|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
3.30e-103 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 297.73 E-value: 3.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATNLVPFLTVKQQFTL---LKKKNKNVMsNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALpllLAGVSRKER-RERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-217 |
4.86e-92 |
|
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: 268.97 E-value: 4.86e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIGFILQATNLVPFLTVKQ--QFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPS 159
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALEnvELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 160 IILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-215 |
2.88e-69 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 212.22 E-value: 2.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQATNLVPFLTVKQqftllkkknkNVM-----------------SNEDYQ---QLMSQLGLTSLLNKLPSEI 140
Cdd:COG3638 79 R-RRIGMIFQQFNLVPRLSVLT----------NVLagrlgrtstwrsllglfPPEDREralEALERVGLADKAYQRADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 141 SGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQvDLARRYADRIIGLRDG 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
3.75e-66 |
|
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: 203.51 E-value: 3.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKQKaLAK 79
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLArAILG-LLKPTSGSIIFDGKDLLKLSRR-LRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRMSEIGFILQ--ATNLVPFLTVKQQFT----LLKKKNKNVMSNEDYQQLMSQLGL-TSLLNKLPSEISGGQKQRVAIAK 152
Cdd:cd03257 79 IRRKEIQMVFQdpMSSLNPRMTIGEQIAeplrIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 153 ALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERL-KAYCDRSYHMKDG 215
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVvAKIADRVAVMYAG 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
6.27e-63 |
|
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: 195.73 E-value: 6.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATNLVPFLTVKQqftllkkknkNVM------SNEDYQQ----LMSQLGLTSLLNKLPSEISGGQKQRVAI 150
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALE----------NVMlplelaGRRDARAraraLLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 151 AKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-217 |
1.42e-62 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 194.50 E-value: 1.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:COG2884 1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSeIGFILQATNLVPFLTVKQqftllkkknkNVM--------SNEDYQQ----LMSQLGLTSLLNKLPSEISGGQKQRV 148
Cdd:COG2884 78 RRR-IGVVFQDFRLLPDRTVYE----------NVAlplrvtgkSRKEIRRrvreVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 149 AIAKALYTNPSIILADEPTAALDTENAIEVIKILRDqAKKRKKACIIVTHDERL-KAYCDRSYHMKDGVL 217
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEE-INRRGTTVLIATHDLELvDRMPKRVLELEDGRL 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-215 |
1.28e-61 |
|
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: 192.78 E-value: 1.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVR 81
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQATNLVPFLTVKQQ--FTLLKKKNK-----NVMSNEDYQ---QLMSQLGLTSLLNKLPSEISGGQKQRVAIA 151
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENvlSGRLGRRSTwrslfGLFPKEEKQralAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 152 KALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERL-KAYCDRSYHMKDG 215
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDG 221
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-217 |
1.75e-60 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 189.10 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATNLVPFLTVKQQFT---LLKKKNKNvMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAmplLIGKKSVK-EAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-217 |
4.03e-60 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 187.92 E-value: 4.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVR 81
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSeIGFILQATNLVPFLTVKQ--QFTL-LKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:TIGR02982 82 RR-IGYIFQAHNLLGFLTARQnvQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 159 SIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-215 |
3.89e-59 |
|
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: 193.97 E-value: 3.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRN-IEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAK 79
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGgVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRmSEIGFILQ--ATNLVPFLTVKQQ--FTLlkkKNKNVMSNEDYQ----QLMSQLGL-TSLLNKLPSEISGGQKQRVAI 150
Cdd:COG1123 340 LR-RRVQMVFQdpYSSLNPRMTVGDIiaEPL---RLHGLLSRAERRervaELLERVGLpPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 151 AKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERL-KAYCDRSYHMKDG 215
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVvRYIADRVAVMYDG 481
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-217 |
6.67e-59 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 185.78 E-value: 6.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKQKALA- 78
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLrALAG-LERPWSGEVTFDGRPVTRRRRKAFRr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KVRMseigfILQ--ATNLVPFLTVKQQ----FTLLKKKNknvmSNEDYQQLMSQLGLT-SLLNKLPSEISGGQKQRVAIA 151
Cdd:COG1124 80 RVQM-----VFQdpYASLHPRHTVDRIlaepLRIHGLPD----REERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 152 KALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAY-CDRSYHMKDGVL 217
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-215 |
1.29e-58 |
|
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: 185.25 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKQKALAK 79
Cdd:COG1120 1 MLEAENLSVGY--GGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLrALAG-LLKPSSGEVLLDGRDLASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VrmseIGFILQATNLVPFLTVKQ--------QFTLLKKknknvMSNEDYQ---QLMSQLGLTSLLNKLPSEISGGQKQRV 148
Cdd:COG1120 76 R----IAYVPQEPPAPFGLTVRElvalgrypHLGLFGR-----PSAEDREaveEALERTGLEHLADRPVDELSGGERQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 149 AIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKA-YCDRSYHMKDG 215
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAArYADRLVLLKDG 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-208 |
9.42e-58 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 185.67 E-value: 9.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFIlqatnlvpFltvkQQFTLLKKKN--KNV--------MSNEDYQQ----LMSQLGLTSLLNKLPSEISGGQKQ 146
Cdd:COG1135 81 R-RKIGMI--------F----QHFNLLSSRTvaENValpleiagVPKAEIRKrvaeLLELVGLSDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 147 RVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDR 208
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmDVVRRICDR 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-199 |
1.40e-57 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 182.12 E-value: 1.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtMKQKALAKV 80
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQATNLVPFLTVKQQFTL----LKKKNKNVmSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYT 156
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLapikVKKMSKAE-AEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 579537805 157 NPSIILADEPTAALDTENAIEVIKILRDQAkKRKKACIIVTHD 199
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLA-KEGMTMVVVTHE 195
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-217 |
2.57e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 180.40 E-value: 2.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVtkSFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMkqkALAKVR 81
Cdd:COG4619 1 LELEGL--SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQatnlVPFL---TVKQQFTLLKKKNKNVMSNEDYQQLMSQLGLT-SLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:COG4619 74 -RQVAYVPQ----EPALwggTVRDNLPFPFQLRERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDpEQIERVADRVLTLEAGRL 209
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-215 |
6.31e-57 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 180.57 E-value: 6.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQATNLVPFLTVKQQF---TLLKKKNKNVM----SNEDYQ---QLMSQLGLTSLLNKLPSEISGGQKQRVAI 150
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVlhgRLGYKPTWRSLlgrfSEEDKEralSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 151 AKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQvDLAKKYADRIVGLKAG 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-199 |
1.57e-55 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 177.59 E-value: 1.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQkalakv 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmsEIGFILQATNLVPFLTVKQqftllkkknkNVM--------SNEDY----QQLMSQLGLTSLLNKLPSEISGGQKQRV 148
Cdd:COG1116 81 ---DRGVVFQEPALLPWLTVLD----------NVAlglelrgvPKAERreraRELLELVGLAGFEDAYPHQLSGGMRQRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 579537805 149 AIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-217 |
1.79e-55 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 176.62 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQATNLVPFLTVKQQFTL------LKKKNKNVMSNEdyqqLMSQLGLTSLLNKLPSEISGGQKQRVAIAKAL 154
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALpleiagVPKAEIEERVLE----LLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 155 YTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEV 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-217 |
1.00e-54 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 174.25 E-value: 1.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqKALAKVR 81
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK-KNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQATNLVPFLTVKQQFTLLKKKNKNvMSNEDYQ----QLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKVKG-MSKAEAEeralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAKKrKKACIIVTHDERL-KAYCDRSYHMKDGVL 217
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-217 |
2.21e-54 |
|
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: 174.01 E-value: 2.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKQKALAK 79
Cdd:COG1127 5 MIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLkLIIG-LLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRMsEIGFILQATNLVPFLTVKQ--QFTLLKKKNknvMSNEDYQQL----MSQLGLTSLLNKLPSEISGGQKQRVAIAKA 153
Cdd:COG1127 80 LRR-RIGMLFQGGALFDSLTVFEnvAFPLREHTD---LSEAEIRELvlekLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 154 LYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-208 |
