAREL------------------LERLE----LD-HKvsvedGRFSTtdLSQGQRKRLALLVALLEDRPIL 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518255160 174 LADEPIASLDPDsSRKV--MEILSTIQREdGRTVIVSLHQvDmaiRY---CPRVIALNQGQVIYDGPAAALTPA 242
Cdd:COG4615 480 VFDEWAADQDPE-FRRVfyTELLPELKAR-GKTVIAISHD-D---RYfdlADRVLKMDYGKLVELTGPAALAAS 547
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-234 |
1.67e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.18 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSlIEVNGqcvqREGRIvsdirSIRSQVGFVFQQFNLvd 98
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGE-ILING----RPLDK-----NFQRSTGYVEQQDVH-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 rLPVLTNVLVGRLHTmpWLRGvmgwfnaqersaalaalervgildchkqrastLSGGQQQRAAIARTLVQGAKLVLADEP 178
Cdd:cd03232 91 -SPNLTVREALRFSA--LLRG--------------------------------LSVEQRKRLTIGVELAAKPSILFLDEP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 179 IASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAI-RYCPRVIAL-NQGQVIYDG 234
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPSASIfEKFDRLLLLkRGGKTVYFG 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-230 |
1.76e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 5 IQNLNKHfANGKhaLRDIDLNIADGEMVALIGASGSGKSTLLRMVAGllvADAGPGSLIEVNGqcvqREGRIVSDIRSIR 84
Cdd:PRK09700 268 VRNVTSR-DRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFG---VDKRAGGEIRLNG----KDISPRSPLDAVK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 85 SQVGFV---------FQQFNLVDRLPVLTNVLVGRLhtmpwlRGVMGWFN-AQERSAALAALERVGIlDCH--KQRASTL 152
Cdd:PRK09700 338 KGMAYItesrrdngfFPNFSIAQNMAISRSLKDGGY------KGAMGLFHeVDEQRTAENQRELLAL-KCHsvNQNITEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSR---KVMEILStiqrEDGRTVIVSLHQVDMAIRYCPRVIALNQGQ 229
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAeiyKVMRQLA----DDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
.
gi 518255160 230 V 230
Cdd:PRK09700 487 L 487
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-234 |
6.70e-10 |
|
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: 58.04 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 17 HALRDIDLNIADGEMVALIGASGSGKSTL----------LRMVAGLLV-ADAGPGSL-------IEVNGQCVQREGRIVS 78
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAyARQFLGQMdkpdvdsIEGLSPAIAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 79 diRSIRSQVGFV----------FQQFNLVDRLPVLTNVLVGRLhtmpwlrgvmgwfnaqersaalaALERvgildchkqR 148
Cdd:cd03270 89 --RNPRSTVGTVteiydylrllFARVGIRERLGFLVDVGLGYL-----------------------TLSR---------S 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 149 ASTLSGGQQQRAAIARTLvqGAKLV----LADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMaIRYCPRVIA 224
Cdd:cd03270 135 APTLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDT-IRAADHVID 210
|
250
....*....|....*.
gi 518255160 225 L------NQGQVIYDG 234
Cdd:cd03270 211 IgpgagvHGGEIVAQG 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-234 |
8.11e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslievnGQCVqregrivsdirsIRSQVGFVFQQ-- 93
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD--------ASVV------------IRGTVAYVPQVsw 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 -FNLVDRlpvlTNVLVGrlhtMPwlrgvmgwFNAQ--ERSAALAALER-VGILDCHKQ-----RASTLSGGQQQRAAIAR 164
Cdd:PLN03130 690 iFNATVR----DNILFG----SP--------FDPEryERAIDVTALQHdLDLLPGGDLteigeRGVNISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518255160 165 TLVQGAKLVLADEPIASLDPDSSRKVMEilSTIQREDGRT--VIVS--LH---QVDmairycpRVIALNQGQVIYDG 234
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELRGKtrVLVTnqLHflsQVD-------RIILVHEGMIKEEG 821
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-235 |
1.19e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGllvadAGPGSLIE-----------------VNGQCVQregrivSDIR 81
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-----RKTGGYIEgdirisgfpkkqetfarISGYCEQ------NDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQV--GFVFQQFNlvdRLPVLtnvlVGRLHTMPWLRGVMGWFNAQERSAALAALERVgildchkqraSTLSGGQQQR 159
Cdd:PLN03140 965 SPQVTVreSLIYSAFL---RLPKE----VSKEEKMMFVDEVMELVELDNLKDAIVGLPGV----------TGLSTEQRKR 1027
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 160 AAIARTLVQGAKLVLADEPIASLDPDSSRKVME-ILSTIqrEDGRTVIVSLHQ--VDMAIRYCPRVIALNQGQVIYDGP 235
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRtVRNTV--DTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYSGP 1104
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-194 |
1.61e-09 |
|
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: 58.02 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVnGQCVqregrivsdirs 82
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT---IEI-GETV------------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 irsQVGFVFQQF-NLVDRLPV-------LTNVLVGRlHTMPwLRGVMGWFN----AQERsaalaaleRVGIldchkqras 150
Cdd:TIGR03719 386 ---KLAYVDQSRdALDPNKTVweeisggLDIIKLGK-REIP-SRAYVGRFNfkgsDQQK--------KVGQ--------- 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518255160 151 tLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEIL 194
Cdd:TIGR03719 444 -LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL 486
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
91-273 |
3.07e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.53 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 91 FQQFNLvDRLPVLTNVLVgrlHTMPWLRGVMGWFNAQersaaLAALERVGILDCHKQRA-STLSGGQQQRAAIARTLvqG 169
Cdd:PRK00635 424 FQQMSL-QELFIFLSQLP---SKSLSIEEVLQGLKSR-----LSILIDLGLPYLTPERAlATLSGGEQERTALAKHL--G 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 170 AKLV----LADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMaIRYCPRVIALNQGQVIYDGPAaaltpallr 245
Cdd:PRK00635 493 AELIgityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQM-ISLADRIIDIGPGAGIFGGEV--------- 561
|
170 180 190
....*....|....*....|....*....|..
