|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-242 |
6.54e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.85 E-value: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAfhdtqLVCNGDLSY 93
Cdd:COG1131 1 IEVRGLTKRYGDKTAL-DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG--------LLRPTSGEV-----RVLGEDVAR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 LGGSWSRAIGS-AGDVPLQGDFSA-EHM-----IFGVDGVDPVRR-EKLVDLLDID--LQWRMHKVSDGQRRRVQICMGL 163
Cdd:COG1131 67 DPAEVRRRIGYvPQEPALYPDLTVrENLrffarLYGLPRKEARERiDELLELFGLTdaADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002242100 164 LHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQrEATIVYATHIFDGLESWATDIAYIQEGELRKSAkysDVEELKSA 242
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADG---TPDELKAR 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-245 |
1.99e-28 |
|
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: 109.18 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYdGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAfhdtqLVCNGDLSY 93
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG--------LLKPDSGSI-----LIDGEDVRK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 LGGSWSRAIGSAGD-VPLQGDFSAEHMI------FGVDGVDPVRR-EKLVDLLDID--LQWRMHKVSDGQRRRVQICMGL 163
Cdd:COG4555 68 EPREARRQIGVLPDeRGLYDRLTVRENIryfaelYGLFDEELKKRiEELIELLGLEefLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 164 LHPYKVLLLDEITVDLDVVTRMDLLDFFKeECEQREATIVYATHIFDGLESWATDIAYIQEGELRKSAKYSDVEELKSAK 243
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
..
gi 1002242100 244 NL 245
Cdd:COG4555 227 NL 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-227 |
1.25e-27 |
|
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: 105.17 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFaRFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAfhdtqLVCNGDLSY 93
Cdd:cd03230 1 IEVRNLSKRYGKKTALD-DISLTVEKGEIYGLLGPNGAGKTTLIKIILG--------LLKPDSGEI-----KVLGKDIKK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 LGGSWSRAIGSA-GDVPLQGDFSAEHMIfgvdgvdpvrreklvdlldidlqwrmhKVSDGQRRRVQICMGLLHPYKVLLL 172
Cdd:cd03230 67 EPEEVKRRIGYLpEEPSLYENLTVRENL---------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002242100 173 DEITVDLDVVTRMDLLDFFKEECeQREATIVYATHIFDGLESWATDIAYIQEGEL 227
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-226 |
1.33e-26 |
|
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: 103.32 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 15 EVSALQFDY-DGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGsafhdTQLVCNGDLSY 93
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNG--------LLGPTSG-----EVLVDGKDLTK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 LG-GSWSRAIGSAgdvpLQgdfSAEHMIFGVD------------GVDPVRREKLVD----LLDID--LQWRMHKVSDGQR 154
Cdd:cd03225 68 LSlKELRRKVGLV----FQ---NPDDQFFGPTveeevafglenlGLPEEEIEERVEealeLVGLEglRDRSPFTLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 155 RRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReATIVYATHIFDGLESWATDIAYIQEGE 226
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-241 |
4.49e-25 |
|
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: 99.71 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG--KHM-----VGGRDVVRvLNGSAFH----- 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKPTsgevlVDGKDITK-KNLRELRrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 82 -----DTQLVCN---GDLSylggswsraigsagdvplqgdFSAEHMifgvdGVDPVRREKLVD----LLDI-DLQWR-MH 147
Cdd:COG1122 80 vfqnpDDQLFAPtveEDVA---------------------FGPENL-----GLPREEIRERVEealeLVGLeHLADRpPH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 148 KVSDGQRRRVQICmGLL--HPyKVLLLDEITVDLDVVTRMDLLDFFKeECEQREATIVYATHIFDGLESWATDIAYIQEG 225
Cdd:COG1122 134 ELSGGQKQRVAIA-GVLamEP-EVLVLDEPTAGLDPRGRRELLELLK-RLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
250 260
....*....|....*....|
gi 1002242100 226 ELRKSAK----YSDVEELKS 241
Cdd:COG1122 211 RIVADGTprevFSDYELLEE 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
14-207 |
7.31e-25 |
|
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: 98.71 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG-KHMVGGRdvVRvLNGSAFHDTQLVCNGDLS 92
Cdd:COG4133 3 LEAENLSCRRGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGlLPPSAGE--VL-WNGEPIRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 YLGgswsraigsaGDVPLQGDFSA-EHMIF--GVDGVdPVRREKLVDLLD-IDLQWRMHK----VSDGQRRRVQICMGLL 164
Cdd:COG4133 79 YLG----------HADGLKPELTVrENLRFwaALYGL-RADREAIDEALEaVGLAGLADLpvrqLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1002242100 165 HPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReATIVYATH 207
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARG-GAVLLTTH 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
34-227 |
2.41e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 95.48 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGK-HMVGGRdvVRVLNGSAFHD-TQLVCNgdLSYLGGSWSRAIGsagDVPLQ 111
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLlQPTSGE--VRVAGLVPWKRrKKFLRR--IGVVFGQKTQLWW---DLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 112 GDFSAEHMIFGVDGVD-PVRREKLVDLLDID--LQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLL 188
Cdd:cd03267 114 DSFYLLAAIYDLPPARfKKRLDELSELLDLEelLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002242100 189 DFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGEL 227
Cdd:cd03267 194 NFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-240 |
2.59e-22 |
|
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: 92.43 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRvlngsafhDTQLV 86
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTtllkptsGRATVAGHDVVR--------EPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 87 cngdlsylggswSRAIGSAG-DVPLQGDFSA-EHM-----IFGVDGvdPVRREKLVDLLD-IDLQWRMHKV----SDGQR 154
Cdd:cd03265 72 ------------RRRIGIVFqDLSVDDELTGwENLyiharLYGVPG--AERRERIDELLDfVGLLEAADRLvktySGGMR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 155 RRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGELRKSAKys 234
Cdd:cd03265 138 RRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGT-- 215
|
....*.
gi 1002242100 235 dVEELK 240
Cdd:cd03265 216 -PEELK 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-226 |
2.62e-22 |
|
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: 90.38 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 15 EVSALQFDYdGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVCNGDLSyl 94
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG--------LLKPTSGEILIDGKDIAKLPLE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 95 ggSWSRAIGsagdvplqgdfsaehMIFGVdgvdpvrreklvdlldidlqwrmhkvSDGQRRRVQICMGLLHPYKVLLLDE 174
Cdd:cd00267 70 --ELRRRIG---------------YVPQL--------------------------SGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 175 ITVDLDVVTRMDLLDFFKEECeQREATIVYATHIFDGLESWATDIAYIQEGE 226
Cdd:cd00267 107 PTSGLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
14-207 |
8.48e-21 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.99 E-value: 8.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHMVGGRDVVRVLngsafhDTQLvcngdlsy 93
Cdd:COG1119 4 LELRNVTVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLF------GERR-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 lgGSWS-----RAIG---SAGDVPLQGDFSAEHMI----FGVDG----VDPVRREKLVDLLDI----DL-QWRMHKVSDG 152
Cdd:COG1119 69 --GGEDvwelrKRIGlvsPALQLRFPRDETVLDVVlsgfFDSIGlyrePTDEQRERARELLELlglaHLaDRPFGTLSQG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002242100 153 QRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
34-227 |
9.37e-20 |
|
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: 85.23 E-value: 9.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRvLNGSA------------FHDTQLvcngdLSYL 94
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGgldrptsGEVRVDGTDISK-LSEKElaafrrrhigfvFQSFNL-----LPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 95 ggswsraigSAGD---VPLqgdfsaehMIFGVDGVDpvRREKLVDLLD-IDLQWRMHK----VSDGQRRRVQICMGLLHP 166
Cdd:cd03255 98 ---------TALEnveLPL--------LLAGVPKKE--RRERAEELLErVGLGDRLNHypseLSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002242100 167 YKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDgLESWATDIAYIQEGEL 227
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
32-228 |
1.61e-19 |
|
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: 84.86 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 32 RFNLRIAPGSrCL-LIGANGSGKTTLLKILAGKH-------MVGGRDVVRVLNgsafhdtqlVCNGDLSYlggswsraig 103
Cdd:cd03263 20 DLSLNVYKGE-IFgLLGHNGAGKTTTLKMLTGELrptsgtaYINGYSIRTDRK---------AARQSLGY---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 104 sagdVPlQGD-----FSA-EHMIF--GVDGV--DPVRREKLVDLLDIDLQ----WRMHKVSDGQRRRVQICMGLLHPYKV 169
Cdd:cd03263 80 ----CP-QFDalfdeLTVrEHLRFyaRLKGLpkSEIKEEVELLLRVLGLTdkanKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002242100 170 LLLDEITVDLDVVTRMDLLDFFKEecEQREATIVYATHIFDGLESWATDIAYIQEGELR 228
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-226 |
1.63e-19 |
|
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: 82.88 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKhmvggrdvvrvlngsafhdtqlvcngdlsy 93
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE------------------------------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 lggswsraigsagDVPLQGDFSaehmifgvdgVDPVRREKLVDLLdidlqwrmhkvSDGQRRRVQICMGLLHPYKVLLLD 173
Cdd:cd03221 50 -------------LEPDEGIVT----------WGSTVKIGYFEQL-----------SGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002242100 174 EITVDLDVVTRMDLLDFFKEEceqrEATIVYATHIFDGLESWATDIAYIQEGE 226
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEY----PGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-235 |
1.67e-19 |
|
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: 88.28 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 13 GIEVSALQFDYDGQP-PLFARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVvrvlngsafhdtq 84
Cdd:COG4987 333 SLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrfldpqsGSITLGGVDL------------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 85 lvcngdLSYLGGSWSRAIG-SAGDVPLqgdFSA---EHMIFGVDGVDP---------VRREKLVDLLDIDLQWRMH---- 147
Cdd:COG4987 400 ------RDLDEDDLRRRIAvVPQRPHL---FDTtlrENLRLARPDATDeelwaalerVGLGDWLAALPDGLDTWLGeggr 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 148 KVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReaTIVYATHIFDGLEsWATDIAYIQEGEL 227
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLE-RMDRILVLEDGRI 547
|
....*...
gi 1002242100 228 RKSAKYSD 235
Cdd:COG4987 548 VEQGTHEE 555
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-207 |
2.15e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.29 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 9 WRRSGIEVSALQfdydgqpplfaRFNLRIAPGSRCLLIGANGSGKTTLLKILAG-KHMVGGRdvVRVLNGSAFHD----- 82
Cdd:COG4586 28 FRREYREVEAVD-----------DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPTSGE--VRVLGYVPFKRrkefa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 83 ----------TQLvcngdlsylggSWsraigsagDVPLQGDFSAEHMIFGVDgvDPV---RREKLVDLLDID--LQWRMH 147
Cdd:COG4586 95 rrigvvfgqrSQL-----------WW--------DLPAIDSFRLLKAIYRIP--DAEykkRLDELVELLDLGelLDTPVR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 148 KVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSH 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-267 |
2.41e-19 |
|
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: 87.65 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDY-DGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHMVGGRdvvrvLNGSAFHDTQLVCNGDLS 92
Cdd:COG1123 5 LEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGR-----ISGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 YLGgswsRAIG------SAGDVPLQ-GDFSAEHM-IFGVDGVDpvRREKLVDLLD-IDLQWRM----HKVSDGQRRRVQI 159
Cdd:COG1123 80 LRG----RRIGmvfqdpMTQLNPVTvGDQIAEALeNLGLSRAE--ARARVLELLEaVGLERRLdrypHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 160 CMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGELRKSAKYSDVeeL 239
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI--L 231
|
250 260
....*....|....*....|....*...