3.86e-54 |
|
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: 176.01 E-value: 3.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTF-LTMAGALQTP--TSGHILINNQDITTMKQKAL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 78 AKVRMSEIGFILQ--ATNLVPFLTVKQQFT-LLKKKNKnvMSNEDYQQ----LMSQLGLT---SLLNKLPSEISGGQKQR 147
Cdd:COG0444 81 RKIRGREIQMIFQdpMTSLNPVMTVGDQIAePLRIHGG--LSKAEAREraieLLERVGLPdpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 148 VAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAY-CDR 208
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADR 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-215 |
1.62e-53 |
|
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: 170.73 E-value: 1.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 3 KFENVTKSFKDGNRNieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvrm 82
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 sEIGFILQATN--LVpFLTVKQQ--FTLlkkKNKNVMSNEDYQ---QLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALY 155
Cdd:cd03225 76 -KVGLVFQNPDdqFF-GPTVEEEvaFGL---ENLGLPEEEIEErveEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 156 TNPSIILADEPTAALDTENAIEVIKILRDqAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEGKTIIIVTHDlDLLLELADRVIVLEDG 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-220 |
1.88e-53 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 171.54 E-value: 1.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATNLVPFLTVKQQFT--LLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAmpLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 159 SIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVLNLE 220
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-215 |
1.76e-52 |
|
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: 166.98 E-value: 1.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVR 81
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 msEIGFILQATNLVPFLTVKQqftllkkknkNVMsnedyqqlmsqLGLtsllnklpseiSGGQKQRVAIAKALYTNPSII 161
Cdd:cd03229 77 --RIGMVFQDFALFPHLTVLE----------NIA-----------LGL-----------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 162 LADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDlDEAARLADRVVVLRDG 177
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-208 |
3.41e-52 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 167.41 E-value: 3.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRMSE 84
Cdd:TIGR03608 2 KNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 85 IGFILQATNLVPFLTVKQQFTL---LKKKNKNVMSNEDYQQLmSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSII 161
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLglkYKKLSKKEKREKKKEAL-EKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 579537805 162 LADEPTAALDTENAIEVIKILRDQaKKRKKACIIVTHDERLKAYCDR 208
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPEVAKQADR 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-199 |
7.95e-52 |
|
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: 166.88 E-value: 7.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTmkqkalakvR 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIGFILQATNLVPFLTVKQqftllkkknkNVM------------SNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVA 149
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLD----------NVAlglelqgvpkaeARERAEELLELVGLSGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579537805 150 IAKALYTNPSIILADEPTAALD--TENAI--EVIKILRdqakKRKKACIIVTHD 199
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDalTREQLqeELLDIWR----ETGKTVLLVTHD 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-217 |
8.72e-52 |
|
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: 165.30 E-value: 8.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKQKALAKvrms 83
Cdd:cd03214 3 ENLSVGY--GGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLkTLAG-LLKPSSGEILLDGKDLASLSPKELAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 84 EIGFILQAtnlvpfltvkqqftllkkknknvmsnedyqqlMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILA 163
Cdd:cd03214 74 KIAYVPQA--------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 164 DEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKA-YCDRSYHMKDGVL 217
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAArYADRVILLKDGRI 176
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-215 |
9.17e-52 |
|
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: 167.12 E-value: 9.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkQKALAKVR 81
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQatN----LVpFLTVKQ--QFTLlkkKNKNVmSNEDY----QQLMSQLGLTSLLNKLPSEISGGQKQRVAIA 151
Cdd:COG1122 75 -RKVGLVFQ--NpddqLF-APTVEEdvAFGP---ENLGL-PREEIrervEEALELVGLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 152 KALYTNPSIILADEPTAALDTENAIEVIKILRDqAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDlDLVAELADRVIVLDDG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-215 |
6.64e-51 |
|
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: 164.23 E-value: 6.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKqkalakV 80
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLrLIAG-LERPDSGEILIDGRDVTGVP------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATNLVPFLTVKQ--QFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:cd03259 70 ERRNIGMVFQDYALFPHLTVAEniAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 159 SIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD--ERLkAYCDRSYHMKDG 215
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDqeEAL-ALADRIAVMNEG 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-208 |
7.56e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.85 E-value: 7.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvr 81
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mseIGFILQATNLVPFLTVKQQFTL---LKKKNKNVmSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:COG1131 75 ---IGYVPQEPALYPDLTVRENLRFfarLYGLPRKE-ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579537805 159 SIILADEPTAALDTENAIEVIKILRDQAkKRKKACIIVTHD----ERLkayCDR 208
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYleeaERL---CDR 200
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-225 |
2.60e-49 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 161.18 E-value: 2.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKv 80
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmseIGFILQATNLVPFLTVKQQFTLLKKKNKNVMS--NEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:COG4555 76 ----IGVLPDERGLYDRLTVRENIRYFAELYGLFDEelKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 159 SIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVLnLENETVE 225
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHImQEVEALCDRVVILHKGKV-VAQGSLD 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.27e-48 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 166.23 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRniEAVKDTNFEINKGDIIALVGPSGSGKSTF-LTMAGALQTP--TSGHILINNQDITTMKqkal 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLaLALMGLLPHGgrISGEVLLDGRDLLELS---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 78 AKVRMSEIGFILQ--ATNLVPfLTVKQQ--FTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKA 153
Cdd:COG1123 78 EALRGRRIGMVFQdpMTQLNP-VTVGDQiaEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 154 LYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVLNLENETVE 225
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-199 |
1.33e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 162.57 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTM-AGaLQTPTSGHILINNQDITTMK-QKala 78
Cdd:COG3842 5 ALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMiAG-FETPDSGRILLDGRDVTGLPpEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 kvRmsEIGFILQATNLVPFLTVKQqftllkkknkNV--------MSNEDYQQ----LMSQLGLTSLLNKLPSEISGGQKQ 146
Cdd:COG3842 77 --R--NVGMVFQDYALFPHLTVAE----------NVafglrmrgVPKAEIRArvaeLLELVGLEGLADRYPHQLSGGQQQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 579537805 147 RVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-215 |
2.51e-48 |
|
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: 156.39 E-value: 2.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVr 81
Cdd:cd03228 1 IEFKNVSFSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mseIGFILQAtnlvPFLtvkqqFtllkkkNKNVMSNedyqqlmsqlgltsLLnklpseiSGGQKQRVAIAKALYTNPSII 161
Cdd:cd03228 78 ---IAYVPQD----PFL-----F------SGTIREN--------------IL-------SGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579537805 162 LADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-215 |
3.66e-48 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 167.21 E-value: 3.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATNLVPFLTVKQQFT-------LLKKKNKnvmsnEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKA 153
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEvpavyagLERKQRL-----LRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 154 LYTNPSIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILH-QLRDRGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-215 |
4.08e-48 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 157.41 E-value: 4.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdgNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:TIGR02673 1 MIEFHNVSKAY---PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSeIGFILQATNLVPFLTVKQQ--FTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENvaLPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 159 SIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHDERL-KAYCDRSYHMKDG 215
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLK-RLNKRGTTVIVATHDLSLvDRVAHRVIILDDG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-217 |
1.26e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 159.97 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSeIGFILQATNLVPFLTVKQQFTL-LKKKNknvMSNEDYQQLMSQL----GLTSLLNKLPSEISGGQKQRVAIAKALY 155
Cdd:PRK11153 81 RRQ-IGMIFQHFNLLSSRTVFDNVALpLELAG---TPKAEIKARVTELlelvGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 156 TNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEmDVVKRICDRVAVIDAGRL 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-215 |
2.47e-47 |
|
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: 155.74 E-value: 2.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRmS 83
Cdd:cd03261 3 LRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 84 EIGFILQATNLVPFLTVKQ--QFTLLKKKNknvMSNEDYQQL----MSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:cd03261 78 RMGMLFQSGALFDSLTVFEnvAFPLREHTR---LSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-215 |
1.61e-46 |
|