gi 518255160 246 dLYGMQADEFLSGSELLQSA----QAQIPSPV 273
Cdd:PRK00635 562 -LFNGSPREFLAKSDSLTAKylrqELTIPIPE 592
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-236 |
3.41e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVadagpGSLIEVNGQcVQREGRIVSDI-RSIRSQVGFVFQQFNlv 97
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTD-----GFHIGVEGV-ITYDGITPEEIkKHYRGDVVYNAETDV-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 98 dRLPVLTN----VLVGRLHTmPWLRgVMGW----FNAQERSAALAALervGILDCHKQRAST-----LSGGQQQRAAIAR 164
Cdd:TIGR00956 149 -HFPHLTVgetlDFAARCKT-PQNR-PDGVsreeYAKHIADVYMATY---GLSHTRNTKVGNdfvrgVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518255160 165 TLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDM-AIRYCPRVIALNQGQVIYDGPA 236
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGYQIYFGPA 295
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-186 |
3.47e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 1 MALrIQNLNKHFANGKHALRD-IDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADagPGSLIEVNGQCVQR------- 72
Cdd:PRK11147 1 MSL-ISIHGAWLSFSDAPLLDnAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLD--DGRIIYEQDLIVARlqqdppr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 73 --EGRIVSDIRSIRSQVGFVFQQFNLVDRLpVLTNVLVGRLHTMPWLRGVM----GWfnaQERSAALAALERVGiLDCHK 146
Cdd:PRK11147 78 nvEGTVYDFVAEGIEEQAEYLKRYHDISHL-VETDPSEKNLNELAKLQEQLdhhnLW---QLENRINEVLAQLG-LDPDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518255160 147 QRAStLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDS 186
Cdd:PRK11147 153 ALSS-LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-253 |
4.03e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.26 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTllrMVAGLL-VADAGPGSLIeVNGQCVQREGrivsdIRSIRSQVGFVFQQfnlv 97
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFrINESAEGEII-IDGLNIAKIG-----LHDLRFKITIIPQD---- 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 98 drlPVLTNVLVgRLHTMPWlrgvmGWFNAQERSAAL---------AALERVGILDChKQRASTLSGGQQQRAAIARTLVQ 168
Cdd:TIGR00957 1369 ---PVLFSGSL-RMNLDPF-----SQYSDEEVWWALelahlktfvSALPDKLDHEC-AEGGENLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 169 GAKLVLADEPIASLDPDSSRKVMEILSTiQREDGrTVIVSLHQVDMAIRYCpRVIALNQGQVI-YDGPAAALTPALLrdL 247
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRT-QFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEVAeFGAPSNLLQQRGI--F 1513
|
....*.
gi 518255160 248 YGMQAD 253
Cdd:TIGR00957 1514 YSMAKD 1519
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-214 |
4.08e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 26 IADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgsliEVNG--------QCVQR--EGRIVSDIRSIRSQVGFVFQQFN 95
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG-----EVDPelkisykpQYIKPdyDGTVEDLLRSITDDLGSSYYKSE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 LVDRLpvltnvlvgrlhtmpwlrgvmgwfnaqersaalaALERvgILDchkQRASTLSGGQQQRAAIARTLVQGAKLVLA 175
Cdd:PRK13409 437 IIKPL----------------------------------QLER--LLD---KNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190
....*....|....*....|....*....|....*....