gi 1002242100 240 KSAKNLLSVVESWLRSETKLPKKEHPRP 267
Cdd:COG1123 232 AAPQALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
35-228 |
3.83e-19 |
|
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: 83.57 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 35 LRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVR----------VLNGSAFHDTQLVCNGDLSYLGGS 97
Cdd:cd03266 26 FTVKPGEVTGLLGPNGAGKTTTLRMLAgllepdaGFATVDGFDVVKepaearrrlgFVSDSTGLYDRLTARENLEYFAGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 98 WsraiGSAGDVPLQgdfsaehmifgvdgvdpvRREKLVDLLDID--LQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEI 175
Cdd:cd03266 106 Y----GLKGDELTA------------------RLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002242100 176 TVDLDVVTRMDLLDFFKEECEQREaTIVYATHIFDGLESWATDIAYIQEGELR 228
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-207 |
5.68e-19 |
|
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: 83.94 E-value: 5.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQlvcngDLSy 93
Cdd:COG1120 2 LEAENLSVGYGGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG--------LLKPSSGEVLLDGR-----DLA- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 lggSWS-----RAIG------------SAGDVPLQGDFSAEHMIFGVDGVDPVRREKLVDLLDI-DLQWR-MHKVSDGQR 154
Cdd:COG1120 67 ---SLSrrelaRRIAyvpqeppapfglTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLeHLADRpVDELSGGER 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002242100 155 RRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH 196
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-207 |
1.83e-18 |
|
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: 80.94 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 15 EVSALQFDYdGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAfhdtqLVCNGDLSYL 94
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG--------LLKPSSGEI-----LLDGKDLASL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 95 GGS-WSRAIGSagdVP--LqgdfsaehmifgvdgvdpvrreKLVDLLDIDLQwRMHKVSDGQRRRVQICMGLLHPYKVLL 171
Cdd:cd03214 67 SPKeLARKIAY---VPqaL----------------------ELLGLAHLADR-PFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002242100 172 LDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLH 156
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-231 |
3.71e-18 |
|
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: 80.80 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 33 FNLRIA---PGSRCLLIGANGSGKTTLLKILAG-KHMVGGRdvvRVLNGSAFHDTQLvcNGDLSylggSWSRAIG----S 104
Cdd:cd03297 13 FTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGlEKPDGGT---IVLNGTVLFDSRK--KINLP----PQQRKIGlvfqQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 105 AGDVPLQGdfSAEHMIFGV----DGVDPVRREKLVDLLDID--LQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVD 178
Cdd:cd03297 84 YALFPHLN--VRENLAFGLkrkrNREDRISVDELLDLLGLDhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002242100 179 LDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGELRKSA 231
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-230 |
2.09e-17 |
|
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: 78.77 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFArFNLRIAPGSRCLLiGANGSGKTTLLKILA-------GKHMVGGRDVVRvlNGSAFHDTqlv 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDG-VSLTLGPGMYGLL-GPNGAGKTTLMRILAtltppssGTIRIDGQDVLK--QPQKLRRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 87 cngdLSYLggswsraigsAGDVPLQGDFSAE----HMIFgVDGVDPVRREKLVD--LLDIDLQWRMHK----VSDGQRRR 156
Cdd:cd03264 74 ----IGYL----------PQEFGVYPNFTVRefldYIAW-LKGIPSKEVKARVDevLELVNLGDRAKKkigsLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002242100 157 VQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReaTIVYATHIFDGLESWATDIAYIQEGELRKS 230
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
33-227 |
3.45e-17 |
|
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: 78.70 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 33 FNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFhdtqlVCNGDLSYLGGSWSRAIGSA-GDVPlQ 111
Cdd:cd03257 24 VSFSIKKGETLGLVGESGSGKSTLARAILG--------LLKPTSGSII-----FDGKDLLKLSRRLRKIRRKEiQMVF-Q 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 112 GDFSA------------EHMIFGVDGVDPVRREKLVDLLDID-------LQWRMHKVSDGQRRRVQICMGL-LHPyKVLL 171
Cdd:cd03257 90 DPMSSlnprmtigeqiaEPLRIHGKLSKKEARKEAVLLLLVGvglpeevLNRYPHELSGGQRQRVAIARALaLNP-KLLI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002242100 172 LDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGEL 227
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-207 |
1.64e-16 |
|
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: 79.33 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 13 GIEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHMVGGRDVvrVLNGSAFHdtqlvcngdlS 92
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV--TLDGVPVS----------S 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 YLGGSWSRAIG-SAGDVPL------------QGDFSAEHMIFGVDGV---DPVRRekLVDLLDIDLQWRMHKVSDGQRRR 156
Cdd:TIGR02868 402 LDQDEVRRRVSvCAQDAHLfdttvrenlrlaRPDATDEELWAALERVglaDWLRA--LPDGLDTVLGEGGARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 157 VQICMGLLHPYKVLLLDEITVDLDVVTRMDLL-DFFKEEceqREATIVYATH 207
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLeDLLAAL---SGRTVVLITH 528
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-207 |
2.32e-16 |
|
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: 78.87 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 12 SGIEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkHMVGGRDVVRVlNGSAFHDtqlvcnGDL 91
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG-FVDPTEGSIAV-NGVPLAD------ADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 92 SylggSWSRAIGSAGDVPL-------------QGDFSAEHMI-----FGVDGVDPVRREKLVDLLDIDlqwrMHKVSDGQ 153
Cdd:TIGR02857 392 D----SWRDQIAWVPQHPFlfagtiaenirlaRPDASDAEIRealerAGLDEFVAALPQGLDTPIGEG----GAGLSGGQ 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002242100 154 RRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReaTIVYATH 207
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTH 515
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
14-227 |
3.54e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.85 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDY-DGQPPLFA--RFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVvrvlngSAFHDT 83
Cdd:COG1136 5 LELRNLTKSYgTGEGEVTAlrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGgldrptsGEVLIDGQDI------SSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 84 QLVcngDLsylggsWSRAIG----SAGDVPlqgDFSAE------HMIFGVDGVDpvRREKLVDLLD-IDLQWRMHK---- 148
Cdd:COG1136 79 ELA---RL------RRRHIGfvfqFFNLLP---ELTALenvalpLLLAGVSRKE--RRERARELLErVGLGDRLDHrpsq 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 149 VSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHifD-GLESWATDIAYIQEGEL 227
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH--DpELAARADRVIRLRDGRI 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
34-177 |
4.88e-16 |
|
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: 73.45 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKHM-VGGRDvvrVLNGSAFHDTQLvcngdlsylgGSWSRAIGSAG-DVPLQ 111
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTI---LLDGQDLTDDER----------KSLRKEIGYVFqDPQLF 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002242100 112 GDFSA-EHMIFGVDGVDPVRREK------------LVDLLDIDLQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITV 177
Cdd:pfam00005 72 PRLTVrENLRLGLLLKGLSKREKdaraeealeklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-245 |
5.47e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 75.51 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFaRFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSafhdtqlvcngdLSY 93
Cdd:COG1121 7 IELENLTVSYGGRPVLE-DVSLTIPPGEFVAIVGPNGAGKSTLLKAILG--------LLPPTSGT------------VRL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 LGGSWSRAIGSAGDVPLQGDFSAE---------------HM-IFGvdGVDPVRREK------LVDLLDIdLQWRMHKVSD 151
Cdd:COG1121 66 FGKPPRRARRRIGYVPQRAEVDWDfpitvrdvvlmgrygRRgLFR--RPSRADREAvdealeRVGLEDL-ADRPIGELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 152 GQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECeQREATIVYATHIFDGLESWATDIAYIQEGELRksa 231
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRGLVA--- 218
|
250
....*....|....
gi 1002242100 232 kYSDVEELKSAKNL 245
Cdd:COG1121 219 -HGPPEEVLTPENL 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-207 |
1.04e-15 |
|
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: 73.19 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQP-PLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVCNGDLS 92
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR--------LYDPTSGEILIDGVDLRDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 ylggSWSRAIGSagdVPlQGDFsaehmIFGvdgvDPVrREKLvdlldidlqwrmhkVSDGQRRRVQICMGLLHPYKVLLL 172
Cdd:cd03228 73 ----SLRKNIAY---VP-QDPF-----LFS----GTI-RENI--------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 1002242100 173 DEITVDLDVVTRMDLLDFFKEECEQReaTIVYATH 207
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGK--TVIVIAH 153
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-207 |
2.17e-15 |
|
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: 73.32 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRVlngsafhdtqlv 86
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAglerpdsGEILIDGRDVTGV------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 87 cngdlsylgGSWSRAIGsagdVPLQgDFS-------AEHMIFGVD--GVD-PVRREK---LVDLLDID--LQWRMHKVSD 151
Cdd:cd03259 68 ---------PPERRNIG----MVFQ-DYAlfphltvAENIAFGLKlrGVPkAEIRARvreLLELVGLEglLNRYPHELSG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002242100 152 GQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:cd03259 134 GQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTH 189
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-207 |
3.11e-15 |
|
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: 75.64 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQ-PPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdvvrvlngsaFHDTQ----LVCN 88
Cdd:COG2274 474 IELENVSFRYPGDsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG-----------------LYEPTsgriLIDG 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 89 GDLSYLG-GSWSRAIGsagdVPLQGD--FS---AEHMIFGVDGVDpvrREKLVDLLDI-----DLQwRM-----HKVSD- 151
Cdd:COG2274 537 IDLRQIDpASLRRQIG----VVLQDVflFSgtiRENITLGDPDAT---DEEIIEAARLaglhdFIE-ALpmgydTVVGEg 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 152 ------GQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReaTIVYATH 207
Cdd:COG2274 609 gsnlsgGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAH 668
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-207 |
4.38e-15 |
|
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: 75.18 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 10 RRSGIEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKH-------MVGGRDVvrvlngSAFHD 82
Cdd:COG4988 333 GPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLppysgsiLINGVDL------SDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 83 TQLvcNGDLSYLG-------GSWsR---AIGSAgdvplqgDFSAEHMI-----FGVDGVdpVRRekLVDLLDIDLQWRMH 147
Cdd:COG4988 407 ASW--RRQIAWVPqnpylfaGTI-RenlRLGRP-------DASDEELEaaleaAGLDEF--VAA--LPDGLDTPLGEGGR 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 148 KVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReaTIVYATH 207
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITH 530
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-228 |
4.62e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 10 RRSG---IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKhmvggrdvVRVLNGSAFHDTQLV 86
Cdd:COG0488 309 ERLGkkvLELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE--------LEPDSGTVKLGETVK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 87 cngdLSYLggSWSRAIgsagdvpLQGDFSA-EHMifgVDGVDPVRREKLVDLL-------DiDLQWRMHKVSDGQRRRVQ 158
Cdd:COG0488 380 ----IGYF--DQHQEE-------LDPDKTVlDEL---RDGAPGGTEQEVRGYLgrflfsgD-DAFKPVGVLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002242100 159 ICMGLLHPYKVLLLDEITVDLDVVTR---MDLLDFFkeeceqrEATIVYATH--IFdgLESWATDIAYIQEGELR 228
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLealEEALDDF-------PGTVLLVSHdrYF--LDRVATRILEFEDGGVR 508
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-207 |
9.90e-15 |
|
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: 71.41 E-value: 9.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 15 EVSALQFDYDGQPPLFArFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdvvrvlngsafhdtqLV--CNGDLS 92
Cdd:cd03235 1 EVEDLTVSYGGHPVLED-VSFEVKPGEFLAIVGPNGAGKSTLLKAILG----------------------LLkpTSGSIR 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 YLGGSWSRAIGSAGDVPLQGDFSAE---------------HMIFGVDGVDPVRRE-----KLVDLLDIdLQWRMHKVSDG 152
Cdd:cd03235 58 VFGKPLEKERKRIGYVPQRRSIDRDfpisvrdvvlmglygHKGLFRRLSKADKAKvdealERVGLSEL-ADRQIGELSGG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002242100 153 QRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECeQREATIVYATH 207
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTH 190
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
23-207 |
2.29e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 70.47 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 23 YDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRvLNGSafhdtqlvcngDLSYLg 95
Cdd:COG2884 11 YPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYgeerptsGQVLVNGQDLSR-LKRR-----------EIPYL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 96 gswSRAIGsagdVPLQgDFS-------AEHMIFG--VDGVDPVRREKLV-DLLD-IDLQWRMHK----VSDGQRRRVQIC 160
Cdd:COG2884 78 ---RRRIG----VVFQ-DFRllpdrtvYENVALPlrVTGKSRKEIRRRVrEVLDlVGLSDKAKAlpheLSGGEQQRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002242100 161 MGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECeQREATIVYATH 207
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATH 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
25-240 |
1.05e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 25 GQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVcngdLSYLggswsraigs 104
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG--------ELEPDSGEVSIPKGLR----IGYL---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 105 AGDVPLQGDFSAEHMIFGVDG--------------------VDPVRREKLVDLLD----------------------IDL 142
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLDGDAelraleaeleeleaklaepdEDLERLAELQEEFEalggweaearaeeilsglgfpeEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 143 QWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKeeceQREATIVYATH--IFdgLESWATDIA 220
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLK----NYPGTVLVVSHdrYF--LDRVATRIL 220
|
250 260
....*....|....*....|.
gi 1002242100 221 YIQEGELRK-SAKYSDVEELK 240
Cdd:COG0488 221 ELDRGKLTLyPGNYSAYLEQR 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-207 |
1.21e-13 |
|
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: 70.70 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFAR----FNLRIAPGSRCLLIGANGSGKTTLLKILAGKH-------MVGGRDVVRvLNGSAFHD 82
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRavddVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrptsgsiLFDGKDLTK-LSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 83 tqlvcngdlsylggsWSRAIG--------------SAGDV---PL--QGDFSAEHmifgvdgvdpvRREKLVDLLDI--- 140
Cdd:COG1123 340 ---------------LRRRVQmvfqdpysslnprmTVGDIiaePLrlHGLLSRAE-----------RRERVAELLERvgl 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002242100 141 ---DLQWRMHKVSDGQRRRVQICMGL-LHPyKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:COG1123 394 ppdLADRYPHELSGGQRQRVAIARALaLEP-KLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH 463
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-226 |
1.80e-13 |
|
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: 67.21 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFArFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVcnGDLSY 93
Cdd:cd03229 1 LELKNVSKRYGQKTVLND-VSLNIEAGEIVALLGPSGSGKSTLLRCIAG--------LEEPDSGSILIDGEDL--TDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 LGGSWSRAIGsagdvplqgdfsaehMIFgvdgvdpvRREKLVDLLDIdLQWRMHKVSDGQRRRVQICMGLLHPYKVLLLD 173
Cdd:cd03229 70 ELPPLRRRIG---------------MVF--------QDFALFPHLTV-LENIALGLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002242100 174 EITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGE 226
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
13-236 |
1.86e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.00 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 13 GIEVSALQFDYDGQPPLFAR----FNLRIAPGSRCLLIGANGSGKTTLLKILAGKHmVGGRDVVRVlngsafhDTQLVCN 88
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEGRalfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-VPTQGSVRV-------DDTLITS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 89 GDLSYLGGSWSRAIGSAGDVPLQGDFsAEHMI---------FGVDGVDPVR--REKLVdLLDIDLQWRMH---KVSDGQR 154
Cdd:PRK13649 74 TSKNKDIKQIRKKVGLVFQFPESQLF-EETVLkdvafgpqnFGVSQEEAEAlaREKLA-LVGISESLFEKnpfELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 155 RRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKeECEQREATIVYATHIFDGLESWATDIAYIQEGELRKSAKYS 234
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFK-KLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
..