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: 154.00 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkQKALAKVR 81
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR---EQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSeIGFILQATNLVPFLTVKQQFTLLKKKNKnvMSNEDYQQ----LMSQLGL--TSLLNKLPSEISGGQKQRVAIAKALY 155
Cdd:cd03295 75 RK-IGYVIQQIGLFPHMTVEENIALVPKLLK--WPKEKIREradeLLALVGLdpAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 156 TNPSIILADEPTAALDTenaievikILRDQ--------AKKRKKACIIVTHD--ERLKaYCDRSYHMKDG 215
Cdd:cd03295 152 ADPPLLLMDEPFGALDP--------ITRDQlqeefkrlQQELGKTIVFVTHDidEAFR-LADRIAIMKNG 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-202 |
3.41e-46 |
|
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: 152.18 E-value: 3.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVR 81
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSeIGFILQATNLVPFLTVKQQ--FTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPS 159
Cdd:cd03292 78 RK-IGVVFQDFRLLPDRNVYENvaFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 579537805 160 IILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHDERL 202
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLK-KINKAGTTVVVATHAKEL 198
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-217 |
3.53e-46 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 151.01 E-value: 3.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGnrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKAlakvr 81
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIGFILQATNLVPFLTVKQQFTLlkkknknvmsnedyqqlmsqlgltsllnklpseiSGGQKQRVAIAKALYTNPSII 161
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENLKL----------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 162 LADEPTAALDTENAIEVIKILRDQaKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-215 |
7.65e-46 |
|
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: 149.70 E-value: 7.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 3 KFENVTKSFKDGnrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvrm 82
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 sEIGFILQatnlvpfltvkqqftllkkknknvmsnedyqqlmsqlgltsllnklpseISGGQKQRVAIAKALYTNPSIIL 162
Cdd:cd00267 74 -RIGYVPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579537805 163 ADEPTAALDTENAIEVIKILRDQAKKrKKACIIVTHDERL-KAYCDRSYHMKDG 215
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELaELAADRVIVLKDG 156
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-217 |
1.97e-45 |
|
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: 160.38 E-value: 1.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVtkSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKQKALAkv 80
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLkLLLG-LYEPTSGRILIDGIDLRQIDPASLR-- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmSEIGFILQAtnlvPFL---TVKQQFTLLKKKnknvMSNEDYQQLMSQLGLTSLLNKLP-----------SEISGGQKQ 146
Cdd:COG2274 549 --RQIGVVLQD----VFLfsgTIRENITLGDPD----ATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 147 RVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
5-200 |
2.75e-45 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 150.72 E-value: 2.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkalakVRMSE 84
Cdd:TIGR00968 4 ANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------ARDRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 85 IGFILQATNLVPFLTVKQQ--FTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIIL 162
Cdd:TIGR00968 74 IGFVFQHYALFKHLTVRDNiaFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 579537805 163 ADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDE 200
Cdd:TIGR00968 154 LDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQ 191
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-217 |
7.56e-45 |
|
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: 157.23 E-value: 7.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvR 81
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR-Q 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIG---FILQAT---NLvpfltvkqqftLLKKKNknvMSNEDYQQLMSQLGLTSLLNKLP-----------SEISGGQ 144
Cdd:COG4988 413 IAWVPqnpYLFAGTireNL-----------RLGRPD---ASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 145 KQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRI 549
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-217 |
7.86e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.85 E-value: 7.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNRniEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKQKalak 79
Cdd:COG1121 6 AIELENLTVSY--GGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLkAILG-LLPPTSGTVRLFGKPPRRARRR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 vrmseIGFILQATNL---VPfLTVKQ--------QFTLLKKKNKnvmsnEDYQ---QLMSQLGLTSLLNKLPSEISGGQK 145
Cdd:COG1121 77 -----IGYVPQRAEVdwdFP-ITVRDvvlmgrygRRGLFRRPSR-----ADREavdEALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 146 QRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQaKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-214 |
1.16e-44 |
|
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: 148.01 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDIttmkQKALAK 79
Cdd:COG4133 2 MLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLrILAG-LLPPSAGEVLWNGEPI----RDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRmSEIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPS 159
Cdd:COG4133 73 YR-RRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 160 IILADEPTAALDTENAIEVIKILRDQAkKRKKACIIVTHDErLKAYCDRSYHMKD 214
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHL-ARGGAVLLTTHQP-LELAAARVLDLGD 204
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-199 |
1.38e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 149.45 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKqkalAK 79
Cdd:COG3839 3 SLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLrMIAG-LEDPTSGEILIGGRDVTDLP----PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRMseIGFILQ--AtnLVPFLTVKQ--QFTLlkkKNKNvMSNEDYQQLMSQ----LGLTSLLNKLPSEISGGQKQRVAIA 151
Cdd:COG3839 74 DRN--IAMVFQsyA--LYPHMTVYEniAFPL---KLRK-VPKAEIDRRVREaaelLGLEDLLDRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 152 KALYTNPSIILADEPTAALDTEnaievikiLRDQA--------KKRKKACIIVTHD 199
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAK--------LRVEMraeikrlhRRLGTTTIYVTHD 193
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-199 |
1.67e-43 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 146.39 E-value: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkalAKV 80
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK----VDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RM--SEIGFILQATNLVPfltvkqQFTLLKkknkNVM---------SNEDYQQ----LMSQLGLTSLLNKLPSEISGGQK 145
Cdd:PRK09493 73 RLirQEAGMVFQQFYLFP------HLTALE----NVMfgplrvrgaSKEEAEKqareLLAKVGLAERAHHYPSELSGGQQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579537805 146 QRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKrKKACIIVTHD 199
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHE 195
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-220 |
2.13e-43 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 145.69 E-value: 2.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATNLVPFLTVKQQF---TLLKKKNKNvMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVelpALLRGESSR-QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVLNLE 220
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-217 |
9.40e-43 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 145.09 E-value: 9.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRMSEIGFILQATNLVPFLT 99
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 100 VKQQ--FTLlkkKNKNVMSNEDYQQLMSQL---GLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTEN 174
Cdd:cd03294 119 VLENvaFGL---EVQGVPRAEREERAAEALelvGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 579537805 175 AIEVIKILRDQAKKRKKACIIVTHD--ERLKaYCDRSYHMKDGVL 217
Cdd:cd03294 196 RREMQDELLRLQAELQKTIVFITHDldEALR-LGDRIAIMKDGRL 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-209 |
4.29e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.20 E-value: 4.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNRNIEAvkdtNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMkqkALAK- 79
Cdd:COG3840 1 MLRLDDLTYRY--GDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL---PPAEr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 -VRMseigfILQATNLVPFLTVKQQFTL-----LKkknknvMSNEDYQQLM---SQLGLTSLLNKLPSEISGGQKQRVAI 150
Cdd:COG3840 72 pVSM-----LFQENNLFPHLTVAQNIGLglrpgLK------LTAEQRAQVEqalERVGLAGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 151 AKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRS 209
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDpEDAARIADRV 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-218 |
6.26e-42 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 142.09 E-value: 6.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNrnieaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKalakvr 81
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIGFILQATNLVPFLTVKQ--QFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPS 159
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKniAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 160 IILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVLN 218
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLI 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-217 |
2.03e-41 |
|
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: 147.52 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKS-TFLTMAGALQTP---TSGHILINNQDITTMKQKA 76
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 77 LAKVRMSEIGFILQ--ATNLVPFLTVKQQF--TLLKKKNknvMSNEDYQQ----LMSQLGLT---SLLNKLPSEISGGQK 145
Cdd:COG4172 86 LRRIRGNRIAMIFQepMTSLNPLHTIGKQIaeVLRLHRG---LSGAAARAraleLLERVGIPdpeRRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 146 QRVAIAKALYTNPSIILADEPTAALD-TENAiEVIKILRDQAKKRKKACIIVTHDERL-KAYCDRSYHMKDGVL 217
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDvTVQA-QILDLLKDLQRELGMALLLITHDLGVvRRFADRVAVMRQGEI 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-225 |
5.00e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 141.05 E-value: 5.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRN-IEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQatnlvpF-------LTVK-------QQFTLLKKKNKnvmsnEDYQQLMSQLGLT-SLLNKLPSEISGGQK 145
Cdd:TIGR04521 81 R-KKVGLVFQ------FpehqlfeETVYkdiafgpKNLGLSEEEAE-----ERVKEALELVGLDeEYLERSPFELSGGQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 146 QRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVLNLENETV 224
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIVLDGTPR 228
|
.