gi 518255160 176 DEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDM 214
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYM 516
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-240 |
4.08e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLlrmVAGLLvadagpGSLIEVNGQCVqregrivsdirSIRSQVGFVfQQFN 95
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSL---ISAML------GELSHAETSSV-----------VIRGSVAYV-PQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 LVDRLPVLTNVLVGRLHTMPWLRGVMGWFNAQERSAALAALERVGIldchKQRASTLSGGQQQRAAIARTLVQGAKLVLA 175
Cdd:PLN03232 689 WIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEI----GERGVNISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 176 DEPIASLDPDSSRKVMEilSTIQRE-DGRTVIVSLHQvdmaIRYCP---RVIALNQGQVIYDGPAAALT 240
Cdd:PLN03232 765 DDPLSALDAHVAHQVFD--SCMKDElKGKTRVLVTNQ----LHFLPlmdRIILVSEGMIKEEGTFAELS 827
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-230 |
4.17e-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: 56.02 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHA-LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslIEVNGQCVQRegrivSDIR 81
Cdd:cd03289 3 MTVKDLTAKYTEGGNAvLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGD----IQIDGVSWNS-----VPLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQVGFVFQqfnlvdRLPVLTNVLvgRLHTMPWlrgvmGWFNAQErsaALAALERVGILDCHKQ-----------RAS 150
Cdd:cd03289 74 KWRKAFGVIPQ------KVFIFSGTF--RKNLDPY-----GKWSDEE---IWKVAEEVGLKSVIEQfpgqldfvlvdGGC 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 151 TLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILStiQREDGRTVIVSLHQVDmAIRYCPRVIALNQGQV 230
Cdd:cd03289 138 VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIE-AMLECQRFLVIEENKV 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-226 |
5.24e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.96 E-value: 5.24e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 151 TLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVdMAIRYCPRVIALN 226
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFN 1432
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-239 |
5.89e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 2 ALRIQNLNKHFANGKhALRDIDLNIADGEMVALIGASGSG--KSTLLRMVAGllvADAGPGSLiEVNGQCVQREG--RIV 77
Cdd:NF000106 13 AVEVRGLVKHFGEVK-AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPW-RF*TWCANRRAlrRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 SDIRSIRSQVGfvfQQFNLVDRLpvltnVLVGRLHTMPwlrgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQ 157
Cdd:NF000106 88 G*HRPVR*GRR---ESFSGRENL-----YMIGR*LDLS---------RKDARARADELLERFSLTEAAGRAAAKYSGGMR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 158 QRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQReDGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYDGPAA 237
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVD 229
|
..
gi 518255160 238 AL 239
Cdd:NF000106 230 EL 231
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
16-235 |
6.08e-09 |
|
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: 55.31 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLL-----RMVAGLL-VADAGPGSLIEVNG-QCVQRegriVSDI------RS 82
Cdd:cd03271 8 ENNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLhLKKEQPGNHDRIEGlEHIDK----VIVIdqspigRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLpvLTNVLVGRLHTMPWL----RGV-------MGWFNAQERSAA-------LAALERVGiLDC 144
Cdd:cd03271 84 PRSNPATYTGVFDEIREL--FCEVCKGKRYNRETLevryKGKsiadvldMTVEEALEFFENipkiarkLQTLCDVG-LGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 145 HK--QRASTLSGGQQQRAAIARTLVQGAK---LVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMaIRYC 219
Cdd:cd03271 161 IKlgQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDV-IKCA 238
|
250 260
....*....|....*....|..
gi 518255160 220 PRVIAL------NQGQVIYDGP 235
Cdd:cd03271 239 DWIIDLgpeggdGGGQVVASGT 260
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-226 |
6.70e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHA--LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLvaDAGPGSLIeVNgqcvqrEGRIVSDI 80
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY--DPTEGDII-IN------DSHNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 81 --RSIRSQVGFVFQQ----------------FNLVDrLPVLTNVL---------------------VGRLHTM------P 115
Cdd:PTZ00265 454 nlKWWRSKIGVVSQDpllfsnsiknnikyslYSLKD-LEALSNYYnedgndsqenknkrnscrakcAGDLNDMsnttdsN 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 116 WLRGVMGWFNAQERSAALAALERVGILDCHK-----------QRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDP 184
Cdd:PTZ00265 533 ELIEMRKNYQTIKDSEVVDVSKKVLIHDFVSalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518255160 185 DSSRKVMEILSTIQREDGRTVIVSLHQVDmAIRYCPRVIALN 226
Cdd:PTZ00265 613 KSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLS 653
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-257 |
9.08e-09 |
|
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: 55.95 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 29 GEMVALIGASGSGKSTLLRMVAGLLVADagpgslievngqcvqrEGRIVSDIR-SIRSQvgFVFQQFNL-VDRLpvLTNV 106
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPD----------------EGEVDEDLKiSYKPQ--YISPDYDGtVEEF--LRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 107 LVGRLHTmpwlrgvmGWFNAQersaalaALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDS 186
Cdd:COG1245 426 NTDDFGS--------SYYKTE-------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 187 SRKVMEILSTIQREDGRTVIVSLHQVDMaIRY-CPRVIalnqgqvIYDG-PAA---ALTPALLRDlyGMqaDEFLS 257