gi 1002242100 235 DV 236
Cdd:PRK13649 231 DI 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-207 |
3.20e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.87 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 23 YDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILAG--KHMVG------GRDVVRVLNGSAFHDTQLVCNGDLSYL 94
Cdd:NF040873 2 YGGRPVL-HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvlRPTSGtvrragGARVAYVPQRSEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 95 G-----GSWSRaigsagdvplqgdfsaehmifgVDGVDPVRREKLVDLLDI-DLQWR-MHKVSDGQRRRVQICMGLLHPY 167
Cdd:NF040873 81 GrwarrGLWRR----------------------LTRDDRAAVDDALERVGLaDLAGRqLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002242100 168 KVLLLDEITVDLDVVTRMDLLDFFKEECEqREATIVYATH 207
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTH 177
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-227 |
5.47e-13 |
|
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: 66.94 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDVVRVlngsafhdtqlv 86
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrlieptSGEIFIDGEDIREQ------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 87 cngDLSYLGGSWSRAIGSAGDVPlqgdfsaeHM--------IFGVDGVDPVRRE-------KLVDLLDIDLQWRM-HKVS 150
Cdd:cd03295 69 ---DPVELRRKIGYVIQQIGLFP--------HMtveenialVPKLLKWPKEKIReradellALVGLDPAEFADRYpHELS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002242100 151 DGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGEL 227
Cdd:cd03295 138 GGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-207 |
7.06e-13 |
|
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: 66.34 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDY---DGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKH-------MVGGRDVVRVLNGSAF--- 80
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLErptsgevLVDGEPVTGPGPDRGYvfq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 81 HDTQLvcngdlsylggSWSRAIGSAgdvplqgdfsaehmIFGVDGVDPVRRE---------KLVDLLDIdLQWRMHKVSD 151
Cdd:cd03293 81 QDALL-----------PWLTVLDNV--------------ALGLELQGVPKAEareraeellELVGLSGF-ENAYPHQLSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002242100 152 GQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:cd03293 135 GMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTH 190
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-231 |
1.52e-12 |
|
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: 65.32 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILAG-KHMVGGRdvVRVLNGSAFHDTqlvcngdls 92
Cdd:cd03268 1 LKTNDLTKTYGKKRVL-DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPDSGE--ITFDGKSYQKNI--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 ylgGSWSRaIGSAGDVP-LQGDFSAEHMiFGVDGVDPVRREKLVD-LLDI-DLQWRMHK----VSDGQRRRVQICMGLLH 165
Cdd:cd03268 69 ---EALRR-IGALIEAPgFYPNLTAREN-LRLLARLLGIRKKRIDeVLDVvGLKDSAKKkvkgFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002242100 166 PYKVLLLDEITVDLDVVTRMDLLDFFKEECEQrEATIVYATHIFDGLESWATDIAYIQEGELRKSA 231
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-208 |
1.69e-12 |
|
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: 65.07 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 25 GQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG-KHMVGGRdvVRvLNGSAFHDTQlvcngdlsylgGSWSRAIG 103
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGlLRPDSGE--VR-WNGTPLAEQR-----------DEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 104 SAGDVP-LQGDFSAE------HMIFGVDGVDPVRREKLVDLLDIDlQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEIT 176
Cdd:TIGR01189 77 YLGHLPgLKPELSALenlhfwAAIHGGAQRTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 1002242100 177 VDLDVVTRMDLLDFFKEECeQREATIVYATHI 208
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHL-ARGGIVLLTTHQ 186
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-227 |
2.75e-12 |
|
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: 63.87 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQP-PLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdvvrvlngsafhdtqlvcngDLS 92
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG---------------------------DLK 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 ylggswsraigsagdvPLQGDFSaehmifgVDGVDPVRREKLVDLLDIDLQWRMH------------KVSDGQRRRVQIC 160
Cdd:cd03247 54 ----------------PQQGEIT-------LDGVPVSDLEKALSSLISVLNQRPYlfdttlrnnlgrRFSGGERQRLALA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002242100 161 MGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReaTIVYATHIFDGLESwATDIAYIQEGEL 227
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEH-MDKILFLENGKI 174
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-210 |
8.06e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 8.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 13 GIEVSALQFdydgqpPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHMvggrdvvrvlngsafhDTQLVCNGDLs 92
Cdd:COG2401 35 GVELRVVER------YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK----------------GTPVAGCVDV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 yLGGSWSRAIGSAGDVPLQGDFSAEHMIFGVDG-VDPV--RReklvdlldidlqwRMHKVSDGQRRRVQICMGLLHPYKV 169
Cdd:COG2401 92 -PDNQFGREASLIDAIGRKGDFKDAVELLNAVGlSDAVlwLR-------------RFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002242100 170 LLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFD 210
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-207 |
1.35e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 63.18 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDY---DGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdvvrVLNGSAfhdtqlvcnGD 90
Cdd:COG1116 8 LELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-----------LEKPTS---------GE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 91 LSYLGGSWSRAIGSAGDVPlQgDFS-------AEHMIFGVDGVD---PVRREKLVDLLD-IDLQWRMHK----VSDGQRR 155
Cdd:COG1116 68 VLVDGKPVTGPGPDRGVVF-Q-EPAllpwltvLDNVALGLELRGvpkAERRERARELLElVGLAGFEDAyphqLSGGMRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 156 RVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH 197
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-225 |
1.46e-11 |
|
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: 62.51 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 21 FDYDGQPPLfaRFNLRIAPGSRCLLIGANGSGKTTLLKILAG-------KHMVGGRDVV------RVLNgSAFHDTQLvc 87
Cdd:cd03298 7 RFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfetpqsgRVLINGVDVTaappadRPVS-MLFQENNL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 88 ngdLSYLGGSWSRAIGSAGDVPLQG-DFSAEHMIF---GVDGVDPVRREKLvdlldidlqwrmhkvSDGQRRRVQICMGL 163
Cdd:cd03298 82 ---FAHLTVEQNVGLGLSPGLKLTAeDRQAIEVALarvGLAGLEKRLPGEL---------------SGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 164 LHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEG 225
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
34-239 |
2.04e-11 |
|
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: 62.60 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDVVRvLNGSA-----------FHDTQLVcngdlsylg 95
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCInglerptSGSVLVDGTDLTL-LSGKElrkarrrigmiFQHFNLL--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 96 gsWSRAIgsAGDV--PLQgdfsaehmIFGVDGVDpvRREKLVDLLD-IDLQWRMHK----VSDGQRRRVQICMGL-LHPy 167
Cdd:cd03258 95 --SSRTV--FENValPLE--------IAGVPKAE--IEERVLELLElVGLEDKADAypaqLSGGQKQRVGIARALaNNP- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 168 KVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGELrksAKYSDVEEL 239
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV---VEEGTVEEV 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-214 |
6.67e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 28 PLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHM-VGGRdvVRvLNGSAFHDTQlvCNGDLSYLGGswSRAIGSAG 106
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPpAAGT--IK-LDGGDIDDPD--VAEACHYLGH--RNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 107 DVPLQGDFSAEhmIFGVDGVDPVRREKLVDLLDI-DLQWRMhkVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRM 185
Cdd:PRK13539 89 TVAENLEFWAA--FLGGEELDIAAALEAVGLAPLaHLPFGY--LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|....*....
gi 1002242100 186 DLLDFFKEECEQrEATIVYATHIFDGLES 214
Cdd:PRK13539 165 LFAELIRAHLAQ-GGIVIAATHIPLGLPG 192
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
34-207 |
8.83e-11 |
|
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: 60.66 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVCNGDLSYLgGSWSRAIG---------- 103
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNG--------LVEPTSGSVLIDGTDINKLKGKAL-RQLRRQIGmifqqfnlie 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 104 --SAGDVPLQGDFSAEHMIFGVDGVDPvRREKL--------VDLLDIDLQwRMHKVSDGQRRRVQICMGLLHPYKVLLLD 173
Cdd:cd03256 92 rlSVLENVLSGRLGRRSTWRSLFGLFP-KEEKQralaalerVGLLDKAYQ-RADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190
....*....|....*....|....*....|....
gi 1002242100 174 EITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRINREEGITVIVSLH 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-235 |
1.16e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.76 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQP-PLFARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVvrvlngSAFHDTQL 85
Cdd:PRK11160 339 LTLNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrawdpqqGEILLNGQPI------ADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 86 ------------VCNGDLsylggswsR-----AIGSAGDvplqgdfsaEHMIfgvdgvDPVRREKLVDLLDIDL---QW- 144
Cdd:PRK11160 413 rqaisvvsqrvhLFSATL--------RdnlllAAPNASD---------EALI------EVLQQVGLEKLLEDDKglnAWl 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 145 ----RmhKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReaTIVYATHIFDGLESWATdIA 220
Cdd:PRK11160 470 geggR--QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDR-IC 544
|
250
....*....|....*
gi 1002242100 221 YIQEGELRKSAKYSD 235
Cdd:PRK11160 545 VMDNGQIIEQGTHQE 559
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-208 |
1.54e-10 |
|
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: 59.43 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 29 LFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAfhdtqLVCNGDLSYLGGSWSRAIGSAGDV 108
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG--------LSPPLAGRV-----LLNGGPLDFQRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 109 P-LQGDFSAE------HMIFGVDGV-DPVRREKLVDLLDIDLqwrmHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLD 180
Cdd:cd03231 82 PgIKTTLSVLenlrfwHADHSDEQVeEALARVGLNGFEDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*...
gi 1002242100 181 VVTRMDLLDFFKEECeQREATIVYATHI 208
Cdd:cd03231 158 KAGVARFAEAMAGHC-ARGGMVVLTTHQ 184
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
12-227 |
3.82e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 59.70 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 12 SGIEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRVlngsafhdtq 84
Cdd:COG3839 2 ASLELENVSKSYGGVEAL-KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAgledptsGEILIGGRDVTDL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 85 lvcngdlsylggswsraigsagdVPLQGDFS--------------AEHMIFG--VDGVDPVRREKLV----DLLDID--L 142
Cdd:COG3839 71 -----------------------PPKDRNIAmvfqsyalyphmtvYENIAFPlkLRKVPKAEIDRRVreaaELLGLEdlL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 143 QWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHifDGLE--SWATDIA 220
Cdd:COG3839 128 DRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTH--DQVEamTLADRIA 205
|
....*..
gi 1002242100 221 YIQEGEL 227
Cdd:COG3839 206 VMNDGRI 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-207 |
4.93e-10 |
|
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: 58.37 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQP-PLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG--KHMVGgrdvvRVLNGSafHDTQLVCNGD 90
Cdd:cd03245 3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlyKPTSG-----SVLLDG--TDIRQLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 91 LsylggswSRAIGSAG-DVPLqgdFSA---EHMIFGVDGVDPVRREKLVDL-------------LDIDLQWRMHKVSDGQ 153
Cdd:cd03245 76 L-------RRNIGYVPqDVTL---FYGtlrDNITLGAPLADDERILRAAELagvtdfvnkhpngLDLQIGERGRGLSGGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002242100 154 RRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReaTIVYATH 207
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITH 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
32-228 |
8.31e-10 |
|
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: 57.65 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 32 RFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRVlnGSAFHDTQLVCNgdlSYlggswsrAIGS 104
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIAgleeptsGRIYIGGRDVTDL--PPKDRDIAMVFQ---NY-------ALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 105 AGDVplqgdfsAEHMIFG--VDGVDPV----RREKLVDLLDID--LQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEIT 176
Cdd:cd03301 86 HMTV-------YDNIAFGlkLRKVPKDeideRVREVAELLQIEhlLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 177 VDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGELR 228
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-236 |
1.23e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.82 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFAR----FNLRIAPGSRCLLIGANGSGKTTLLKILAGKhMVGGRDVVRVlngsafhdtqlvcnG 89
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGL-LQPTEGKVTV--------------G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 90 DLSYLGGSWSRAI-------GSAGDVPLQGDFSA---EHMIFGVD--GVDPVRREKL----VDLLDIDLQ-WRMH--KVS 150
Cdd:PRK13643 67 DIVVSSTSKQKEIkpvrkkvGVVFQFPESQLFEEtvlKDVAFGPQnfGIPKEKAEKIaaekLEMVGLADEfWEKSpfELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 151 DGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFkEECEQREATIVYATHIFDGLESWATDIAYIQEGELRKS 230
Cdd:PRK13643 147 GGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISC 225
|
....*.
gi 1002242100 231 AKYSDV 236
Cdd:PRK13643 226 GTPSDV 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-207 |
1.37e-09 |
|
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: 57.25 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRVLN-----GSAFH 81
Cdd:cd03300 1 IELENVSKFYGGFVAL-DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgfetptsGEILLDGKDITNLPPhkrpvNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 82 DTQLVCNGDLsylggswsraigsagdvplqgdfsAEHMIFG--VDGVDP-VRREKLVDLLDI----DLQWRM-HKVSDGQ 153
Cdd:cd03300 80 NYALFPHLTV------------------------FENIAFGlrLKKLPKaEIKERVAEALDLvqleGYANRKpSQLSGGQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002242100 154 RRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:cd03300 136 QQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTH 189
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
33-188 |
1.38e-09 |
|
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: 56.50 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 33 FNLRIAPGSRCLLIGANGSGKTTLLKILAGKHMVGGR---DVvrVLNGSAFHDTQLVCNGDLSYLGgswsraigsagdvp 109
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSvegDI--HYNGIPYKEFAEKYPGEIIYVS-------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 110 lQGDFSAEHMIfgvdgvdpVRReklvdLLDIDLQWRMH----KVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRM 185
Cdd:cd03233 90 -EEDVHFPTLT--------VRE-----TLDFALRCKGNefvrGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
...