gi 579537805 225 E 225
Cdd:TIGR04521 229 E 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-208 |
6.68e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.59 E-value: 6.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFkdGNRNieAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKqkalaKVRMS 83
Cdd:COG1118 6 RNISKRF--GSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLrIIAG-LETPDSGRIVLNGRDLFTNL-----PPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 84 EIGFILQATNLVPFLTVKQ--QFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSII 161
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAEniAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 579537805 162 LADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDeRLKAY--CDR 208
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHD-QEEALelADR 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-168 |
8.17e-41 |
|
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: 136.62 E-value: 8.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKQKALAKvrmsEIGFILQATNLVPFLT 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLkLIAG-LLSPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 100 VKQQ--FTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKL----PSEISGGQKQRVAIAKALYTNPSIILADEPTA 168
Cdd:pfam00005 76 VRENlrLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-217 |
2.11e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 138.73 E-value: 2.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGnrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMK----QKA 76
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 77 LAKVRMSEIGFILQATNLVPFLTVKQQFT---LLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKA 153
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPHRTVLENIIegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 154 LYTNPSIILADEPTAALDTENAIEVIKILRDQAKKrKKACIIVTHDERL-KAYCDRSYHMKDGVL 217
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFaRDVADRAIFMDQGRI 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-217 |
3.23e-40 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 136.89 E-value: 3.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 3 KFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALqTPTSGHILINNQDITTMKQKalakvr 81
Cdd:cd03235 1 EVEDLTVSY--GGHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLkAILGLL-KPTSGSIRVFGKPLEKERKR------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mseIGFILQATNL---VPfLTVKQ-----------QFTLLKKKNKnvmsnEDYQQLMSQLGLTSLLNKLPSEISGGQKQR 147
Cdd:cd03235 70 ---IGYVPQRRSIdrdFP-ISVRDvvlmglyghkgLFRRLSKADK-----AKVDEALERVGLSELADRQIGELSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 148 VAIAKALYTNPSIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRREGMTILVVTHDlGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-200 |
7.10e-40 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 136.70 E-value: 7.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkalakVR 81
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIGFILQATNLVPFLTVKQQ--FTLLKKKNKNVMSNEDYQQLMSQL----GLTSLLNKLPSEISGGQKQRVAIAKALY 155
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNvaFGLRVKPRSERPPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 579537805 156 TNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDE 200
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQ 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-217 |
7.66e-40 |
|
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: 135.89 E-value: 7.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 23 DTNFEINkGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRMSEIGFILQATNLVPFLTVKQ 102
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 103 QFTL-LKKKNKNVMSNEdYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKI 181
Cdd:cd03297 95 NLAFgLKRKRNREDRIS-VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 579537805 182 LRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRL 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-215 |
1.17e-39 |
|
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: 142.98 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNieAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQtPTSGHILINNQDITTMKQKALAKV 80
Cdd:COG4987 334 LELEDVSFRYPGAGRP--VLDGLSLTLPPGERVAIVGPSGSGKSTLLaLLLRFLD-PQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmseIGFILQATNLvpFLTvkqqfTLLKkknkNVM------SNEDYQQLMSQLGLTSLLNKLP-----------SEISGG 143
Cdd:COG4987 411 ----IAVVPQRPHL--FDT-----TLRE----NLRlarpdaTDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 144 QKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDG 545
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-201 |
1.56e-39 |
|
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: 135.48 E-value: 1.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQTP--TSGHILINNQ--DITTMKQka 76
Cdd:cd03234 4 LPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdAISGRVEGGgtTSGQILFNGQprKPDQFQK-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 77 lakvrmsEIGFILQATNLVPFLTVKQ------QFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAI 150
Cdd:cd03234 82 -------CVAYVRQDDILLPGLTVREtltytaILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 579537805 151 AKALYTNPSIILADEPTAALDTENAIEVIKILRDQAkKRKKACIIVTHDER 201
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLA-RRNRIVILTIHQPR 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-217 |
3.63e-39 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 134.55 E-value: 3.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKAlakvr 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIGFILQATNLVPFLTVKQQ---FTLLKKKNKNVMSNEDyQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHlrfYARLKGLPKSEIKEEV-ELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 159 SIILADEPTAALDTENAIEVIKILrdQAKKRKKACIIVTHD----ERLkayCDRSYHMKDGVL 217
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLI--LEVRKGRSIILTTHSmdeaEAL---CDRIAIMSDGKL 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-215 |
4.41e-39 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 133.92 E-value: 4.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFKdgnRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkqkalAKVRMSE 84
Cdd:cd03226 3 ENISFSYK---KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 85 IGFILQATNLVPFL-TVKQQFTLLKKKNKNvmSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILA 163
Cdd:cd03226 73 IGYVMQDVDYQLFTdSVREELLLGLKELDA--GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 579537805 164 DEPTAALDTENAIEVIKILRDQAkKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELA-AQGKAVIVITHDyEFLAKVCDRVLLLANG 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-200 |
5.10e-39 |
|
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: 134.29 E-value: 5.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGnrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMkqkaLAKVR 81
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL----PPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 msEIGFILQATNLVPFLTVKQQ--FTL-LKKKNKNVMsNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:cd03300 73 --PVNTVFQNYALFPHLTVFENiaFGLrLKKLPKAEI-KERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 579537805 159 SIILADEPTAALD----TENAIEvikiLRDQAKKRKKACIIVTHDE 200
Cdd:cd03300 150 KVLLLDEPLGALDlklrKDMQLE----LKRLQKELGITFVFVTHDQ 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-217 |
5.27e-39 |
|
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: 133.92 E-value: 5.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkalAKVR 81
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP----PKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 msEIGFILQATNLVPFLTVKQQ--FTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPS 159
Cdd:cd03301 73 --DIAMVFQNYALYPHMTVYDNiaFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 160 IILADEPTAALDT----ENAIEVIKILRDQakkrKKACIIVTHD--ERLkAYCDRSYHMKDGVL 217
Cdd:cd03301 151 VFLMDEPLSNLDAklrvQMRAELKRLQQRL----GTTTIYVTHDqvEAM-TMADRIAVMNDGQI 209
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-199 |
1.11e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 134.16 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMK------- 73
Cdd:COG4598 8 ALEVRDLHKSFGD----LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 74 ---QKALAKVRmSEIGFILQATNLVPFLTVKQqftllkkknkNVM-------------SNEDYQQLMSQLGLTSLLNKLP 137
Cdd:COG4598 84 padRRQLQRIR-TRLGMVFQSFNLWSHMTVLE----------NVIeapvhvlgrpkaeAIERAEALLAKVGLADKRDAYP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 138 SEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKrKKACIIVTHD 199
Cdd:COG4598 153 AHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHE 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-199 |
1.23e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 133.60 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDI---TTMKQKALAKVRmSEIGFILQATNLV 95
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLR-QKVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 96 PFLTVKQQFT-----LLKKKNKNvmSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAAL 170
Cdd:COG4161 95 PHLTVMENLIeapckVLGLSKEQ--AREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180
....*....|....*....|....*....
gi 579537805 171 DTENAIEVIKILRDQAKKRKKAcIIVTHD 199
Cdd:COG4161 173 DPEITAQVVEIIRELSQTGITQ-VIVTHE 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-208 |
2.66e-38 |
|
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: 132.56 E-value: 2.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAkvR 81
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSeIGFILQATNLVPFLTV------------KQQFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVA 149
Cdd:cd03219 75 LG-IGRTFQIPRLFPELTVlenvmvaaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILRDqAKKRKKACIIVTHD-ERLKAYCDR 208
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRE-LRERGITVLLVEHDmDVVMSLADR 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-215 |
4.57e-38 |
|
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: 131.46 E-value: 4.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 28 INKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMkQKALAKVRMseigfILQATNLVPFLTVKQQFTLl 107
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA-PPADRPVSM-----LFQENNLFAHLTVEQNVGL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 108 kKKNKNVMSNEDYQQLM----SQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILR 183
Cdd:cd03298 94 -GLSPGLKLTAEDRQAIevalARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|...