Cdd:COG1245 491 RLAVAKAIRRFAENRGKTAMVVDHDIYL-IDYiSDRLM-------VFEGePGVhghASGPMDMRE--GM--NRFLK 554
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-216 |
2.70e-08 |
|
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: 54.41 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 29 GEMVALIGASGSGKSTLLRMVAGLLVADAG----PGSLIEV----NGQCVQREGRIVSD--IR-SIRSQvgfvfqqfnLV 97
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGdydeEPSWDEVlkrfRGTELQDYFKKLANgeIKvAHKPQ---------YV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 98 DRLPVLTNVLVGRLhtmpwLRgvmgwfNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADE 177
Cdd:COG1245 170 DLIPKVFKGTVREL-----LE------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518255160 178 PIASLDpdsSRKVMEILSTIQR--EDGRTVIVSLHqvDMAI 216
Cdd:COG1245 239 PSSYLD---IYQRLNVARLIRElaEEGKYVLVVEH--DLAI 274
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-216 |
5.20e-08 |
|
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: 52.75 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 27 ADGEMVALIGASGSGKSTLLRMVAGLLVADAG----PGSLIEV----NGQCVQ------REGrivsDIRSIRSQvgfvfq 92
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddPPDWDEIldefRGSELQnyftklLEG----DVKVIVKP------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 93 QFnlVDRLPVLTNVLVGRLHTMPWLRGVMgwfnaqerSAALAALERVGILDchkQRASTLSGGQQQRAAIARTLVQGAKL 172
Cdd:cd03236 94 QY--VDLIPKAVKGKVGELLKKKDERGKL--------DELVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518255160 173 VLADEPIASLDpdsSRKVMEILSTIQR--EDGRTVIVSLHqvDMAI 216
Cdd:cd03236 161 YFFDEPSSYLD---IKQRLNAARLIRElaEDDNYVLVVEH--DLAV 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-213 |
7.64e-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: 53.38 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 5 IQNLN-KHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslIEVNGqcvqregriVS----D 79
Cdd:TIGR01271 1220 VQGLTaKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE----IQIDG---------VSwnsvT 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 80 IRSIRSQVGFVFQqfnlvdRLPVLTNVLvgRLHTMPWLRgvmgWFNAQERSAAlaalERVGILDCHKQ-----------R 148
Cdd:TIGR01271 1287 LQTWRKAFGVIPQ------KVFIFSGTF--RKNLDPYEQ----WSDEEIWKVA----EEVGLKSVIEQfpdkldfvlvdG 1350
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 149 ASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILStiQREDGRTVIVSLHQVD 213
Cdd:TIGR01271 1351 GYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK--QSFSNCTVILSEHRVE 1413
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-240 |
1.16e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGriVSDIRSIRSqvgfvfqqfnLVD 98
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGR---IMIDDCDVAKFG--LTDLRRVLS----------IIP 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 RLPVLTNVLVgRLHTMPwlrgvmgwFNAQERSAALAALERVGILDCHKQR-----------ASTLSGGQQQRAAIARTLV 167
Cdd:PLN03232 1317 QSPVLFSGTV-RFNIDP--------FSEHNDADLWEALERAHIKDVIDRNpfgldaevsegGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 168 QGAKLVLADEPIASLDpdssrkvMEILSTIQ---REDGR--TVIVSLHQVDMAIRyCPRVIALNQGQVI-YDGPAAALT 240
Cdd:PLN03232 1388 RRSKILVLDEATASVD-------VRTDSLIQrtiREEFKscTMLVIAHRLNTIID-CDKILVLSSGQVLeYDSPQELLS 1458
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-58 |
1.54e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 1.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 1 MALRIQNLNKHFANGKhALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAG 58
Cdd:PRK15064 318 NALEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-230 |
2.07e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 20 RDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqregRIVSDIRSIRSQVGFVF-----QQF 94
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGR---IMLNGK------EINALSTAQRLARGLVYlpedrQSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 95 NLVDRLPVLTNVLVGRLHTMP-WLRGvmgwfnAQERsaalAALER----VGILDCHK-QRASTLSGGQQQRAAIARTLVQ 168
Cdd:PRK15439 351 GLYLDAPLAWNVCALTHNRRGfWIKP------AREN----AVLERyrraLNIKFNHAeQAARTLSGGNQQKVLIAKCLEA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518255160 169 GAKLVLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-183 |
4.13e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 6 QNLNKHFaNGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVnGQCVqregrivsdirsirs 85
Cdd:PRK11819 328 ENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT---IKI-GETV--------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 86 QVGFVFQQF-NLVDRLPV-------LTNVLVGRlHTMPwLRGVMGWFN----AQErsaalaalervgildchkQRASTLS 153
Cdd:PRK11819 388 KLAYVDQSRdALDPNKTVweeisggLDIIKVGN-REIP-SRAYVGRFNfkggDQQ------------------KKVGVLS 447
|
170 180 190
....*....|....*....|....*....|
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLD 183
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-198 |
4.73e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 20 RDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGpgslievngqcvqregrivSDIRSIRSQVGfVFQQFNlVDR 99
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG-------------------TVFRSAKVRMA-VFSQHH-VDG 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 100 LPVLTNVLVGRLHTMPwlrGVMgwfnAQERSAALAALERVGILDChkQRASTLSGGQQQRAAIARTLVQGAKLVLADEPI 179
Cdd:PLN03073 585 LDLSSNPLLYMMRCFP---GVP----EQKLRAHLGSFGVTGNLAL--QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170
....*....|....*....