gi 1002242100 186 DLL 188
Cdd:cd03233 156 EIL 158
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-226 |
2.56e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.30 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPplfARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDV---------VRVLng 77
Cdd:COG3840 2 LRLDDLTYRYGDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAgflppdsGRILWNGQDLtalppaerpVSML-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 78 saFHDTQLvcngdlsylggswsraigsagdvplqgdFS----AEHMIFGVD---GVDPVRREKLVDLLD----IDLQWRM 146
Cdd:COG3840 77 --FQENNL----------------------------FPhltvAQNIGLGLRpglKLTAEQRAQVEQALErvglAGLLDRL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 147 -HKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEG 225
Cdd:COG3840 127 pGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADG 206
|
.
gi 1002242100 226 E 226
Cdd:COG3840 207 R 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-248 |
2.90e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.68 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPL-FARFNLRIAPGSRCLLIGANGSGKTTLLKIlagkhMVGgrdVVRVLNGSAFHDTQLVCNGDLS 92
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKL-----MIG---IEKVKSGEIFYNNQAITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 YLggswSRAIGSAGDVP---LQGDFSAEHMIFGVDG----VDPVRREKLVDLLDIDLQWRM----HKVSDGQRRRVQICM 161
Cdd:PRK13648 80 KL----RKHIGIVFQNPdnqFVGSIVKYDVAFGLENhavpYDEMHRRVSEALKQVDMLERAdyepNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 162 GLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHifDGLESWATD-IAYIQEGELRKSAKYSDVeeLK 240
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITH--DLSEAMEADhVIVMNKGTVYKEGTPTEI--FD 231
|
....*...
gi 1002242100 241 SAKNLLSV 248
Cdd:PRK13648 232 HAEELTRI 239
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-243 |
3.41e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.54 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDG-QPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVCNGDLS 92
Cdd:PRK13632 8 IKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG--------LLKPQSGEIKIDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 YLGGSW--------SRAIGSagdvplqgdfSAEHMI-FGVDG--VDPVRREKLVDLL----DID--LQWRMHKVSDGQRR 155
Cdd:PRK13632 80 EIRKKIgiifqnpdNQFIGA----------TVEDDIaFGLENkkVPPKKMKDIIDDLakkvGMEdyLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 156 RVQICMGL-LHPyKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDglESWATD-IAYIQEGELRKSAKY 233
Cdd:PRK13632 150 RVAIASVLaLNP-EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD--EAILADkVIVFSEGKLIAQGKP 226
|
250
....*....|....
gi 1002242100 234 SDV----EELKSAK 243
Cdd:PRK13632 227 KEIlnnkEILEKAK 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-241 |
3.56e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.57 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPlFAR-----FNLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDVvrvlngsafh 81
Cdd:PRK13634 3 ITFQKVEHRYQYKTP-FERralydVNVSIPSGSYVAIIGHTGSGKSTLLQHLngllqptSGTVTIGERVI---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 82 dTQLVCNGDLSYLggswSRAIGSAGDVP--------LQGDFSAEHMIFGVDGVDPVRREK-LVDL--LDIDLQWRM-HKV 149
Cdd:PRK13634 72 -TAGKKNKKLKPL----RKKVGIVFQFPehqlfeetVEKDICFGPMNFGVSEEDAKQKAReMIELvgLPEELLARSpFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 150 SDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGELRK 229
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
250
....*....|....*.
gi 1002242100 230 SAK----YSDVEELKS 241
Cdd:PRK13634 227 QGTpreiFADPDELEA 242
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-227 |
4.03e-09 |
|
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: 54.92 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDY-DGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHM-VGGRdvVRvLNGSAFHDTqlvcngDL 91
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGR--VR-LDGADISQW------DP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 92 SYLGgswsRAIGS-AGDVPLQGDFSAEHmIFgvdgvdpvrreklvdlldidlqwrmhkvSDGQRRRVQICMGLLHPYKVL 170
Cdd:cd03246 72 NELG----DHVGYlPQDDELFSGSIAEN-IL----------------------------SGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002242100 171 LLDEITVDLDVVTRMDLLDFFKeECEQREATIVYATHIFDGLESwATDIAYIQEGEL 227
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIA-ALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-207 |
4.40e-09 |
|
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: 55.49 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDVVRvLNGSAfhdtqlv 86
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIykeelptSGTIRVNGQDVSD-LRGRA------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 87 cngdLSYLggswSRAIGsagdVPLQgDFS-------AEHMIFG--VDGVDP-VRREKLVDLLD-IDLQWRMH----KVSD 151
Cdd:cd03292 73 ----IPYL----RRKIG----VVFQ-DFRllpdrnvYENVAFAleVTGVPPrEIRKRVPAALElVGLSHKHRalpaELSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002242100 152 GQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKeECEQREATIVYATH 207
Cdd:cd03292 140 GEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLK-KINKAGTTVVVATH 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-207 |
5.06e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 56.74 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 24 DGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG--KHmvGGRDVVRVLNGSAFHDTQlvcngdLSYLggswsrA 101
Cdd:COG4178 374 DGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwPY--GSGRIARPAGARVLFLPQ------RPYL------P 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 102 IGSAGDV---PLQ-GDFSAEHMIfgvDGVDPVRREKLVDLLDIDLQWRmHKVSDGQRRRVQICMGLLHPYKVLLLDEITV 177
Cdd:COG4178 439 LGTLREAllyPATaEAFSDAELR---EALEAVGLGHLAERLDEEADWD-QVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190
....*....|....*....|....*....|
gi 1002242100 178 DLDVVTRMDLLDFFKEECEqrEATIVYATH 207
Cdd:COG4178 515 ALDEENEAALYQLLREELP--GTTVISVGH 542
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-225 |
6.00e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.90 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDY-DGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHM-------VGGRDV-------VRVLNGS 78
Cdd:PRK13647 5 IEVEDLHFRYkDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLpqrgrvkVMGREVnaenekwVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 79 AFHDTQlvcngDLSYLGGSWSraigsagDVPlqgdFSAEHMIFGVDGVDPVRRE--KLVDLLDIDLQWRMHkVSDGQRRR 156
Cdd:PRK13647 84 VFQDPD-----DQVFSSTVWD-------DVA----FGPVNMGLDKDEVERRVEEalKAVRMWDFRDKPPYH-LSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 157 VQICMGLLHPYKVLLLDEITVDLDVV---TRMDLLDFFkeecEQREATIVYATHIFDGLESWATDIAYIQEG 225
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRgqeTLMEILDRL----HNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-180 |
7.25e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 17 SALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVCNGDLsylgg 96
Cdd:PRK13543 15 HALAFSRNEEP-VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAG--------LLHVESGQIQIDGKTATRGDR----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 97 swSRAIGSAGDVP-LQGDFSA---EHMIFGVDGVDPVRRE----KLVDLLDIDlQWRMHKVSDGQRRRVQICMGLLHPYK 168
Cdd:PRK13543 81 --SRFMAYLGHLPgLKADLSTlenLHFLCGLHGRRAKQMPgsalAIVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAP 157
|
170
....*....|..
gi 1002242100 169 VLLLDEITVDLD 180
Cdd:PRK13543 158 LWLLDEPYANLD 169
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-207 |
7.48e-09 |
|
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: 54.88 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFaRFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhMVGGRDVVRVlNGSAFHDTQLVCNGDLSY 93
Cdd:cd03260 1 IELRDLNVYYGDKHALK-DISLDIPKGEITALIGPSGCGKSTLLRLLNR--LNDLIPGAPD-EGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 LggSWSRAIGSAGDVPLQGDFS-AEHMIFGVdgvdPVRREKLVDLLDIDLQWRMHKV---------------SDGQRRRV 157
Cdd:cd03260 77 L--ELRRRVGMVFQKPNPFPGSiYDNVAYGL----RLHGIKLKEELDERVEEALRKAalwdevkdrlhalglSGGQQQRL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002242100 158 QICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECeqREATIVYATH 207
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTH 198
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-207 |
8.59e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 55.49 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 12 SGIEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRVlngSAFHdtq 84
Cdd:COG3842 4 PALELENVSKRYGDVTAL-DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgfetpdsGRILLDGRDVTGL---PPEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 85 lvcngdlsylggswsRAIGsagdvplqgdfsaehMIF-------------------GVDGVDPVRREKLVD-LLDI---- 140
Cdd:COG3842 77 ---------------RNVG---------------MVFqdyalfphltvaenvafglRMRGVPKAEIRARVAeLLELvgle 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002242100 141 DLQWRM-HKVSDGQRRRVQICMGL-LHPyKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:COG3842 127 GLADRYpHQLSGGQQQRVALARALaPEP-RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTH 194
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-62 |
1.05e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 1.05e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 11 RSGIEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:PRK15064 317 RNALEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG 367
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
14-225 |
1.08e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.85 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDY-DGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVcngDLS 92
Cdd:PRK13636 6 LKVEELNYNYsDGTHAL-KGININIKKGEVTAILGGNGAGKSTLFQNLNG--------ILKPSSGRILFDGKPI---DYS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 YLG-GSWSRAIGSAGDVPLQGDFSA---EHMIFGVDGV----DPVRR--EKLVDLLDID-LQWR-MHKVSDGQRRRVQIC 160
Cdd:PRK13636 74 RKGlMKLRESVGMVFQDPDNQLFSAsvyQDVSFGAVNLklpeDEVRKrvDNALKRTGIEhLKDKpTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002242100 161 MGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEG 225
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-207 |
1.13e-08 |
|
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: 53.71 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 12 SGIEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHMVGGrdvvrvLNGsafhdtQLVCNGDL 91
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG------VSG------EVLINGRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 92 SYLgGSWSRAIGSagdVPlQGDfsaehMIFGVDGVdpvrREKLvdlldiDLQWRMHKVSDGQRRRVQICMGLLHPYKVLL 171
Cdd:cd03213 75 LDK-RSFRKIIGY---VP-QDD-----ILHPTLTV----RETL------MFAAKLRGLSGGERKRVSIALELVSNPSLLF 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002242100 172 LDEITVDLDVVTRMDLLDFFKEECEQREaTIVYATH 207
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIH 169
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-185 |
1.14e-08 |
|
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: 54.54 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDG-QPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDVvrvlngsafHDTQL 85
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRILIDGHDV---------RDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 86 vcngdlsylgGSWSRAIG-SAGDVPLQGDFSAEHMIFGVDGVDP--VRR-----------EKLVDLLDIDLQWRMHKVSD 151
Cdd:cd03251 72 ----------ASLRRQIGlVSQDVFLFNDTVAENIAYGRPGATReeVEEaaraanahefiMELPEGYDTVIGERGVKLSG 141
|
170 180 190
....*....|....*....|....*....|....
gi 1002242100 152 GQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRM 185
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESER 175
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-183 |
1.40e-08 |
|
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: 55.33 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHM-------VGgrDVVRVLNGSAFHDT--- 83
Cdd:TIGR03719 323 IEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQpdsgtieIG--ETVKLAYVDQSRDAldp 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 84 -----QLVCNG-DLSYLGGSW--SRAIGSAgdvplqgdfsaehmiFGVDGVDpvrREKLVDLLdidlqwrmhkvSDGQRR 155
Cdd:TIGR03719 400 nktvwEEISGGlDIIKLGKREipSRAYVGR---------------FNFKGSD---QQKKVGQL-----------SGGERN 450
|
170 180
....*....|....*....|....*...
gi 1002242100 156 RVQICMGLLHPYKVLLLDEITVDLDVVT 183
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-71 |
1.45e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 55.56 E-value: 1.45e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002242100 11 RSGIEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDV 71
Cdd:COG1132 337 RGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsGRILIDGVDI 404
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
33-207 |
1.53e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.11 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 33 FNLRiaPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDVVRVLN----------GSAFHDTQLVCNgdlsylg 95
Cdd:PRK10908 23 FHMR--PGEMAFLTGHSGAGKSTLLKLIcgierpsAGKIWFSGHDITRLKNrevpflrrqiGMIFQDHHLLMD------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 96 gswsRAIGSAGDVPLqgdfsaehMIFGVDGVDPVRREKL----VDLLDIDLQWRMhKVSDGQRRRVQICMGLLHPYKVLL 171
Cdd:PRK10908 94 ----RTVYDNVAIPL--------IIAGASGDDIRRRVSAaldkVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002242100 172 LDEITVDLDVVTRMDLLDFFkEECEQREATIVYATH 207
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLF-EEFNRVGVTVLMATH 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-207 |
1.99e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 35 LRIAPGSRCLLIGANGSGKTTLLKILAGKHMVGGRDVvrVLNGSAFH--DTQLVCNgDLSYL-------GGSWSRAIGSA 105
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI--LLDAQPLEswSSKAFAR-KVAYLpqqlpaaEGMTVRELVAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 106 GDVPLQGDFSAehmiFGVDgvDPVRREKLVDLldIDLQWRMHKVSD----GQRRRVQICMGLLHPYKVLLLDEITVDLDV 181
Cdd:PRK10575 109 GRYPWHGALGR----FGAA--DREKVEEAISL--VGLKPLAHRLVDslsgGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180
....*....|....*....|....*.