gi 579537805 184 DQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:cd03298 173 DLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNG 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-215 |
1.21e-37 |
|
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: 130.39 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGnrniEAVKDTNFEINKGdIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvr 81
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mseIGFILQATNLVPFLTVKQQ---FTLLKKKNKnvmSNEDY--QQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYT 156
Cdd:cd03264 74 ---IGYLPQEFGVYPNFTVREFldyIAWLKGIPS---KEVKArvDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 157 NPSIILADEPTAALDTENAIEVIKILRDQAKKRkkaCIIV-THD-ERLKAYCDRSYHMKDG 215
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDR---IVILsTHIvEDVESLCNQVAVLNKG 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-215 |
1.27e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 137.60 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALakvr 81
Cdd:COG1132 340 IEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIGFILQAtnlvPFL---TVKQqftllkkknkNV-MSNEDY--QQLMS---QLGLTSLLNKLP-----------SEIS 141
Cdd:COG1132 413 RRQIGVVPQD----TFLfsgTIRE----------NIrYGRPDAtdEEVEEaakAAQAHEFIEALPdgydtvvgergVNLS 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 142 GGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHdeRLK--AYCDRSYHMKDG 215
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAH--RLStiRNADRILVLDDG 550
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-215 |
1.70e-37 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 131.40 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDitTMKQKALAKVR 81
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQ-------ATnlvpflTVKQQ--FTLlkkKNKNVMSNEDYQ---QLMSQLGLTSLLNKLPSEISGGQKQRVA 149
Cdd:TIGR04520 77 -KKVGMVFQnpdnqfvGA------TVEDDvaFGL---ENLGVPREEMRKrvdEALKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD--ERLKAycDRSYHMKDG 215
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDmeEAVLA--DRVIVMNKG 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-215 |
4.33e-37 |
|
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: 129.25 E-value: 4.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVtkSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkalAKVR 81
Cdd:cd03245 3 IEFRNV--SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD----PADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIGFILQATNLVpFLTVKQQFTLlkkkNKNVMSNEDYQQLMSQLGLTSLLNKLP-----------SEISGGQKQRVAI 150
Cdd:cd03245 77 RRNIGYVPQDVTLF-YGTLRDNITL----GAPLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 151 AKALYTNPSIILADEPTAALDTENAIEVIKILRdqAKKRKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLR--QLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-215 |
8.09e-37 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 128.71 E-value: 8.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFK---DGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQ----DITTMK 73
Cdd:COG4778 4 LLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 74 QKALAKVRMSEIGFILQATNLVPFLT----VKQqfTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKL-PSEISGGQKQRV 148
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSaldvVAE--PLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 149 AIAKALYTNPSIILADEPTAALDTENAIEVIKILRDqaKKRKKACII-VTHDERL-KAYCDRSYHMKDG 215
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE--AKARGTAIIgIFHDEEVrEAVADRVVDVTPF 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-212 |
8.44e-36 |
|
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: 132.03 E-value: 8.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkqKALAKVR 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA----DADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIGFILQAtnlvPFL---TVKQQFTLlkkkNKNVMSNEDYQQLMSQLGLTSLLNKLP-----------SEISGGQKQR 147
Cdd:TIGR02857 395 RDQIAWVPQH----PFLfagTIAENIRL----ARPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 148 VAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHDERLKAYCDRSYHM 212
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-225 |
8.58e-36 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 129.04 E-value: 8.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNrnieaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKAlakv 80
Cdd:NF040840 1 MIRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmSEIGFILQATNLVPFLTVKQQ--FTL-LKKKNKNVMSnEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:NF040840 72 --RGIAYVYQNYMLFPHKTVFENiaFGLkLRKVPKEEIE-RKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTH--DERLkAYCDRSYHMKDGVLNLENETVE 225
Cdd:NF040840 149 PKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHnfEEAL-SLADRVGIMLNGRLSQVGDVRE 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-217 |
1.24e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 125.17 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKv 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmseIGFILQATNLVPFLTVKQQFTL------LKKKNKNVMSNEdyqqLMSQLGLTSLLNKLPSEISGGQKQRVAIAKAL 154
Cdd:cd03266 80 ----LGFVSDSTGLYDRLTARENLEYfaglygLKGDELTARLEE----LADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 155 YTNPSIILADEPTAALD---TENAIEVIKILRDQAKkrkkaCIIV-THD-ERLKAYCDRSYHMKDGVL 217
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDvmaTRALREFIRQLRALGK-----CILFsTHImQEVERLCDRVVVLHRGRV 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-199 |
1.30e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 125.90 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDI---TTMKQKALAKVRmSEIGFILQATNLV 95
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 96 PFLTVKQQFT--------LLKKKnknvmSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPT 167
Cdd:PRK11124 95 PHLTVQQNLIeapcrvlgLSKDQ-----ALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190
....*....|....*....|....*....|..
gi 579537805 168 AALDTENAIEVIKILRDQAKKrKKACIIVTHD 199
Cdd:PRK11124 170 AALDPEITAQIVSIIRELAET-GITQVIVTHE 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-215 |
1.59e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkDGNRnieAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQtPTSGHILINNQDITtmkqkaLAK 79
Cdd:COG1129 4 LLEMRGISKSF-GGVK---ALDGVSLELRPGEVHALLGENGAGKSTLMkILSGVYQ-PDSGEILLDGEPVR------FRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRMSE---IGFILQATNLVPFLTV---------KQQFTLLkkkNKNVMsNEDYQQLMSQLGLTSLLNKLPSEISGGQKQR 147
Cdd:COG1129 73 PRDAQaagIAIIHQELNLVPNLSVaeniflgrePRRGGLI---DWRAM-RRRARELLARLGLDIDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 148 VAIAKALYTNPSIILADEPTAAL---DTENAIEVIKILRDQakkrKKACIIVTH--DErLKAYCDRSYHMKDG 215
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLterEVERLFRIIRRLKAQ----GVAIIYISHrlDE-VFEIADRVTVLRDG 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
2.28e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.26 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILInnqDITTMKQKALAKV 80
Cdd:PRK13632 7 MIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI---DGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQ-ATNLVPFLTVKQQ--FTLlkkKNKNVMSNE------DYQQlmsQLGLTSLLNKLPSEISGGQKQRVAIA 151
Cdd:PRK13632 82 R-KKIGIIFQnPDNQFIGATVEDDiaFGL---ENKKVPPKKmkdiidDLAK---KVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 152 KALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD--ERLKA 204
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDmdEAILA 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-200 |
3.49e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 128.03 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkDGnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQkalakv 80
Cdd:PRK11607 19 LLEIRNLTKSF-DG---QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATNLVPFLTVKQQFTLLKKKNKnVMSNEDYQQLMSQLGLTSLL---NKLPSEISGGQKQRVAIAKALYTN 157
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFGLKQDK-LPKAEIASRVNEMLGLVHMQefaKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 579537805 158 PSIILADEPTAALDTE----NAIEVIKILrdqaKKRKKACIIVTHDE 200
Cdd:PRK11607 168 PKLLLLDEPMGALDKKlrdrMQLEVVDIL----ERVGVTCVMVTHDQ 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-217 |
4.39e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 127.51 E-value: 4.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkalAKVRmsE 84
Cdd:PRK10851 6 ANIKKSF--GRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH----ARDR--K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 85 IGFILQATNLVPFLTVKQQ----FTLLKKK--------NKNVMsnedyqQLMSQLGLTSLLNKLPSEISGGQKQRVAIAK 152
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNiafgLTVLPRRerpnaaaiKAKVT------QLLEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 153 ALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQGNI 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-215 |
1.09e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 123.42 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITT--MKQKAlak 79
Cdd:cd03218 1 LRAENLSKRY--GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpMHKRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 vRMSeIGFILQATNLVPFLTVKQ------QFTLLKKKNKnvmsNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKA 153
Cdd:cd03218 74 -RLG-IGYLPQEASIFRKLTVEEnilavlEIRGLSKKER----EEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 154 LYTNPSIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHDER-LKAYCDRSYHMKDG 215
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIK-ILKDRGIGVLITDHNVReTLSITDRAYIIYEG 209
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-215 |
1.64e-34 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 122.28 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 25 NFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTmkqkaLAKVRmSEIGFILQATNLVPFLTVKQQF 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG-----LAPYQ-RPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 105 TL-LKKKNK-NVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKIL 182
Cdd:TIGR01277 92 GLgLHPGLKlNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....