gi 518255160 180 ASLDPDSSRKVMEILSTIQ 198
Cdd:PLN03073 656 NHLDLDAVEALIQGLVLFQ 674
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-245 |
4.79e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 22 IDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVqregRIVSDIRSIRSqvGFVF-----QQFNL 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQ---VYLDGKPI----DIRSPRDAIRA--GIMLcpedrKAEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 97 VDRLPVLTNVLVG-RLHTMPWlrgvmGWF--NAQERSAALAALERVGI-LDCHKQRASTLSGGQQQRAAIARTLVQGAKL 172
Cdd:PRK11288 343 IPVHSVADNINISaRRHHLRA-----GCLinNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 173 VLADEPIASLDPDSSRKVMEILSTIQrEDGRTVIV---SLHQVdMAIryCPRVIALNQGQVIYD------GPAAALTPAL 243
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFvssDLPEV-LGV--ADRIVVMREGRIAGElareqaTERQALSLAL 493
|
..
gi 518255160 244 LR 245
Cdd:PRK11288 494 PR 495
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-216 |
6.58e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 28 DGEMVALIGASGSGKSTLLRMVAGLLVADAG----PGSLIEV----NGQCVQ------REGrivsDIRSIRSQvgfvfqQ 93
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeEPSWDEVlkrfRGTELQnyfkklYNG----EIKVVHKP------Q 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 94 FnlVDRLPVLTNVLVGRLhtmpwLRGVmgwfnaQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLV 173
Cdd:PRK13409 168 Y--VDLIPKVFKGKVREL-----LKKV------DERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518255160 174 LADEPIASLDpdsSRKVMEILSTIQRE-DGRTVIVSLHqvDMAI 216
Cdd:PRK13409 235 FFDEPTSYLD---IRQRLNVARLIRELaEGKYVLVVEH--DLAV 273
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-240 |
1.26e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.44 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANGKHALR--DIDLNIADGEMVALIGASGSGKSTLLRMVAGllvadAGPGSL---IEVNGQCVQregrIV 77
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALFG-----AYPGKFegnVFINGKPVD----IR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 78 SDIRSIRSQVGFVFQQFNLVDRLPVLTnvlVGRLHTMPWLR---GVMGWFNAQERSAALAALERVGILDCHKQRAST-LS 153
Cdd:TIGR02633 329 NPAQAIRAGIAMVPEDRKRHGIVPILG---VGKNITLSVLKsfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGrLS 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREdGRTVIVSLHQVDMAIRYCPRVIALNQGQVIYD 233
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
....*..
gi 518255160 234 GPAAALT 240
Cdd:TIGR02633 485 FVNHALT 491
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-211 |
2.31e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLnKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGllvadaGPGSLIeVNGQCVQREGRIVSDIRS 82
Cdd:CHL00131 8 LEIKNL-HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG------HPAYKI-LEGDILFKGESILDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGfVFQQFNLVDRLPVLTNvlvgrlhtMPWLRGVmgwFNAQERSAALAALERVG-------ILDCHKQRASTL--- 152
Cdd:CHL00131 80 ERAHLG-IFLAFQYPIEIPGVSN--------ADFLRLA---YNSKRKFQGLPELDPLEfleiineKLKLVGMDPSFLsrn 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518255160 153 -----SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQ 211
Cdd:CHL00131 148 vnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
140-258 |
2.54e-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: 46.80 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 140 GILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYC 219
Cdd:cd03222 60 GITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLS 139
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 518255160 220 PRVIalnqgqVIYDGPAA---ALTPALLRDlyGMqaDEFLSG 258
Cdd:cd03222 140 DRIH------VFEGEPGVygiASQPKGTRE--GI--NRFLRG 171
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-208 |
3.29e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 5 IQNLNKHFAnGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGP---GSLIEVNgqcvqregrivsdir 81
Cdd:PRK11147 322 MENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihcGTKLEVA--------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 sirsqvgfVFQQF--NLVDRLPVLTNVLVGRLHTMpwlrgvmgwFNAQERSaALAALErvgilD--CHKQRAST----LS 153
Cdd:PRK11147 386 --------YFDQHraELDPEKTVMDNLAEGKQEVM---------VNGRPRH-VLGYLQ-----DflFHPKRAMTpvkaLS 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 154 GGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQredGRTVIVS 208
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQ---GTVLLVS 494
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-198 |
3.97e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHfaNGKHalrDIDLniaDGEMVALIGASGSGKSTLL---------------RMVAGLLVADAGPGSL---IE 64
Cdd:COG0419 5 LRLENFRSY--RDTE---TIDF---DDGLNLIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVGSEEASVeleFE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 65 VNGQCVQ---REGRIVSDIRSIRSQVGFVFQQF-------NLVDRLPVLTNVLVGRLHTMPWLRGVmgwfnAQERSAALA 134