gi 1002242100 182 VTRMDLLDFFKEECEQREATIVYATH 207
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-207 |
2.54e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.43 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 23 YDGQPplfARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHMVGGRDVvrVLNGSAFHDTqlvcngdlsylggswsrai 102
Cdd:PRK10771 11 YHHLP---MRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL--TLNGQDHTTT------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 103 gsagdVPLQGDFS---AEHMIF---------GVdGVDP------VRREKLVDLLD----IDLQWRM-HKVSDGQRRRVQI 159
Cdd:PRK10771 67 -----PPSRRPVSmlfQENNLFshltvaqniGL-GLNPglklnaAQREKLHAIARqmgiEDLLARLpGQLSGGQRQRVAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002242100 160 CMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
33-180 |
3.73e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.17 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 33 FNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQlvcngDLSYLgGSWSRAiGSAGDV---P 109
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAG--------SLPPDSGSILIDGK-----DVTKL-PEYKRA-KYIGRVfqdP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 110 LQGdfSAEHM-I-------------FGVD-GVDPVRRE---KLVDLLDIDLQWRMH-KV---SDGQRRRVQICMGLLHPY 167
Cdd:COG1101 90 MMG--TAPSMtIeenlalayrrgkrRGLRrGLTKKRRElfrELLATLGLGLENRLDtKVgllSGGQRQALSLLMATLTKP 167
|
170
....*....|...
gi 1002242100 168 KVLLLDEITVDLD 180
Cdd:COG1101 168 KLLLLDEHTAALD 180
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-242 |
3.93e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 53.27 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDY-DGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG----------KHMVGGRDV-------VRVL 75
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpnsKITVDGITLtaktvwdIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 76 NGSAFH--DTQLV---CNGDLSYlgGSWSRAIgsagdvplqgdfSAEHMIFGVDGVdpVRREKLVDLLDIDLQWrmhkVS 150
Cdd:PRK13640 86 VGIVFQnpDNQFVgatVGDDVAF--GLENRAV------------PRPEMIKIVRDV--LADVGMLDYIDSEPAN----LS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 151 DGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESwATDIAYIQEGELRKS 230
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQ 224
|
250
....*....|....*.
gi 1002242100 231 AK----YSDVEELKSA 242
Cdd:PRK13640 225 GSpveiFSKVEMLKEI 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-207 |
4.07e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRVlnGSAFHDtqlv 86
Cdd:PRK13538 2 LEARNLACERDERI-LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAglarpdaGEVLWQGEPIRRQ--RDEYHQ---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 87 cngDLSYLGgswsRAIGsagdvpLQGDFSA-EHMIFGVDGVDPVRREKLVDLLD-IDLQWRM----HKVSDGQRRRVQIC 160
Cdd:PRK13538 75 ---DLLYLG----HQPG------IKTELTAlENLRFYQRLHGPGDDEALWEALAqVGLAGFEdvpvRQLSAGQQRRVALA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002242100 161 MGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEqREATIVYATH 207
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAE-QGGMVILTTH 187
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-207 |
4.29e-08 |
|
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: 52.73 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 13 GIEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRVlngsafhDTQl 85
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL-DDVSLDIPSGELVALLGPSGSGKTTLLRLIAglerpdsGTILFGGEDATDV-------PVQ- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 86 vcngdlsylggswSRAIGSAgdvpLQGDFSAEHMI------FGVDgVDPVR--------REKLVDLLD-IDLQW---RM- 146
Cdd:cd03296 73 -------------ERNVGFV----FQHYALFRHMTvfdnvaFGLR-VKPRSerppeaeiRAKVHELLKlVQLDWladRYp 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002242100 147 HKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:cd03296 135 AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTH 195
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-249 |
8.76e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.11 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTL-------LKILAGKHMVGGRDV-------VRVLNGSA 79
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLfrhfngiLKPTSGSVLIRGEPItkenireVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 80 FHdtqlvcNGDLSYLGGSWSRAIgSAGDVPLQGDFSA-EHmifgvdgvdpvRREKLVDLLDI-DLQWRM-HKVSDGQRRR 156
Cdd:PRK13652 84 FQ------NPDDQIFSPTVEQDI-AFGPINLGLDEETvAH-----------RVSSALHMLGLeELRDRVpHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 157 VQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGELrksAKYSDV 236
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI---VAYGTV 222
|
250
....*....|...
gi 1002242100 237 EELKSAKNLLSVV 249
Cdd:PRK13652 223 EEIFLQPDLLARV 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
14-244 |
8.93e-08 |
|
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: 51.90 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDVVRvLNGSAFHDTQlv 86
Cdd:COG1127 6 IEVRNLTKSFGDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIigllrpdSGEILVDGQDITG-LSEKELYELR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 87 cngdlsylggswsRAIG------------SAGD---VPLQgdfsaEHMIFGVDGVDPVRREKL--VDLLDIdlqwrMHK- 148
Cdd:COG1127 82 -------------RRIGmlfqggalfdslTVFEnvaFPLR-----EHTDLSEAEIRELVLEKLelVGLPGA-----ADKm 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 149 ---VSDGQRRRVqicmGL-----LHPyKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIA 220
Cdd:COG1127 139 pseLSGGMRKRV----ALaralaLDP-EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVA 213
|
250 260
....*....|....*....|....
gi 1002242100 221 YIQEGELRKSAkysDVEELKSAKN 244
Cdd:COG1127 214 VLADGKIIAEG---TPEELLASDD 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
34-203 |
9.40e-08 |
|
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: 51.96 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKH-------MVGGRDVV------RVLNGSA--FHDTQLVcnGDLS------ 92
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNLITGFYrptsgriLFDGRDITglpphrIARLGIArtFQNPRLF--PELTvlenvl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 --YLGGSWSRAIGSAGDVPLQGDFSAEHmifgvdgvdpvrREKLVDLLD-IDLQWRMHKVSD----GQRRRVQICMGL-L 164
Cdd:COG0411 102 vaAHARLGRGLLAALLRLPRARREEREA------------RERAEELLErVGLADRADEPAGnlsyGQQRRLEIARALaT 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002242100 165 HPyKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIV 203
Cdd:COG0411 170 EP-KLLLLDEPAAGLNPEETEELAELIRRLRDERGITIL 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
33-227 |
1.09e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 33 FNLRIAPGSRCLLIGANGSGKTTLLKILAgkhmvggrDVVRVLNGSAFHDTQLVcngdLSYLGGSWSRAIG-------SA 105
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLS--------RLMTPAHGHVWLDGEHI----QHYASKEVARRIGllaqnatTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 106 GDVPLQ-----GDFSAEHMI--FGVDGVDPVRRE-KLVDLLDIDLQwRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITV 177
Cdd:PRK10253 94 GDITVQelvarGRYPHQPLFtrWRKEDEEAVTKAmQATGITHLADQ-SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002242100 178 DLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGEL 227
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
34-210 |
1.29e-07 |
|
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: 50.12 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKH-------MVGGRDVvrvlngsAFHDTQlvcngdlsylgGSWSRAIGsag 106
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYkpdsgeiLVDGKEV-------SFASPR-----------DARRAGIA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 107 dvplqgdfsaehMIfgvdgvdpvrreklvdlldidlqwrmHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMD 186
Cdd:cd03216 79 ------------MV--------------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180
....*....|....*....|....
gi 1002242100 187 LLDFFKEECEQrEATIVYATHIFD 210
Cdd:cd03216 121 LFKVIRRLRAQ-GVAVIFISHRLD 143
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
14-184 |
1.38e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 51.62 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVCngdlsy 93
Cdd:PRK11248 2 LQISHLYADYGGKPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIAG--------FVPYQHGSITLDGKPVE------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 94 lGGSWSRAIGSAGDVPLQGDFSAEHMIFGVD--GVDPVRRE-------KLVDLLDIDlQWRMHKVSDGQRRRVQICMGLL 164
Cdd:PRK11248 67 -GPGAERGVVFQNEGLLPWRNVQDNVAFGLQlaGVEKMQRLeiahqmlKKVGLEGAE-KRYIWQLSGGQRQRVGIARALA 144
|
170 180
....*....|....*....|
gi 1002242100 165 HPYKVLLLDEITVDLDVVTR 184
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTR 164
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
33-236 |
1.80e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.33 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 33 FNLRiaPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVCNGDLSYLG---------GSWS---- 99
Cdd:PRK15112 34 FTLR--EGQTLAIIGENGSGKSTLAKMLAG--------MIEPTSGELLIDDHPLHFGDYSYRSqrirmifqdPSTSlnpr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 100 RAIGSAGDVPLQGDfsaehmifgvDGVDPVRREK-------LVDLLDIDLQWRMHKVSDGQRRRVQICMGLLHPYKVLLL 172
Cdd:PRK15112 104 QRISQILDFPLRLN----------TDLEPEQREKqiietlrQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002242100 173 DEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGELRKSAKYSDV 236
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
25-207 |
1.96e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.86 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 25 GQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLK-------ILAGKHMVGGRDVvrvlNGSAFHDtqlvcngdlsylggs 97
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVDGLKV----NDPKVDE--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 98 wsRAI-GSAGDVPLQGDF-----SAEHMIFG---VDGVDPVRREKLV-DLLD-IDLQWRMH----KVSDGQRRRVQICMG 162
Cdd:PRK09493 73 --RLIrQEAGMVFQQFYLfphltALENVMFGplrVRGASKEEAEKQArELLAkVGLAERAHhypsELSGGQQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1002242100 163 LLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQrEATIVYATH 207
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTH 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
130-207 |
2.15e-07 |
|
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: 51.21 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 130 RREKLVDLLD---IDLQWRM-----HKVSDGQRRRVQICMGL-LHPyKVLLLDEITVDLDVVTRMDLLDFFKEECEQREA 200
Cdd:COG0444 124 ARERAIELLErvgLPDPERRldrypHELSGGMRQRVMIARALaLEP-KLLIADEPTTALDVTIQAQILNLLKDLQRELGL 202
|
....*..
gi 1002242100 201 TIVYATH 207
Cdd:COG0444 203 AILFITH 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-228 |
2.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.14 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDY-DGQPPLfARFNLRIAPGSRCLLIGANGSGKTT-------LLKILAGKHMVGGRDV--------VRVLNG 77
Cdd:PRK13644 2 IRLENVSYSYpDGTPAL-ENINLVIKKGEYIGIIGKNGSGKSTlalhlngLLRPQKGKVLVSGIDTgdfsklqgIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 78 SAFH--DTQLVcngdlsylggswsraigsagdvplqGDFSAEHMIFGVDG--VDPVRREKLVD--LLDIDLQWRMHK--- 148
Cdd:PRK13644 81 IVFQnpETQFV-------------------------GRTVEEDLAFGPENlcLPPIEIRKRVDraLAEIGLEKYRHRspk 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 149 -VSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKeECEQREATIVYATHIFDGLESwATDIAYIQEGEL 227
Cdd:PRK13644 136 tLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIK-KLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKI 213
|
.
gi 1002242100 228 R 228
Cdd:PRK13644 214 V 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-254 |
5.83e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 28 PLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrDVVrvlngsaFHDTQLVCNGDL--SYLGGSWSRAIgsA 105
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-------EVL-------LDDGRIIYEQDLivARLQQDPPRNV--E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 106 GDVplqGDFSAE------------HMIFGVDGVDPVRR-----EKLVDLLDIDLQW----RMHKV--------------- 149
Cdd:PRK11147 81 GTV---YDFVAEgieeqaeylkryHDISHLVETDPSEKnlnelAKLQEQLDHHNLWqlenRINEVlaqlgldpdaalssl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 150 SDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEeceqREATIVY-----------ATHIFD----GLES 214
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFishdrsfirnmATRIVDldrgKLVS 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1002242100 215 WATDI-AYIQEGE--LRksakysdVEELKSAK--NLLSVVESWLR 254
Cdd:PRK11147 234 YPGNYdQYLLEKEeaLR-------VEELQNAEfdRKLAQEEVWIR 271
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
12-174 |
8.47e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.80 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 12 SGIEVSALQFDY--DGQPPLFA--RFNLRIAPGSRCLLIGANGSGKTTLLKILAG-KHMVGGRdvVRvLNGSAFHDTQLV 86
Cdd:COG4615 326 QTLELRGVTYRYpgEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRPESGE--IL-LDGQPVTADNRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 87 cngdlsylggsWSRAIgsagdvplqgdFSA--------EHMIFGVDGVDPVRREKLVDLLDIDlqwrmHKV--------- 149
Cdd:COG4615 403 -----------AYRQL-----------FSAvfsdfhlfDRLLGLDGEADPARARELLERLELD-----HKVsvedgrfst 455
|
170 180 190
....*....|....*....|....*....|..
gi 1002242100 150 ---SDGQRRRVqicmGLLHPY----KVLLLDE 174
Cdd:COG4615 456 tdlSQGQRKRL----ALLVALledrPILVFDE 483
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
34-207 |
9.17e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 49.70 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAG-KHMVGGRdvvrvlngSAFHDTqlvcngDLSYLGGSwSRAIGSAgdvpLQG 112
Cdd:PRK10851 22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGlEHQTSGH--------IRFHGT------DVSRLHAR-DRKVGFV----FQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 113 DFSAEHMI------FGVDgVDPVR--------REKLVDLLDI----DLQWRM-HKVSDGQRRRVQICMGLLHPYKVLLLD 173
Cdd:PRK10851 83 YALFRHMTvfdniaFGLT-VLPRRerpnaaaiKAKVTQLLEMvqlaHLADRYpAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190
....*....|....*....|....*....|....