gi 579537805 183 RDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHlSDARAIASQIAVVSQG 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-198 |
3.85e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 122.00 E-value: 3.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVT-------KSFkdgnrnieavkdtNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMk 73
Cdd:PRK10771 1 MLKLTDITwlyhhlpMRF-------------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 74 qkALAK--VRMseigfILQATNLVPFLTVKQQFTL-----LKKknkNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQ 146
Cdd:PRK10771 67 --PPSRrpVSM-----LFQENNLFSHLTVAQNIGLglnpgLKL---NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 579537805 147 RVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTH 198
Cdd:PRK10771 137 RVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-215 |
4.98e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 122.19 E-value: 4.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVtkSFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALqTPTSGHILINNQDITTMKQKALAK 79
Cdd:PRK13548 2 MLEARNL--SVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLrALSGEL-SPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRmseiGFILQATNLV-PFlTVKQ-------QFTLLKKKNKNVMsnedyQQLMSQLGLTSLLNKLPSEISGGQKQRVAIA 151
Cdd:PRK13548 77 RR----AVLPQHSSLSfPF-TVEEvvamgraPHGLSRAEDDALV-----AAALAQVDLAHLAGRDYPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 152 KAL------YTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKA-YCDRSYHMKDG 215
Cdd:PRK13548 147 RVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAArYADRIVLLHQG 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-199 |
7.65e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 123.30 E-value: 7.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSF--KDG--NRNIEAVK---DTNFEINKGDIIALVGPSGSGKSTF---LTMagaLQTPTSGHILINNQDITT 71
Cdd:COG4608 8 LEVRDLKKHFpvRGGlfGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLgrlLLR---LEEPTSGEILFDGQDITG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 72 MKQKALAKVRmSEIGFILQ--ATNLVPFLTVKQQ-------FTLLKKKNKnvmsnEDY-QQLMSQLGL-TSLLNKLPSEI 140
Cdd:COG4608 85 LSGRELRPLR-RRMQMVFQdpYASLNPRMTVGDIiaeplriHGLASKAER-----RERvAELLELVGLrPEHADRYPHEF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 141 SGGQKQRVAIAKALYTNPSIILADEPTAALDTenAIE--VIKILRDQAKKRKKACIIVTHD 199
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDV--SIQaqVLNLLEDLQDELGLTYLFISHD 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-199 |
1.28e-33 |
|
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: 120.36 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQ----TPTSGHILINNQDITTMKQKA 76
Cdd:cd03260 1 IELRDLNVYYGD----KHALKDISLDIPKGEITALIGPSGCGKSTLLrLLNRLNDlipgAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 77 LAkVRMsEIGFILQATNLVPF-------LTVKqqftLLKKKNKNVMSNEDYQQLmSQLGLT-SLLNKL-PSEISGGQKQR 147
Cdd:cd03260 77 LE-LRR-RVGMVFQKPNPFPGsiydnvaYGLR----LHGIKLKEELDERVEEAL-RKAALWdEVKDRLhALGLSGGQQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 579537805 148 VAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHD 199
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHN 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-215 |
1.53e-33 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 120.41 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVrms 83
Cdd:cd03253 3 FENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 84 eIGFILQATNLV------------PFLTVKQQFTLLKKKN--KNVMS-NEDYQQLMSQLGLtsllnklpsEISGGQKQRV 148
Cdd:cd03253 77 -IGVVPQDTVLFndtigynirygrPDATDEEVIEAAKAAQihDKIMRfPDGYDTIVGERGL---------KLSGGEKQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 149 AIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVNADKIIVLKDG 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-217 |
1.57e-33 |
|
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: 118.47 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVtkSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQtPTSGHILINNQDITTMKQKALAKv 80
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLArLILGLLR-PTSGRVRLDGADISQWDPNELGD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmsEIGFILQATNLVPFlTVKQqftllkkknkNVMSnedyqqlmsqlgltsllnklpseisGGQKQRVAIAKALYTNPSI 160
Cdd:cd03246 77 ---HVGYLPQDDELFSG-SIAE----------NILS-------------------------GGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 161 ILADEPTAALDTEN--AI-EVIKilrdQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:cd03246 118 LVLDEPNSHLDVEGerALnQAIA----ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-200 |
2.15e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.12 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSfkdgNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLT-MAGALQTP--TSGHILINNQDITTMKQKAl 77
Cdd:COG4136 1 MLSLENLTIT----LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAEQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 78 akvRmsEIGFILQATNLVPFLTVKQ--QFTL---LKKKNKNVMSnedyQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAK 152
Cdd:COG4136 76 ---R--RIGILFQDDLLFPHLSVGEnlAFALpptIGRAQRRARV----EQALEEAGLAGFADRDPATLSGGQRARVALLR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 579537805 153 ALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDE 200
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDE 194
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-199 |
2.31e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 120.71 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKD-----GNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKA 76
Cdd:COG4167 5 LEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 77 LAK-VRMseigfILQ--ATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQLMSQLGLTSLL----NKLPSEISGGQKQRVA 149
Cdd:COG4167 85 RCKhIRM-----IFQdpNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLpehaNFYPHMLSSGQKQRVA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-215 |
8.62e-33 |
|
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: 123.64 E-value: 8.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 18 IEAVKDTNFEINKGDIIALVGPSGSGKSTfLTMAgALQ-TPTSGHILINNQDITTMKQKALAKVRmSEIGFILQAtnlvP 96
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKST-LGLA-LLRlIPSEGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQD----P 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 97 F------LTVKQ--------QFTLLKKKNKNVMSnedyQQLMSQLGLT-SLLNKLPSEISGGQKQRVAIAKALYTNPSII 161
Cdd:COG4172 372 FgslsprMTVGQiiaeglrvHGPGLSAAERRARV----AEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 162 LADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERL-KAYCDRSYHMKDG 215
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVvRALAHRVMVMKDG 502
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-215 |
9.64e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.21 E-value: 9.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKdgNRNIeaVKDTNFEINKGDIIALVGPSGSGKST-FLTMAGaLQTPTSGHILINNQDITT--MKQKAl 77
Cdd:COG1137 3 TLEAENLVKSYG--KRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTtFYMIVG-LVKPDSGRIFLDGEDITHlpMHKRA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 78 akvRMSeIGFILQATNLvpF--LTVKQ------QFTLLKKKNKNvmsnEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVA 149
Cdd:COG1137 77 ---RLG-IGYLPQEASI--FrkLTVEDnilavlELRKLSKKERE----ERLEELLEEFGITHLRKSKAYSLSGGERRRVE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHDER--LKAyCDRSYHMKDG 215
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQKIIR-HLKERGIGVLITDHNVRetLGI-CDRAYIISEG 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-215 |
2.06e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 117.81 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKv 80
Cdd:PRK11231 2 TLRTENLTVGY--GTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmsEIGFILQaTNLVP-FLTVKQ--------QFTLLKKknknvMSNEDYQ---QLMSQLGLTSLLNKLPSEISGGQKQRV 148
Cdd:PRK11231 77 ---RLALLPQ-HHLTPeGITVRElvaygrspWLSLWGR-----LSAEDNArvnQAMEQTRINHLADRRLTDLSGGQRQRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 149 AIAKALYTNPSIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDlNQASRYCDHLVVLANG 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-171 |
2.19e-32 |
|
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: 120.21 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 23 DTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDIttmkQKALAKVRMS----EIGFILQATNLVPF 97
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLrAIAG-LERPDSGRIRLGGEVL----QDSARGIFLPphrrRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 98 LTVKQ--QFTLlkKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALD 171
Cdd:COG4148 92 LSVRGnlLYGR--KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-199 |
3.77e-32 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 116.80 E-value: 3.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkqkALAKVRMseigFILQATNLVPFLTV 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-----EPGPDRM----VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 101 KQQFTLLKKKNKNVMSNEDYQQLMSQ----LGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAI 176
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRAIVEEhialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|...