Cdd:COG0419 77 HGGKRYRierRQGEFAEFLEAKPSERKEALKRLlgleiyeELKERLKELEEALESALEELAELQKL-----KQEILAQLS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518255160 135 ALERVgildchkqraSTLSGGQQQRAAIARTLvqgaKLVLaDepIASLDPDSSRKVMEILSTIQ 198
Cdd:COG0419 152 GLDPI----------ETLSGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDALEELA 198
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
16-213 |
7.88e-06 |
|
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: 46.93 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLL-----RMVAGLLV-ADAGPGS------------LIEVNGQCVQREGR-- 75
Cdd:TIGR00630 621 ENNLKNITVSIPLGLFTCITGVSGSGKSTLIndtlyPALANRLNgAKTVPGRytsieglehldkVIHIDQSPIGRTPRsn 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 76 ------IVSDIRSIRSQV------GFVFQQFNLvdrlpvltNVLVGRLH----------TMPWLRGV------------- 120
Cdd:TIGR00630 701 patytgVFDEIRELFAETpeakvrGYTPGRFSF--------NVKGGRCEacqgdgvikiEMHFLPDVyvpcevckgkryn 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 121 ------------------MGWFNAQERSAALAALER-------VGiLDCHK--QRASTLSGGQQQRAAIARTL---VQGA 170
Cdd:TIGR00630 773 retlevkykgkniadvldMTVEEAYEFFEAVPSISRklqtlcdVG-LGYIRlgQPATTLSGGEAQRIKLAKELskrSTGR 851
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 518255160 171 KLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVD 213
Cdd:TIGR00630 852 TLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLD 893
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
148-234 |
1.02e-05 |
|
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: 46.54 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 148 RASTLSGGQQQRAAIARTLvqGAKLV----LADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMaIRYCPRVI 223
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDT-IRAADYVI 560
|
90
....*....|.
gi 518255160 224 ALNQGQVIYDG 234
Cdd:TIGR00630 561 DIGPGAGEHGG 571
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-186 |
1.96e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 6 QNLNKHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLlvaDAgpgsliEVNGqcvqrEGRIVSDIRsirs 85
Cdd:PRK11819 10 NRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DK------EFEG-----EARPAPGIK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 86 qVGFVFQQFNLVDRLPVLTNVLVGrlhtMPWLRGVMGWFNaqERSAALAA--------LERVG----ILDCHK------- 146
Cdd:PRK11819 72 -VGYLPQEPQLDPEKTVRENVEEG----VAEVKAALDRFN--EIYAAYAEpdadfdalAAEQGelqeIIDAADawdldsq 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518255160 147 -QRA-------------STLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDS 186
Cdd:PRK11819 145 lEIAmdalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-230 |
2.91e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 17 HALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQcvqregrivSDIRSIRSqvgfvfqqfNL 96
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT---VDIKGS---------AALIAISS---------GL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 97 VDRLPVLTNVlvgrlhtmpWLRGV-MGWFNAQERSAALAALERVGILDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLA 175
Cdd:PRK13545 97 NGQLTGIENI---------ELKGLmMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518255160 176 DEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDMAIRYCPRVIALNQGQV 230
Cdd:PRK13545 168 DEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
16-218 |
3.17e-05 |
|
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: 43.50 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLLRMVaGLLVADAGPGSLIEVNGQCvqregrivsdirsiRSQVGFVfqqfn 95
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI-GLALGGAQSATRRRSGVKA--------------GCIVAAV----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 lvdrlpvltnvlvgrlhtmpwlrgvmgwfnaqersaalaALERVGILDChkqrastLSGGQQQRAAIARTL----VQGAK 171
Cdd:cd03227 68 ---------------------------------------SAELIFTRLQ-------LSGGEKELSALALILalasLKPRP 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518255160 172 LVLADEPIASLDPDSSRKVMEILSTiQREDGRTVIVSLHQVDMAIRY 218
Cdd:cd03227 102 LYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAELA 147
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-234 |
3.38e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHfANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGllvadagpGSLIEVNGQCVQREGRIVSDIRS 82
Cdd:PRK09580 2 LSIKDLHVS-VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--------REDYEVTGGTVEFKGKDLLELSP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 IRSQVGFVFQQFNLVDRLPVLTNVLVgrLHTMpwlrgvmgwFNAQERSAALAALERVGILDCHKQRASTL---------- 152
Cdd:PRK09580 73 EDRAGEGIFMAFQYPVEIPGVSNQFF--LQTA---------LNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 -----SGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMAIRYCPRVIALNQ 227
Cdd:PRK09580 142 vnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQ 221
|
....*..