gi 1002242100 174 EITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTH 195
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
34-193 |
9.45e-07 |
|
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: 48.97 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKH-------MVGGRDV------VRVLNGSA--FHDTQLVCN---------G 89
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrptsgsvLFDGEDItglpphEIARLGIGrtFQIPRLFPEltvlenvmvA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 90 DLSYLGGSWSRAigsagdvplqGDFSAEHMIfgvdgvdpvrREKLVDLLD-IDLQWRMHKV----SDGQRRRVQICMGL- 163
Cdd:cd03219 100 AQARTGSGLLLA----------RARREEREA----------RERAEELLErVGLADLADRPagelSYGQQRRLEIARALa 159
|
170 180 190
....*....|....*....|....*....|
gi 1002242100 164 LHPyKVLLLDEITVDLDVVTRMDLLDFFKE 193
Cdd:cd03219 160 TDP-KLLLLDEPAAGLNPEETEELAELIRE 188
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-203 |
1.05e-06 |
|
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: 48.64 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFAR-FNLRIAPGSRCLLIGANGSGKTTLLKILAGKHM-VGGRDVVrvlNGsafHDTQLVcngDL 91
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDnISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVpENGRVLV---DG---HDLALA---DP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 92 SYLggswSRAIGsagdVPLQGDF----SAEHMIFGVDGVDPVRR----EKLVDLLDIDLQW----------RMHKVSDGQ 153
Cdd:cd03252 72 AWL----RRQVG----VVLQENVlfnrSIRDNIALADPGMSMERvieaAKLAGAHDFISELpegydtivgeQGAGLSGGQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002242100 154 RRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIV 203
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIII 193
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
34-207 |
1.06e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.91 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAG-KHMVGGRdvvrVLNGSA------------FHDTQLVcngdlsylggSWSR 100
Cdd:PRK11247 32 DLHIPAGQFVAVVGRSGCGKSTLLRLLAGlETPSAGE----LLAGTAplaearedtrlmFQDARLL----------PWKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 101 AIGSAGdVPLQGDFSaehmifgvdgvdPVRREKL--VDLLDIDLQWRMhKVSDGQRRRVQICMGLLHPYKVLLLDEITVD 178
Cdd:PRK11247 98 VIDNVG-LGLKGQWR------------DAALQALaaVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180
....*....|....*....|....*....
gi 1002242100 179 LDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
34-62 |
1.28e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.54 E-value: 1.28e-06
10 20
....*....|....*....|....*....
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAG 74
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
133-261 |
1.33e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 133 KLVDLLDIDLQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREaTIVYATHIFDGL 212
Cdd:PRK13651 150 ELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNV 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002242100 213 ESWATDIAYIQEGELRKSAK----YSDVEELKSAK----NLLSVVESWLRSETKLPK 261
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGDtydiLSDNKFLIENNmeppKLLNFVNKLEKKGIDVPK 285
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-207 |
1.38e-06 |
|
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: 48.94 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKHMV-GGRdvVRVlNGSAFHDTQLVCNgdLSylggSWSRAIGsagdvplqg 112
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPdSGR--IRL-GGEVLQDSARGIF--LP----PHRRRIG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 113 dfsaehMIF---------------------GVDGVDPVRREKLVDLLDID--LQWRMHKVSDGQRRRVQICMGLL-HPyK 168
Cdd:COG4148 81 ------YVFqearlfphlsvrgnllygrkrAPRAERRISFDEVVELLGIGhlLDRRPATLSGGERQRVAIGRALLsSP-R 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002242100 169 VLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSH 192
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-71 |
1.77e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 48.60 E-value: 1.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002242100 13 GIEVSALQFDYdGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG-------KHMVGGRDV 71
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGletpdsgRIVLNGRDL 66
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-272 |
1.87e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKhmvggrdvVRVLNGSAFHDTQLVCNgdLSY------LGGSWSRA---IGS 104
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGE--------LPLLSGERQSQFSHITR--LSFeqlqklVSDEWQRNntdMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 105 AG--DVplqGDFSAEHMIFGVDgvDPVRREKLVDLLDID--LQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLD 180
Cdd:PRK10938 93 PGedDT---GRTTAEIIQDEVK--DPARCEQLAQQFGITalLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 181 VVTRMDLLDFFkEECEQREATIVYATHIFDGLESWATDIAYIQEGELRKSAKYSDVEElksaknlLSVVESWLRSET--- 257
Cdd:PRK10938 168 VASRQQLAELL-ASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ-------QALVAQLAHSEQleg 239
|
250 260
....*....|....*....|.
gi 1002242100 258 -KLPKKEHPR-----PETQPR 272
Cdd:PRK10938 240 vQLPEPDEPSarhalPANEPR 260
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
35-207 |
2.09e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.14 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 35 LRIAPGSRCLLIGANGSGKTTLLKILAG--KHMVG-----GRDVVRvLNGS---AFH-DTQLVCNGDLSYLGGswSRAIG 103
Cdd:PRK10419 33 LSLKSGETVALLGRSGCGKSTLARLLVGleSPSQGnvswrGEPLAK-LNRAqrkAFRrDIQMVFQDSISAVNP--RKTVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 104 SAGDVPLQgdfsaeHMIfgvdGVDPVRRE-------KLVDLLDIDLQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEIT 176
Cdd:PRK10419 110 EIIREPLR------HLL----SLDKAERLarasemlRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190
....*....|....*....|....*....|.
gi 1002242100 177 VDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
149-240 |
2.21e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.29 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 149 VSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEecEQREA-TIVYATHIFDGLESWATDIAYIQEGEL 227
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD--YQKAGhTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
90
....*....|....*..
gi 1002242100 228 RKSAK----YSDVEELK 240
Cdd:PRK13641 224 IKHASpkeiFSDKEWLK 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-62 |
2.33e-06 |
|
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: 46.76 E-value: 2.33e-06
10 20 30
....*....|....*....|....*....|....*
gi 1002242100 28 PLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG 49
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-210 |
2.47e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.09 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQP-PLFARFNLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDV-------VRVLNGS 78
Cdd:PRK13635 6 IRVEHISFRYPDAAtYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLnglllpeAGTITVGGMVLseetvwdVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 79 AFH--DTQLVcngdlsylggswsraiGS--AGDVPL----QGdFSAEHMIFGVDgvDPVRREKLVDLLDIDlqwrMHKVS 150
Cdd:PRK13635 86 VFQnpDNQFV----------------GAtvQDDVAFglenIG-VPREEMVERVD--QALRQVGMEDFLNRE----PHRLS 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002242100 151 DGQRRRVQICMGL-LHPyKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFD 210
Cdd:PRK13635 143 GGQKQRVAIAGVLaLQP-DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLD 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-203 |
3.68e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.36 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 30 FARFNLRI-APGSRCLLIGANGSGKTTLLKILAGKHM--VGG-------RDVVRVLNGSAFHD--TQLVcNGDLSYlggs 97
Cdd:cd03236 15 FKLHRLPVpREGQVLGLVGPNGIGKSTALKILAGKLKpnLGKfddppdwDEILDEFRGSELQNyfTKLL-EGDVKV---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 98 wSRAIGSAGDVPLQGDFSAEHMIFGVDgvDPVRREKLVDLLDID--LQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEI 175
Cdd:cd03236 90 -IVKPQYVDLIPKAVKGKVGELLKKKD--ERGKLDELVDQLELRhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180
....*....|....*....|....*...
gi 1002242100 176 TVDLDVVTRMDLLDFFKEECEQREATIV 203
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDNYVLV 194
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
8-228 |
4.36e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 8 GWRRsgIEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGSAFHDTQLVC 87
Cdd:PRK10522 319 DWQT--LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTG--------LYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 88 NGDL-SYlggswsRAIGSAgdvpLQGDFSAEHMIFGVDGVDP--------VRREKLVDLLDI-DLQWRMHKVSDGQRRRV 157
Cdd:PRK10522 389 AEQPeDY------RKLFSA----VFTDFHLFDQLLGPEGKPAnpalvekwLERLKMAHKLELeDGRISNLKLSKGQKKRL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002242100 158 QICMGLLHPYKVLLLDEITVDLDVVTR----MDLLDFFKEECEqreaTIVYATH---IFDGleswATDIAYIQEGELR 228
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDPHFRrefyQVLLPLLQEMGK----TIFAISHddhYFIH----ADRLLEMRNGQLS 528
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-62 |
4.47e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 4.47e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1002242100 19 LQFdydGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:PRK15064 9 MQF---GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGG 49
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-255 |
4.58e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.03 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdvvrVLNgsafHDTqlvcnGDLSYLGGSWSRA----IG------ 103
Cdd:COG4152 21 SFTVPKGEIFGLLGPNGAGKTTTIRIILG-----------ILA----PDS-----GEVLWDGEPLDPEdrrrIGylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 104 ------SAGdvplqgdfsaEHMIF-----GVDGVDPVRR-EKLVDLLDIDlQWRMHKV---SDGQRRRVQICMGLLHPYK 168
Cdd:COG4152 81 glypkmKVG----------EQLVYlarlkGLSKAEAKRRaDEWLERLGLG-DRANKKVeelSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 169 VLLLDEITVDLDVVTRMDLLDFFKEECEQrEATIVYATHIFDGLESWATDIAYIQEGelRKSAkYSDVEELKS--AKNLL 246
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKG--RKVL-SGSVDEIRRqfGRNTL 225
|
250
....*....|...
gi 1002242100 247 SVV----ESWLRS 255
Cdd:COG4152 226 RLEadgdAGWLRA 238
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
33-207 |
4.64e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 46.76 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 33 FNLRIAPGSRCLLIGANGSGKTTLLKILAGkhMVGGRDVVRvLNGSafhdtqlvcngDLSylggSWS-------RAIGSA 105
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG--LLPGQGEIL-LNGR-----------PLS----DWSaaelarhRAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 106 GDVPLQG-------DFSAEHMifGVDGVDPVRREKLVDLLDID--LQWRMHKVSDGQRRRVQICMGLL------HPY-KV 169
Cdd:COG4138 77 QQSPPFAmpvfqylALHQPAG--ASSEAVEQLLAQLAEALGLEdkLSRPLTQLSGGEWQRVRLAAVLLqvwptiNPEgQL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002242100 170 LLLDEITVDLDVVTRMDLLDFFKEECEQrEATIVYATH 207
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSH 191
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-207 |
4.75e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.44 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 39 PGSRCLLIGANGSGKTTLLKILAGKHMVGGRDVVRVlngsafhdtqlvcngdlsylggswsraigsagdvplqgdfsaeh 118
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 119 mifgvdGVDPVRREKLVDLLDIDLQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLD-----FFKE 193
Cdd:smart00382 37 ------DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLLL 110
|
170
....*....|....
gi 1002242100 194 ECEQREATIVYATH 207
Cdd:smart00382 111 LKSEKNLTVILTTN 124
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
35-228 |
5.35e-06 |
|
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: 46.12 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 35 LRIAPGSRCLLIGANGSGKTTLLkilagkhmvggrdvvRVLNGSAFHDTqlvcnGDLSYLGGSWSRAIGSA-GDVP---- 109
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTI---------------RMILGIILPDS-----GEVLFDGKPLDIAARNRiGYLPeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 110 LQGDFS-AEHMIF-----GVDGVDPVRR-EKLVDLLDIDLQW--RMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLD 180
Cdd:cd03269 81 LYPKMKvIDQLVYlaqlkGLKKEEARRRiDEWLERLELSEYAnkRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002242100 181 VVTRmdllDFFKEEC-EQREA--TIVYATHIFDGLESWATDIAYIQEGELR 228
Cdd:cd03269 161 PVNV----ELLKDVIrELARAgkTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-176 |
6.96e-06 |
|
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: 45.89 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFArFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdVVRVLNGS-AFHDTQlvcngdls 92
Cdd:cd03224 1 LEVENLNAGYGKSQILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMG--------LLPPRSGSiRFDGRD-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 93 yLGGSWSRAIGSAG--DVPlQGdfsaeHMIF---------------GVDGVDPVRREKLVDLLDIdLQWRMHK----VSD 151
Cdd:cd03224 64 -ITGLPPHERARAGigYVP-EG-----RRIFpeltveenlllgayaRRRAKRKARLERVYELFPR-LKERRKQlagtLSG 135
|
170 180
....*....|....*....|....*
gi 1002242100 152 GQRRRVQICMGLLHPYKVLLLDEIT 176
Cdd:cd03224 136 GEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
34-207 |
7.79e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.03 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDVVRvLNGSAFhdTQLvcngDLSYLGGSWSRaigsag 106
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGQDVAT-LDADAL--AQL----RREHFGFIFQR------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 107 dVPLQGDFSAEHMIfGVDGV-----DPVRREKLVDLLD-IDLQWRMH----KVSDGQRRRVQICMGLLHPYKVLLLDEIT 176
Cdd:PRK10535 95 -YHLLSHLTAAQNV-EVPAVyagleRKQRLLRAQELLQrLGLEDRVEyqpsQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190
....*....|....*....|....*....|.