gi 579537805 177 EVIKILRDQAKKRKKACIIVTHD 199
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHD 174
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
4.66e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 114.45 E-value: 4.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkdgnRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQtPTSGHILINNQDIttmkqkALAKV 80
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMkILSGLYK-PDSGEILVDGKEV------SFASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSE---IGFILQatnlvpfltvkqqftllkkknknvmsnedyqqlmsqlgltsllnklpseISGGQKQRVAIAKALYTN 157
Cdd:cd03216 70 RDARragIAMVYQ-------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQaKKRKKACIIVTH--DErLKAYCDRSYHMKDGVL 217
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHrlDE-VFEIADRVTVLRDGRV 160
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-200 |
5.51e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 119.36 E-value: 5.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 6 NVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQditTMKQKALAKvrmSEI 85
Cdd:PRK11000 8 NVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPAE---RGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 86 GFILQATNLVPFLTVKQQ--FTL-LKKKNKNVMsNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIIL 162
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENmsFGLkLAGAKKEEI-NQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 579537805 163 ADEPTAALDTenAIEV---IKILRDQaKKRKKACIIVTHDE 200
Cdd:PRK11000 157 LDEPLSNLDA--ALRVqmrIEISRLH-KRLGRTMIYVTHDQ 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-216 |
1.36e-31 |
|
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: 115.33 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVtkSFKDGNR-NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIttmKQKALAKVRm 82
Cdd:cd03249 3 FKNV--SFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI---RDLNLRWLR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 SEIGFILQATNLVPfLTVKQQFTLlkkkNKNVMSNEDYQQLMSQLGLTSLLNKLP-----------SEISGGQKQRVAIA 151
Cdd:cd03249 77 SQIGLVSQEPVLFD-GTIAENIRY----GKPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 152 KALYTNPSIILADEPTAALDTENAIEVIKILrDQAKKrKKACIIVTHdeRLKA--YCDRSYHMKDGV 216
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAESEKLVQEAL-DRAMK-GRTTIVIAH--RLSTirNADLIAVLQNGQ 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-215 |
1.49e-31 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 117.91 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 23 DTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRMSEIGFILQATNLVPFLTVKQ 102
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 103 QFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKIL 182
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 579537805 183 RDQAKKRKKACIIVTHD----ERLkayCDRSYHMKDG 215
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSlqevLRL---ADRVVVLEDG 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
6-215 |
2.41e-31 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 117.13 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 6 NVTKSFKDGNrnIEAVKDTNFEINKGDIIALVGPSGSGKS-TFLTMAGALQTP--TSGHILINNQDITTMKQKALAKVRM 82
Cdd:PRK09473 19 RVTFSTPDGD--VTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 SEIGFILQ--ATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQLMSQLGLTSL------LNKLPSEISGGQKQRVAIAKAL 154
Cdd:PRK09473 97 EQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpearkrMKMYPHEFSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 155 YTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKA-YCDRSYHMKDG 215
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICDKVLVMYAG 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-198 |
2.69e-31 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 114.24 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 3 KFENVTKSFkdgNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALakvrM 82
Cdd:cd03254 4 EFENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 SEIGFILQATNLVPFlTVKQQFTLlkkkNKNVMSNEDYQQLMSQLGLTSLLNKLP-----------SEISGGQKQRVAIA 151
Cdd:cd03254 77 SMIGVVLQDTFLFSG-TIMENIRL----GRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 579537805 152 KALYTNPSIILADEPTAALD--TENAI-EVIKILRDQakkrkKACIIVTH 198
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDteTEKLIqEALEKLMKG-----RTSIIIAH 196
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-225 |
4.16e-31 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 114.00 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKStfLTMAGALQ------TPTSGHILINNQDIttmkqkALAKVRMSEIGFILQA-- 91
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKS--LTCLAILGllppglTQTSGEILLDGRPL------LPLSIRGRHIATIMQNpr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 92 TNLVPFLTVKQQF--TLLKKKNKNVMSNEDYQQLMSQLGL---TSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEP 166
Cdd:TIGR02770 73 TAFNPLFTMGNHAieTLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 167 TAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYC-DRSYHMKDGVLnLENETVE 225
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIaDEVAVMDDGRI-VERGTVK 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
7.98e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.40 E-value: 7.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKST-FLTMAGALQtPTSGHILINNQDITTMKqKALAK 79
Cdd:PRK13639 1 ILETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTlFLHFNGILK-PTSGEVLIKGEPIKYDK-KSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRMSeIGFILQATNLVPFL-TVKQQ--FTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYT 156
Cdd:PRK13639 76 VRKT-VGIVFQNPDDQLFApTVEEDvaFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 157 NPSIILADEPTAALDTENAIEVIKILRDqAKKRKKACIIVTHDERL-KAYCDRSYHMKDG 215
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYD-LNKEGITIIISTHDVDLvPVYADKVYVMSDG 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-202 |
1.95e-30 |
|
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: 112.32 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTksFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkaLAKVR 81
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQATnlvpFL---TVKQqftllkkknkNVM------SNEDYQQLMSQLGLTSLLNKLP-----------SEIS 141
Cdd:cd03251 76 -RQIGLVSQDV----FLfndTVAE----------NIAygrpgaTREEVEEAARAANAHEFIMELPegydtvigergVKLS 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 142 GGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHdeRL 202
Cdd:cd03251 141 GGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAH--RL 197
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-199 |
2.91e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.49 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRN-IEAVKDTNFEINKGDIIALVGPSGSGKSTFLTM-AGALqTPTSGHILINNQDITTMKQKALA 78
Cdd:COG1101 1 MLELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAiAGSL-PPDSGSILIDGKDVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KVrmseIGFILQ--ATNLVPFLTVKQQFTL-------------LKKKNKnvmsnEDYQQLMSQLGLtSLLNKLPSEI--- 140
Cdd:COG1101 80 KY----IGRVFQdpMMGTAPSMTIEENLALayrrgkrrglrrgLTKKRR-----ELFRELLATLGL-GLENRLDTKVgll 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 141 SGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-215 |
3.09e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.13 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVtkSFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALqTPTSGHILINNQDITTMKQKALAK 79
Cdd:COG4559 1 MLEAENL--SVRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLkLLTGEL-TPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VR--MSeigfilQATNLV-PFlTVKQ-------QFTLLKKKNKNVMsnedyQQLMSQLGLTSLLNKLPSEISGGQKQRVA 149
Cdd:COG4559 76 RRavLP------QHSSLAfPF-TVEEvvalgraPHGSSAAQDRQIV-----REALALVGLAHLAGRSYQTLSGGEQQRVQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 150 IAKAL-------YTNPSIILADEPTAALDTENAIEVIKILRDQAkKRKKACIIVTHDERLKA-YCDRSYHMKDG 215
Cdd:COG4559 144 LARVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLA-RRGGGVVAVLHDLNLAAqYADRILLLHQG 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
1.08e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.11 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkalakv 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmSEIGFILQATNLVPFLTVKQQFTL---LKKKNKnVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:COG4525 76 --ADRGVVFQKDALLPWLNVLDNVAFglrLRGVPK-AERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 579537805 158 PSIILADEPTAALD--TENAIEVIkILRDQAKKRKKACIIvTHD 199
Cdd:COG4525 153 PRFLLMDEPFGALDalTREQMQEL-LLDVWQRTGKGVFLI-THS 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
1.44e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNqDITtmkqkalakvrm 82
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLkILAG-ELEPDSGEVSIPK-GLR------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 seIGFILQATNLVPFLTV--------KQQFTLLKKKNKNVMSNEDY--------------------------QQLMSQLG 128
Cdd:COG0488 63 --IGYLPQEPPLDDDLTVldtvldgdAELRALEAELEELEAKLAEPdedlerlaelqeefealggweaearaEEILSGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 129 LT-SLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDtenaIEVIKILRDQAKKRKKACIIVTHDeR--LKAY 205
Cdd:COG0488 141 FPeEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHD-RyfLDRV 215
|
250
....*....|....