gi 518255160 228 GQVIYDG 234
Cdd:PRK09580 222 GRIVKSG 228
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
3-211 |
9.15e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNkhFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQregrivsdirs 82
Cdd:PRK13541 2 LSLHQLQ--FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 83 iRSQVGFVFQQFNLVDRLPVLTNVLVgrlhtmpwlrgvmgWFNAQERSAAL-AALERVGILDCHKQRASTLSGGQQQRAA 161
Cdd:PRK13541 69 -KPYCTYIGHNLGLKLEMTVFENLKF--------------WSEIYNSAETLyAAIHYFKLHDLLDEKCYSLSSGMQKIVA 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518255160 162 IARTLVQGAKLVLADEPIASLDPDsSRKVMEILSTIQREDGRTVIVSLHQ 211
Cdd:PRK13541 134 IARLIACQSDLWLLDEVETNLSKE-NRDLLNNLIVMKANSGGIVLLSSHL 182
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
10-68 |
2.46e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 2.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 10 KHFANGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQ 68
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK---VDRNGE 86
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-68 |
3.76e-04 |
|
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: 40.05 E-value: 3.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 518255160 29 GEMVALIGASGSGKSTLLRMVAGLLVADAGPgsLIEVNGQ 68
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGE 39
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
152-235 |
4.83e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 152 LSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQ-VDMAIRYCPRVIALNQGQV 230
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpAPETFDLFDDIILLSEGQI 416
|
....*
gi 518255160 231 IYDGP 235
Cdd:PLN03140 417 VYQGP 421
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-213 |
5.62e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 14 NGKHALRDIDLNIADGEMVALIGASGSGKSTLLRMVAGllvaDAGPGSLIEVNGQCVQR-EGRIVSDIRSirsQVGFVFQ 92
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQGYSNDLTLFGRRRgSGETIWDIKK---HIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 93 QFNLVDRlpVLTNVlvgrlhtmpwlRGVM--GWFNA---------QERSAALAALERVGILDC-HKQRASTLSGGQQQRA 160
Cdd:PRK10938 344 SLHLDYR--VSTSV-----------RNVIlsGFFDSigiyqavsdRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLA 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518255160 161 AIARTLVQGAKLVLADEPIASLDPDSS---RKVMEILSTiqreDGRT--VIVSLHQVD 213
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLIS----EGETqlLFVSHHAED 464
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
4-55 |
7.83e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 7.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 518255160 4 RIQNLNKHFANGKhalrdiDLNIADGEMVALIGASGSGKSTLLRMVAGLLVA 55
Cdd:pfam13555 3 RLQLINWGTFDGH------TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-240 |
8.32e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPgslIEVNGQCVQREGrivsdIRSIRSQVGFVFQQfnlvd 98
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGR---ILIDGCDISKFG-----LMDLRKVLGIIPQA----- 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 99 rlPVLTNVLVgRLHTMPwlrgvmgwFNAQERSAALAALERVGILDCHKQRASTL-----------SGGQQQRAAIARTLV 167
Cdd:PLN03130 1322 --PVLFSGTV-RFNLDP--------FNEHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518255160 168 QGAKLVLADEPIASLDpdsSRKVMEILSTIqREDGR--TVIVSLHQVDMAIRyCPRVIALNQGQVI-YDGPAAALT 240
Cdd:PLN03130 1391 RRSKILVLDEATAAVD---VRTDALIQKTI-REEFKscTMLIIAHRLNTIID-CDRILVLDAGRVVeFDTPENLLS 1461
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-210 |
1.23e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 28 DGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLIEVNGQCVQREGrivsdirSIRSQVGFVFQQFN-----LVDRLPV 102
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIREG-------EVRAQVKLAFENANgkkytITRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 103 LTNVLvgrlhtmpwlrgvmgwFNAQERSAALAALERVgildchkqrasTLSGGQQQ------RAAIARTLvqGAKL-VLA 175
Cdd:cd03240 94 LENVI----------------FCHQGESNWPLLDMRG-----------RCSGGEKVlasliiRLALAETF--GSNCgILA 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 518255160 176 -DEPIASLDPDSSRKVM-EILSTIQREDGRTVIVSLH 210
Cdd:cd03240 145 lDEPTTNLDEENIEESLaEIIEERKSQKNFQLIVITH 181
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-45 |
1.43e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 1.43e-03
10 20
....*....|....*....|....*....
gi 518255160 17 HALRDIDLNIADGEMVALIGASGSGKSTL 45
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-208 |
1.97e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 19 LRDIDLNIADGEMVALIGASGSGKSTLLRMVAGLLVADAGPGSLievngqcvqregrivsdIRSIRsqVGFVFQ---QFN 95
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------------AKGIK--LGYFAQhqlEFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 96 LVDRLPVLTNVLVGRLHTMPWLRGVMGWFNAQErsaalaalervgilDCHKQRASTLSGGQQQRAAIARTLVQGAKLVLA 175
Cdd:PRK10636 389 RADESPLQHLARLAPQELEQKLRDYLGGFGFQG--------------DKVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190
....*....|....*....|....*....|...