gi 1002242100 177 VDLDVVTRMDLLDFFKEECEQREaTIVYATH 207
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLRDRGH-TVIIVTH 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
34-228 |
7.81e-06 |
|
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: 45.99 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdvvrvlngsafhdTQLVCNGDLSYLGG-SWSRAIGSAgdvpLQG 112
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAG--------------------IYPPDSGTVTVRGRvSSLLGLGGG----FNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 113 DFSAE------HMIFGVDGVDpvRREKLVDLLD-------IDLQWRMHkvSDGQRRRVQICMGLLHPYKVLLLDEITVDL 179
Cdd:cd03220 98 ELTGReniylnGRLLGLSRKE--IDEKIDEIIEfselgdfIDLPVKTY--SSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1002242100 180 DVVTRMDLLDFFKEECEQrEATIVYATHIFDGLESWATDIAYIQEGELR 228
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
34-226 |
9.29e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.74 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKHMVGGRDVVRVLNG-----SAFHDT----------QLVCNGDLSYLggsw 98
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGsplkaSNIRDTeragiviihqELTLVPELSVA---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 99 sRAIGSAGDVPLQGDFSAEHMIFgvdgvdpVRREKLVDLLDIDLQWRMHKVSD---GQRRRVQICMGLLHPYKVLLLDEI 175
Cdd:TIGR02633 97 -ENIFLGNEITLPGGRMAYNAMY-------LRAKNLLRELQLDADNVTRPVGDyggGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002242100 176 TVDLDVVTRMDLLDFFKeECEQREATIVYATHIFDGLESWATDIAYIQEGE 226
Cdd:TIGR02633 169 SSSLTEKETEILLDIIR-DLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-183 |
9.68e-06 |
|
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: 45.68 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDV-------VRVLNGSA 79
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLmrfydpqKGQILIDGIDIrdisrksLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 80 FHDTQLVcNGDLS---YLGGS------WSRAIGSAGdvplqgdfsAEHMIfgvdgvdpvrrEKLVDLLDIDLQWRMHKVS 150
Cdd:cd03254 83 LQDTFLF-SGTIMeniRLGRPnatdeeVIEAAKEAG---------AHDFI-----------MKLPNGYDTVLGENGGNLS 141
|
170 180 190
....*....|....*....|....*....|...
gi 1002242100 151 DGQRRRVQICMGLLHPYKVLLLDEITVDLDVVT 183
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-236 |
1.06e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 45.67 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 11 RSGIEVSALQFDYdGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILagKHMVGGRDVVRVlNGSAFHDTQLVCNGD 90
Cdd:PRK14247 1 MNKIEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF--NRLIELYPEARV-SGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 91 LSYLGGSWSRAIGSAGDVPLQGDFSAEHMIFGVDGVDPVRRE------------KLVDLLDIDLQWRMHKVSDGQRRRVQ 158
Cdd:PRK14247 77 VIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqervrwalekaQLWDEVKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002242100 159 ICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEecEQREATIVYATHiFDGLESWATD-IAYIQEGELRKSAKYSDV 236
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLE--LKKDMTIVLVTH-FPQQAARISDyVAFLYKGQIVEWGPTREV 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
147-225 |
1.06e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 1.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002242100 147 HKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEG 225
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
45-203 |
1.13e-05 |
|
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: 45.34 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 45 LIGANGSGKTTLLKILAGKHMVGGRDVVRVL-NGSAFH-DTQLVCngdLSYLggswsraigsagdvpLQGDFSA------ 116
Cdd:cd03234 38 ILGSSGSGKTTLLDAISGRVEGGGTTSGQILfNGQPRKpDQFQKC---VAYV---------------RQDDILLpgltvr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 117 EHMIFGV-------------DGVDPVRREKLVDLLDIDLQwRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVT 183
Cdd:cd03234 100 ETLTYTAilrlprkssdairKKRVEDVLLRDLALTRIGGN-LVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180
....*....|....*....|
gi 1002242100 184 RMDLLDFFKEECEQREATIV 203
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVIL 198
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-226 |
1.65e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.60 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILAG-KHMVGGrdvvrvlngsafhdtQLVCNG-DL 91
Cdd:PRK11607 20 LEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAG---------------QIMLDGvDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 92 SYLgGSWSRAIgsagDVPLQGDFSAEHMI------FGVD------GVDPVRREKLVDLLDID--LQWRMHKVSDGQRRRV 157
Cdd:PRK11607 84 SHV-PPYQRPI----NMMFQSYALFPHMTveqniaFGLKqdklpkAEIASRVNEMLGLVHMQefAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002242100 158 QICMGLLHPYKVLLLDEITVDLD--VVTRMDL--LDFFkeecEQREATIVYATHIFDGLESWATDIAYIQEGE 226
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDkkLRDRMQLevVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
14-62 |
1.95e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 45.15 E-value: 1.95e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1002242100 14 IEVSALQFDYdGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:PRK13548 3 LEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG 50
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
37-77 |
2.17e-05 |
|
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: 44.16 E-value: 2.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1002242100 37 IAPGSRCLLIGANGSGKTTLLKILAGKHMVGGRDVVRVLNG 77
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILING 70
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-62 |
2.37e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 2.37e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1002242100 14 IEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG 557
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-62 |
2.42e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.17 E-value: 2.42e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1002242100 14 IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:PRK13540 2 LDVIELDFDYHDQP-LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG 49
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
34-189 |
2.60e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKHMVGGR-DVVRV-----LNG---SAFHDTQLVCngdlsylggswSRAIgs 104
Cdd:PRK13547 21 SLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGApRGARVtgdvtLNGeplAAIDAPRLAR-----------LRAV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 105 agdVPLQGD----FSAEHMIfgVDGVDP-VRREKLVDLLDIDLQWR--------------MHKVSDGQRRRVQICMGL-- 163
Cdd:PRK13547 88 ---LPQAAQpafaFSAREIV--LLGRYPhARRAGALTHRDGEIAWQalalagatalvgrdVTTLSGGELARVQFARVLaq 162
|
170 180 190
....*....|....*....|....*....|...
gi 1002242100 164 LHPY-------KVLLLDEITVDLDVVTRMDLLD 189
Cdd:PRK13547 163 LWPPhdaaqppRYLLLDEPTAALDLAHQHRLLD 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-241 |
2.78e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.69 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDV--------VRVLNGSAFH--DTQLVcngdlsylgg 96
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMnallipsEGKVYVDGLDTsdeenlwdIRNKAGMVFQnpDNQIV---------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 97 swsrAIGSAGDVPlqgdFSAEHMifgvdGVDPVRREKLVD--LLDIDL-QWRMHK---VSDGQRRRVQICmGLL--HPyK 168
Cdd:PRK13633 100 ----ATIVEEDVA----FGPENL-----GIPPEEIRERVDesLKKVGMyEYRRHAphlLSGGQKQRVAIA-GILamRP-E 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002242100 169 VLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDglESWATD-IAYIQEGELRKSAK----YSDVEELKS 241
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYME--EAVEADrIIVMDSGKVVMEGTpkeiFKEVEMMKK 240
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-239 |
3.71e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.31 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 26 QPPLFARFNLRIAPGSRCLLIGANGSGKT----TLLKIL-AGkhmvggrdvVRVLNGSAFHDTQLVCNGDLsylggswsR 100
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAG---------VRQTAGRVLLDGKPVAPCAL--------R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 101 AIGSAgdVPLQGDFSA--------EHMI-----FGVDGVDPVRREKL--VDLLDIDLQWRMH--KVSDGQRRRVQICMGL 163
Cdd:PRK10418 78 GRKIA--TIMQNPRSAfnplhtmhTHARetclaLGKPADDATLTAALeaVGLENAARVLKLYpfEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002242100 164 LHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGELRKSAkysDVEEL 239
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG---DVETL 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
145-207 |
4.32e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.33 E-value: 4.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 145 RM----HKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTR---MDLLDFFKEECeqrEATIVYATH 207
Cdd:PRK09473 154 RMkmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQaqiMTLLNELKREF---NTAIIMITH 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
33-207 |
4.91e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.55 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 33 FNLRiaPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVrVLNGSAFHdtQLVcngdlSYlggswsraigSA 105
Cdd:PRK10247 28 FSLR--AGEFKLITGPSGCGKSTLLKIVAslisptsGTLLFEGEDIS-TLKPEIYR--QQV-----SY----------CA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 106 GDVPLQGDFSAEHMIF--GVDGVDPVRREKLVDLL-----DIDLQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVD 178
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFpwQIRNQQPDPAIFLDDLErfalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180
....*....|....*....|....*....
gi 1002242100 179 LDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-207 |
7.62e-05 |
|
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: 43.77 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 23 YDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKhmvggrdvvrvlngsafhdtqlvcngDLSYLGGSWSRAI 102
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV--------------------------DKDFNGEARPQPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 103 GSAGDVPLQGDFSAEHMIFGV--DGVDPVRR-------------------EKL-------------VDLLDIDLQ----- 143
Cdd:TIGR03719 68 IKVGYLPQEPQLDPTKTVRENveEGVAEIKDaldrfneisakyaepdadfDKLaaeqaelqeiidaADAWDLDSQleiam 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002242100 144 ---------WRMHKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEeceqREATIVYATH 207
Cdd:TIGR03719 148 dalrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE----YPGTVVAVTH 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-193 |
8.95e-05 |
|
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: 43.52 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFAR----------FNLRIAPGSRCLLIGANGSGKTTL-LKIL-----AGKHMVGGRDVVRvLNG 77
Cdd:COG4172 276 LEARDLKVWFPIKRGLFRRtvghvkavdgVSLTLRRGETLGLVGESGSGKSTLgLALLrlipsEGEIRFDGQDLDG-LSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 78 SAF----HDTQLVC---NGDLSylggswsraigsagdvPLQ--GDFSAE----HMIfGVDGVDpvRREKLVDL-----LD 139
Cdd:COG4172 355 RALrplrRRMQVVFqdpFGSLS----------------PRMtvGQIIAEglrvHGP-GLSAAE--RRARVAEAleevgLD 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002242100 140 IDLQWRM-HKVSDGQRRRVQICMGL-LHPyKVLLLDEITVDLDVVTRMDLLDFFKE 193
Cdd:COG4172 416 PAARHRYpHEFSGGQRQRIAIARALiLEP-KLLVLDEPTSALDVSVQAQILDLLRD 470
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-63 |
9.09e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 9.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002242100 11 RSG---IEVSALQFDYDGQPpLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGK 63
Cdd:PRK11147 314 RSGkivFEMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQ 368
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-243 |
9.97e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 43.14 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTL-------LKILAGKHMVGGRDV---------VRVLNG 77
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLflhfngiLKPTSGEVLIKGEPIkydkkslleVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 78 SAFH--DTQLVcngdlsylggswsrAIGSAGDVPlqgdFSAEHMIFGVDGVDPVRREKL--VDLLDIDLQwRMHKVSDGQ 153
Cdd:PRK13639 82 IVFQnpDDQLF--------------APTVEEDVA----FGPLNLGLSKEEVEKRVKEALkaVGMEGFENK-PPHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 154 RRRVQICmGLL--HPyKVLLLDEITVDLD---VVTRMDLLdffkEECEQREATIVYATHIFDGLESWATDIAYIQEGELR 228
Cdd:PRK13639 143 KKRVAIA-GILamKP-EIIVLDEPTSGLDpmgASQIMKLL----YDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
250
....*....|....*....
gi 1002242100 229 KSAK----YSDVEELKSAK 243
Cdd:PRK13639 217 KEGTpkevFSDIETIRKAN 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
34-176 |
1.01e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.47 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKH-------MVGGRDVvrvlngsAFHDTQ---------------LVcnGDL 91
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYqpdsgeiLLDGEPV-------RFRSPRdaqaagiaiihqelnLV--PNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 92 S-----YLGgswsRAIGSAGDVplqgDFSAEHmifgvdgvdpvRR-EKLVDLLDIDLQWRMhKVSD---GQRRRVQICMG 162
Cdd:COG1129 95 SvaeniFLG----REPRRGGLI----DWRAMR-----------RRaRELLARLGLDIDPDT-PVGDlsvAQQQLVEIARA 154
|
170
....*....|....
gi 1002242100 163 LLHPYKVLLLDEIT 176
Cdd:COG1129 155 LSRDARVLILDEPT 168
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
34-62 |
1.09e-04 |
|
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: 42.42 E-value: 1.09e-04
10 20
....*....|....*....|....*....
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLAG 60
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-245 |
1.13e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 43.29 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQ-FDYDGQP---PLfarfNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdvvrVLN--GSafhdtqLVC 87
Cdd:PRK11174 350 IEAEDLEiLSPDGKTlagPL----NFTLPAGQRIALVGPSGAGKTSLLNALLG-----------FLPyqGS------LKI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 88 NG-DLSYLG-GSWSRAIGSAGDVP-----------LQGDFSA-EHMIFGVdgvdpVRR-------EKLVDLLDIDLQWRM 146
Cdd:PRK11174 409 NGiELRELDpESWRKHLSWVGQNPqlphgtlrdnvLLGNPDAsDEQLQQA-----LENawvseflPLLPQGLDTPIGDQA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 147 HKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQReaTIVYATHIFDGLESWATdIAYIQEGE 226
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQ-IWVMQDGQ 560
|
250
....*....|....*....
gi 1002242100 227 LRKSAKYsdvEELKSAKNL 245
Cdd:PRK11174 561 IVQQGDY---AELSQAGGL 576
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-236 |
1.15e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.77 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQPPL--FARFNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdvvrvlngsAFHDTQLVCNGDL 91
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDG----------------LFEEFEGKVKIDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 92 SYLGGS--WS--RAIGSAGDVP---LQGDFSAEHMIFGVDGvDPVRREKLVDLLD--------IDLQWRM-HKVSDGQRR 155
Cdd:PRK13642 69 ELLTAEnvWNlrRKIGMVFQNPdnqFVGATVEDDVAFGMEN-QGIPREEMIKRVDeallavnmLDFKTREpARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 156 RVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDglESWATD-IAYIQEGELRKSAKYS 234
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLD--EAASSDrILVMKAGEIIKEAAPS 225
|
..
gi 1002242100 235 DV 236
Cdd:PRK13642 226 EL 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
34-226 |
1.33e-04 |
|
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: 42.07 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKhmvggrdvVRVLNGSAFHdtqlvcNGDLSYlggswsraigsagdVP---- 109
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGE--------LEKLSGSVSV------PGSIAY--------------VSqepw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 110 LQGDFSAEHMIFGVDgVDPVRREKLVDL--LDIDLQwRMHK------------VSDGQRRRVQICMGLLHPYKVLLLDEI 175
Cdd:cd03250 77 IQNGTIRENILFGKP-FDEERYEKVIKAcaLEPDLE-ILPDgdlteigekginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002242100 176 TVDLDVVTRMDLLdffkEECEQ----REATIVYATHIFDGLESwATDIAYIQEGE 226
Cdd:cd03250 155 LSAVDAHVGRHIF----ENCILglllNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
149-226 |
1.61e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 42.34 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002242100 149 VSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGE 226
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-62 |
1.73e-04 |
|
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: 42.10 E-value: 1.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1002242100 14 IEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:cd03261 1 IELRGLTKSFGGRTVL-KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG 48
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
33-207 |
1.83e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 42.32 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 33 FNLRIAPGSRCLLIGANGSGKTTLLKILAGkhmvggrdvvrvlngsaFHDtqlVCNGDLsYLGGSwsraigSAGDVP--- 109
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAG-----------------LED---ITSGDL-FIGEK------RMNDVPpae 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 110 -----------LQGDFS-AEHMIFGVD--GVDPVRREKLV----DLLDID--LQWRMHKVSDGQRRRVQICMGLLHPYKV 169
Cdd:PRK11000 75 rgvgmvfqsyaLYPHLSvAENMSFGLKlaGAKKEEINQRVnqvaEVLQLAhlLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002242100 170 LLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTH 192
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
34-62 |
1.96e-04 |
|
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: 41.89 E-value: 1.96e-04
10 20
....*....|....*....|....*....
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISG 51
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-247 |
2.50e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 41.57 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 45 LIGANGSGKTTLLKILAgkhmvggrdvvRVLNgsaFHDTQLVCNGDLSYLGGSWSR--AIGSAGDVPL--QGDFSAEHMI 120
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLN-----------RLIE---IYDSKIKVDGKVLYFGKDIFQidAIKLRKEVGMvfQQPNPFPHLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 121 FGVDGVDPVRREKLVD-----------LLDIDLQWRMH--------KVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDV 181
Cdd:PRK14246 107 IYDNIAYPLKSHGIKEkreikkiveecLRKVGLWKEVYdrlnspasQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002242100 182 VTRMDLLDFFKEecEQREATIVYATHIFDGLESWATDIAYIQEGELRKSAKYSDVeeLKSAKNLLS 247
Cdd:PRK14246 187 VNSQAIEKLITE--LKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI--FTSPKNELT 248
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-227 |
2.66e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.94 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDVVRVLNGsafhDTQLVCNGDLSYLGGSWsrAIGSAG 106
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLnrlieptRGQVLIDGVDIAKISDA----ELREVRRKKIAMVFQSF--ALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 107 DVPLQGDFSAEhmIFGVDGVDpvRREKLVDLL-DIDLQWRMH----KVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDV 181
Cdd:PRK10070 122 TVLDNTAFGME--LAGINAEE--RREKALDALrQVGLENYAHsypdELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002242100 182 VTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGEL 227
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
148-227 |
2.92e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 41.69 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 148 KVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGEL 227
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
33-62 |
3.80e-04 |
|
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: 40.59 E-value: 3.80e-04
10 20 30
....*....|....*....|....*....|
gi 1002242100 33 FNLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMG 48
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-73 |
4.19e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 40.84 E-value: 4.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002242100 14 IEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVR 73
Cdd:COG4604 2 IEIKNVSKRYGGKVVL-DDVSLTIPKGGITALIGPNGAGKSTLLSMISrllppdsGEVLVDGLDVAT 67
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-180 |
4.36e-04 |
|
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: 40.99 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDGQP--PLFARFNLRIAPGSRCLLIGANGSGKTTLLKIL-------AGKHMVGGRDvVRVLNgsafhdtq 84
Cdd:cd03249 1 IEFKNVSFRYPSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLDGVD-IRDLN-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 85 lvcngdLSYLggswSRAIGSAGDVPLQGDFS-AEHMIFGVDGVDPVRRE-------------KLVDLLDIDLQWRMHKVS 150
Cdd:cd03249 72 ------LRWL----RSQIGLVSQEPVLFDGTiAENIRYGKPDATDEEVEeaakkanihdfimSLPDGYDTLVGERGSQLS 141
|
170 180 190
....*....|....*....|....*....|
gi 1002242100 151 DGQRRRVQICMGLLHPYKVLLLDEITVDLD 180
Cdd:cd03249 142 GGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-62 |
4.99e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 4.99e-04
10 20
....*....|....*....|....*...
gi 1002242100 35 LRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:PRK10636 333 LNLVPGSRIGLLGRNGAGKSTLIKLLAG 360
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
34-61 |
6.94e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 6.94e-04
10 20
....*....|....*....|....*...
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILA 61
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALR 42
|
|
| Arl9_Arfrp2_like |
cd04162 |
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ... |
44-176 |
7.64e-04 |
|
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.
Pssm-ID: 133362 [Multi-domain] Cd Length: 164 Bit Score: 39.35 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 44 LLIGANGSGKTTLLKILAGKhmvggrdvvRVLNGSA----FHDTQLVCNG---DLSYLGGS------WSRAIgSAGDVpl 110
Cdd:cd04162 3 LVLGLDGAGKTSLLHSLSSE---------RSLESVVpttgFNSVAIPTQDaimELLEIGGSqnlrkyWKRYL-SGSQG-- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 111 qgdfsaehMIFGVDGVD----PVRREKLVDLLDIDLQWRMHKVSDGQRRRVQICMGLLHPYkvLLLDEIT 176
Cdd:cd04162 71 --------LIFVVDSADserlPLARQELHQLLQHPPDLPLVVLANKQDLPAARSVQEIHKE--LELEPIA 130
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-207 |
8.53e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.54 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAGKHM-------VGGRDVVRVL------NGSAFHDTQLVCNGDLSYLGGSWsr 100
Cdd:PRK09700 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEptkgtitINNINYNKLDhklaaqLGIGIIYQELSVIDELTVLENLY-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 101 aigsAGDVPLQgdfsaehMIFGVDGVD----PVRREKLVDLLDI--DLQWRMHKVSDGQRRRVQICMGLLHPYKVLLLDE 174
Cdd:PRK09700 103 ----IGRHLTK-------KVCGVNIIDwremRVRAAMMLLRVGLkvDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190
....*....|....*....|....*....|...
gi 1002242100 175 ITVDLdVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:PRK09700 172 PTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
34-250 |
1.11e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 39.99 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLlkilagkhmvggrdvVRVLNGSAFHDTQLVCNGDLSYLGG--------SWSRAIGSA 105
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTM---------------IQLTNGLIISETGQTIVGDYAIPANlkkikevkRLRKEIGLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 106 GDVP--------LQGDFSAEHMIFGVDGVDPVRR-EKLVDLLDIDLQWRMH---KVSDGQRRRVQICMGLLHPYKVLLLD 173
Cdd:PRK13645 96 FQFPeyqlfqetIEKDIAFGPVNLGENKQEAYKKvPELLKLVQLPEDYVKRspfELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002242100 174 EITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFDGLESWATDIAYIQEGE-LRKSAKYsdveELKSAKNLLSVVE 250
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKvISIGSPF----EIFSNQELLTKIE 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
34-207 |
1.56e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 39.62 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 34 NLRIAPGS-RCLLiGANGSGKTTLLKILAGKH-------MVGGRDVvrvlngsAFHDTQlvcngdlsylggswsRAIgSA 105
Cdd:COG3845 25 SLTVRPGEiHALL-GENGAGKSTLMKILYGLYqpdsgeiLIDGKPV-------RIRSPR---------------DAI-AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 106 G---------DVPlqgDFS-AEHMIFGVDGVDPVR------REKLVDL-----LDIDLQWRMHKVSDGQRRRVQICMGLL 164
Cdd:COG3845 81 GigmvhqhfmLVP---NLTvAENIVLGLEPTKGGRldrkaaRARIRELserygLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002242100 165 HPYKVLLLDEIT-------VDldvvtrmDLLDFFKEECEQrEATIVYATH 207
Cdd:COG3845 158 RGARILILDEPTavltpqeAD-------ELFEILRRLAAE-GKSIIFITH 199
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-210 |
1.65e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 39.33 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 14 IEVSALQFDYDG--QPPLFARFNLRIAPGSRCLLIGANGSGKTTllkilagkhmvggrdVVRVLNGSAFHDT-QLVCNGD 90
Cdd:PRK13650 5 IEVKNLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKST---------------TVRLIDGLLEAESgQIIIDGD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 91 LSYLGGSWS--RAIGSAGDVP---LQGDFSAEHMIFGVD--GVDPVR-REKLVDLLDI----DLQWRM-HKVSDGQRRRV 157
Cdd:PRK13650 70 LLTEENVWDirHKIGMVFQNPdnqFVGATVEDDVAFGLEnkGIPHEEmKERVNEALELvgmqDFKEREpARLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002242100 158 QICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATHIFD 210
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD 202
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
130-207 |
1.70e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.34 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 130 RREKLVDLLDI----DLQWRM----HKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREAT 201
Cdd:PRK11022 127 RRQRAIDLLNQvgipDPASRLdvypHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMA 206
|
....*.
gi 1002242100 202 IVYATH 207
Cdd:PRK11022 207 LVLITH 212
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
34-62 |
2.11e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.85 E-value: 2.11e-03
10 20
....*....|....*....|....*....
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:CHL00131 27 NLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
23-57 |
2.12e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 2.12e-03
10 20 30
....*....|....*....|....*....|....*
gi 1002242100 23 YDGQPplfarfnLRIAPGSRCLLIGANGSGKTTLL 57
Cdd:pfam13555 12 FDGHT-------IPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
148-241 |
2.28e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 38.95 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 148 KVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQrEATIVYATHIFDGLESWATDIAYIQEGEL 227
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
90
....*....|....
gi 1002242100 228 RKSAKysdVEELKS 241
Cdd:NF000106 223 IADGK---VDELKT 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
121-236 |
2.71e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 38.70 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 121 FGVDGVDPVRREKLVDLLDID-LQWRM-HKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQR 198
Cdd:PRK11144 99 YGMAKSMVAQFDKIVALLGIEpLLDRYpGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
90 100 110
....*....|....*....|....*....|....*...
gi 1002242100 199 EATIVYATHIFDGLESWATDIAYIQEGELRKSAKYSDV 236
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
44-61 |
3.20e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.52 E-value: 3.20e-03
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
44-61 |
3.52e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.44 E-value: 3.52e-03
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-62 |
3.66e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 3.66e-03
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
147-207 |
4.09e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 38.68 E-value: 4.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002242100 147 HKVSDGQRRRVQICMGLLHPYKVLLLDEITVDLDVVTRMDLLDFFKEECEQREATIVYATH 207
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITH 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-60 |
4.57e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 37.81 E-value: 4.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1002242100 12 SGIEVSALQFDYDGQPPLFArFNLRIAPGSRCLLIGANGSGKTTLLKIL 60
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHG-IDLEVKPGEVVAIIGPSGSGKTTLLRCI 49
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-241 |
7.20e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 38.18 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 21 FDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAGKHmvggrdvvrvlngSAFHDTQLVCNGDLSYLGG-SWS 99
Cdd:PLN03130 624 WDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL-------------PPRSDASVVIRGTVAYVPQvSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 100 raigsagdvplqgdFSA---EHMIFGVDgVDPVRREKLVDL--LDIDLQW-----------RMHKVSDGQRRRVQICMGL 163
Cdd:PLN03130 691 --------------FNAtvrDNILFGSP-FDPERYERAIDVtaLQHDLDLlpggdlteigeRGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002242100 164 LHPYKVLLLDEITVDLDV-VTRMDLLDFFKEECEQReaTIVYATHIFDGLeSWATDIAYIQEGELRKSAKYsdvEELKS 241
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAhVGRQVFDKCIKDELRGK--TRVLVTNQLHFL-SQVDRIILVHEGMIKEEGTY---EELSN 828
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
34-62 |
7.38e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 37.60 E-value: 7.38e-03
10 20
....*....|....*....|....*....
gi 1002242100 34 NLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
14-74 |
8.25e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 37.23 E-value: 8.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002242100 14 IEVSALQFDYDGQPPLfARFNLRIAPGSRCLLIGANGSGKTTLLKILA-------GKHMVGGRDVVRV 74
Cdd:PRK09452 15 VELRGISKSFDGKEVI-SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAgfetpdsGRIMLDGQDITHV 81
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-62 |
9.24e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 37.39 E-value: 9.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002242100 4 GEDEGWRRSG-IEVSALQFDYDGQPPLFARFNLRIAPGSRCLLIGANGSGKTTLLKILAG 62
Cdd:PRK10790 330 GNDDRPLQSGrIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG 389
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
147-194 |
9.71e-03 |
|
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: 37.36 E-value: 9.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1002242100 147 HKVSDGQRRRVQICMGLL-HPyKVLLLDEITVDLDVVTR---MDLLDFFKEE 194
Cdd:COG4172 155 HQLSGGQRQRVMIAMALAnEP-DLLIADEPTTALDVTVQaqiLDLLKDLQRE 205
|
|
| |