gi 518255160 176 DEPIASLDPDSSRKVMEILSTIqreDGRTVIVS 208
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEALIDF---EGALVVVS 484
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
18-76 |
2.01e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.14 E-value: 2.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 518255160 18 ALRDIDLNIadGEMVALIGASGSGKSTLLRmvAGLLVADAGPGSLIEVngqcVQREGRI 76
Cdd:COG4637 12 SLRDLELPL--GPLTVLIGANGSGKSNLLD--ALRFLSDAARGGLQDA----LARRGGL 62
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-45 |
2.23e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 2.23e-03
10 20
....*....|....*....|....*....
gi 518255160 17 HALRDIDLNIADGEMVALIGASGSGKSTL 45
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
16-46 |
2.44e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 2.44e-03
10 20 30
....*....|....*....|....*....|.
gi 518255160 16 KHALRDIDLNIADGEMVALIGASGSGKSTLL 46
Cdd:PRK00349 622 ENNLKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
3-223 |
2.45e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.40 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 3 LRIQNLNKHFANgkhalRDIDLNIADGEMVALI-GASGSGKSTLLrmvagllvaDAGPGSLIevnGQcVQREGRIVSDiR 81
Cdd:cd03279 6 LELKNFGPFREE-----QVIDFTGLDNNGLFLIcGPTGAGKSTIL---------DAITYALY---GK-TPRYGRQENL-R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 82 SIRSQ------VGFVFQQFN---LVDRLPVLTNVLVGRLHTMPwlrgvmgwfnaQERSAALaaLERvgildchkqRASTL 152
Cdd:cd03279 67 SVFAPgedtaeVSFTFQLGGkkyRVERSRGLDYDQFTRIVLLP-----------QGEFDRF--LAR---------PVSTL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 153 SGGQQQRAAIARTL-----VQ---GAKL--VLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSlHQVDMAIRYCPRV 222
Cdd:cd03279 125 SGGETFLASLSLALalsevLQnrgGARLeaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVIS-HVEELKERIPQRL 203
|
.
gi 518255160 223 I 223
Cdd:cd03279 204 E 204
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-45 |
2.65e-03 |
|
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: 39.23 E-value: 2.65e-03
10 20
....*....|....*....|....*....
gi 518255160 17 HALRDIDLNIADGEMVALIGASGSGKSTL 45
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-53 |
3.41e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.06 E-value: 3.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 518255160 3 LRIQNLnKHFANgkhalRDIDLNIADGeMVALIGASGSGKSTLLRMVAGLL 53
Cdd:COG3950 6 LTIENF-RGFED-----LEIDFDNPPR-LTVLVGENGSGKTTLLEAIALAL 49
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
145-230 |
4.02e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.56 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 145 HKQRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLDPDSSRKVMEILSTIQREDGRTVIVSLHQVDMaIRYCPRVIA 224
Cdd:PRK10982 385 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPEL-LGITDRILV 463
|
....*.
gi 518255160 225 LNQGQV 230
Cdd:PRK10982 464 MSNGLV 469
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-137 |
5.90e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.95 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 34 LIGASGSGKSTLLRMVAGLLVADAGPGSLiEVNgqcvQREGRIvsdirsirSQVGFVFQQFNLVDrlpvltNVLVGrlHT 113
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSL-DPN----ERLGKL--------RQDQFAFEEFTVLD------TVIMG--HT 90
|
90 100
....*....|....*....|....
gi 518255160 114 MPWlrGVMgwfnaQERSAALAALE 137
Cdd:PRK15064 91 ELW--EVK-----QERDRIYALPE 107
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-239 |
6.95e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518255160 136 LERVGI----LDchkQRASTLSGGQQQRAAIARTLvqGAKL-----VLaDEPIASLDP-DSSRkvmeILSTIQ--REDGR 203
Cdd:COG0178 469 LVDVGLdyltLD---RSAGTLSGGEAQRIRLATQI--GSGLvgvlyVL-DEPSIGLHQrDNDR----LIETLKrlRDLGN 538
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 518255160 204 TVIVSLHQVDMaIRYCPRVIAL------NQGQVIYDGPAAAL 239
Cdd:COG0178 539 TVIVVEHDEDT-IRAADYIIDIgpgageHGGEVVAQGTPEEI 579
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
147-214 |
8.77e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 8.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518255160 147 QRASTLSGGQQQRAAIARTLVQ---GAKLVLADEPIASLDPDSSRKVMEILSTIqREDGRTVIVSLHQVDM 214
Cdd:PRK00349 826 QPATTLSGGEAQRVKLAKELSKrstGKTLYILDEPTTGLHFEDIRKLLEVLHRL-VDKGNTVVVIEHNLDV 895
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
147-183 |
9.63e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 37.29 E-value: 9.63e-03
10 20 30
....*....|....*....|....*....|....*..
gi 518255160 147 QRASTLSGGQQQRAAIARTLVQGAKLVLADEPIASLD 183
Cdd:PRK10762 391 QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| |