gi 579537805 206 CDRSYHMKDGVLNL 219
Cdd:COG0488 216 ATRILELDRGKLTL 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-215 |
1.84e-29 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 114.85 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQtPTSGHILINNQDITTMKQKALAKV 80
Cdd:COG4618 331 LSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLArLLVGVWP-PTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmseIGFILQATNLVPFlTVKQqftllkkknkNV--MSNEDYQQLMS--QL-GLTSLLNKLP-----------SEISGGQ 144
Cdd:COG4618 408 ----IGYLPQDVELFDG-TIAE----------NIarFGDADPEKVVAaaKLaGVHEMILRLPdgydtrigeggARLSGGQ 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 145 KQRVAIAKALYTNPSIILADEPTAALDTE------NAIEvikilrdQAKKRKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLDDEgeaalaAAIR-------ALKARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-216 |
4.74e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.58 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkDGNrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkqKALAKVR 81
Cdd:PRK09452 15 VELRGISKSF-DGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT----HVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 msEIGFILQATNLVPFLTVKQQ--FTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPS 159
Cdd:PRK09452 87 --HVNTVFQSYALFPHMTVFENvaFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 160 IILADEPTAALDTEnaievikiLRDQAKKRKKAC--------IIVTHD-ERLKAYCDRSYHMKDGV 216
Cdd:PRK09452 165 VLLLDESLSALDYK--------LRKQMQNELKALqrklgitfVFVTHDqEEALTMSDRIVVMRDGR 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-199 |
4.84e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 109.29 E-value: 4.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTM------------KQKALAKVRMSeig 86
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadkNQLRLLRTRLT--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 87 FILQATNLVPFLTVKQ-------QFTLLKKKNknvmSNEDYQQLMSQLGLT-SLLNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:PRK10619 96 MVFQHFNLWSHMTVLEnvmeapiQVLGLSKQE----ARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 579537805 159 SIILADEPTAALDTENAIEVIKILRDQAKKrKKACIIVTHD 199
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHE 211
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-215 |
1.18e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 113.04 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVtkSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkQKALAKVRmS 83
Cdd:TIGR03375 466 FRNV--SFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR---QIDPADLR-R 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 84 EIGFILQATNLvpFL-TVKQQFTLlkkkNKNVMSNEDYQQLMSQLGLTSLLNKLPS-----------EISGGQKQRVAIA 151
Cdd:TIGR03375 540 NIGYVPQDPRL--FYgTLRDNIAL----GAPYADDEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALA 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 152 KALYTNPSIILADEPTAALDTENAIEVIKILRDQAKkrKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:TIGR03375 614 RALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLDLVDRIIVMDNG 675
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-215 |
1.47e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.60 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNR-NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKaLAKV 80
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQL---MSQLGLT--SLLNKLPSEISGGQKQRVAIAKALY 155
Cdd:PRK13637 82 R-KKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVkraMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 156 TNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKG 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
2.84e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.01 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKST-FLTMAGALQtPTSGHILINNQDITtMKQKALAK 79
Cdd:PRK13636 5 ILKVEELNYNYSDGT---HALKGININIKKGEVTAILGGNGAGKSTlFQNLNGILK-PSSGRILFDGKPID-YSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRMSeIGFILQATNLVPF-LTVKQQFTL----LKKKNKNVmsNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKAL 154
Cdd:PRK13636 80 LRES-VGMVFQDPDNQLFsASVYQDVSFgavnLKLPEDEV--RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 155 YTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVLNLE 220
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRVILQ 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-215 |
4.40e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.02 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgNRNIEAVkdtNFEINKGDIIALVGPSGSGKSTFLTMAGAL----QTPTSGHILINNqdiTTMKQKA 76
Cdd:PRK09984 4 IIRVEKLAKTFNQ-HQALHAV---DLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGR---TVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 77 LAK-VRMS--EIGFILQATNLVPFLTVKQQF-------TLLKKKNKNVMSNEDYQ---QLMSQLGLTSLLNKLPSEISGG 143
Cdd:PRK09984 77 LARdIRKSraNTGYIFQQFNLVNRLSVLENVligalgsTPFWRTCFSWFTREQKQralQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 144 QKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTH--DERLKaYCDRSYHMKDG 215
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHqvDYALR-YCERIVALRQG 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-188 |
6.65e-28 |
|
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: 104.99 E-value: 6.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNrnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKAlakvr 81
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQATNLVPFLTVKQQF----TLLKKKNKNVMSNEDYqqlmsqLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:cd03268 72 -RRIGALIEAPGFYPNLTARENLrllaRLLGIRKKRIDEVLDV------VGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190
....*....|....*....|....*....|.
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAKK 188
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQ 175
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-217 |
1.04e-27 |
|
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: 104.17 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFK--DGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQTP-TSGHILINNQDIttmKQKAL 77
Cdd:cd03213 4 LSFRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLnALAGRRTGLgVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 78 AKvrmsEIGFILQATNLVPFLTVkqqftllkkknknvmsnedYQQLMSQLGLTSllnklpseISGGQKQRVAIAKALYTN 157
Cdd:cd03213 81 RK----IIGYVPQDDILHPTLTV-------------------RETLMFAAKLRG--------LSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAkKRKKACIIVTHDERLKAY--CDRSYHMKDGVL 217
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHQPSSEIFelFDKLLLLSQGRV 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-215 |
1.42e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 106.32 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGN-RNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:PRK13651 3 IKVKNIVKIFNKKLpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIgfILQATNLVPFLTVKQ---------QF--------TLLKK-----KNKNVMSNEDYQ---QLMSQLGL-TSLLN 134
Cdd:PRK13651 83 VLEKL--VIQKTRFKKIKKIKEirrrvgvvfQFaeyqlfeqTIEKDiifgpVSMGVSKEEAKKraaKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 135 KLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILrDQAKKRKKACIIVTHD-ERLKAYCDRSYHMK 213
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIF-DNLNKQGKTIILVTHDlDNVLEWTKRTIFFK 239
|
..
gi 579537805 214 DG 215
Cdd:PRK13651 240 DG 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-199 |
1.70e-27 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 104.80 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 27 EINKGDIIALVGPSGSGKSTFLTM-AGALQtPTSGHILINNQDITTMKQKALAKVRMseigfilqatnlvpflTVKQqft 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMlAGVLK-PDEGDIEIELDTVSYKPQYIKADYEG----------------TVRD--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 106 LLKKKNKNVMSNEDYQ-QLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRD 184
Cdd:cd03237 81 LLSSITKDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170
....*....|....*
gi 579537805 185 QAKKRKKACIIVTHD 199
Cdd:cd03237 161 FAENNEKTAFVVEHD 175
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-199 |
3.81e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 105.94 E-value: 3.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 16 RNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRmSEIGFILQ--ATN 93
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQdpLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 94 LVPFLTVKQQFTLLKKKNKNVMSNEDYQQ----LMSQLGL-TSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTA 168
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTYHPKLSRQEVKDrvkaMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190
....*....|....*....|....*....|.
gi 579537805 169 ALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-204 |
4.01e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 105.59 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKS-TFLTMAGALQTP---TSGHILINNQDITTMKQKA 76
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 77 LAKVRMSEIGFILQ--ATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQ---LMSQLGL---TSLLNKLPSEISGGQKQRV 148
Cdd:PRK11022 83 RRNLVGAEVAMIFQdpMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRaidLLNQVGIpdpASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 149 AIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKA 204
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVA 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-204 |
4.11e-27 |
|
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: 103.72 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVTksFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvrms 83
Cdd:cd03252 3 FEHVR--FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 84 EIGFILQaTNLVPFLTVKQQFTLlkkkNKNVMSNEDYQQLMSQLGLTSLLNKLP-----------SEISGGQKQRVAIAK 152
Cdd:cd03252 77 QVGVVLQ-ENVLFNRSIRDNIAL----ADPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIAR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 579537805 153 ALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHdeRLKA 204
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAH--RLST 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-215 |
4.83e-27 |
|
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: 102.55 E-value: 4.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIEAV-KDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQtPTSGHILINNQdittmkqkalak 79
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLsALLGELE-KLSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 vrmseIGFILQatnlVPFL---TVKQQFTLLKKknknvMSNEDYQQLMSQLGLTSLLNKLP----SEI-------SGGQK 145
Cdd:cd03250 68 -----IAYVSQ----EPWIqngTIRENILFGKP-----FDEERYEKVIKACALEPDLEILPdgdlTEIgekginlSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 146 QRVAIAKALYTNPSIILADEPTAALD--TENAI--EVIKilrdQAKKRKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDahVGRHIfeNCIL----GLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-220 |
7.17e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.94 E-value: 7.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQditTMKQKALAKVR 81
Cdd:PRK13635 6 IRVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQ-ATNLVPFLTVKQQ--FTLlkkKNKNVMSNE---DYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALY 155
Cdd:PRK13635 81 -RQVGMVFQnPDNQFVGATVQDDvaFGL---ENIGVPREEmveRVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 156 TNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVLNLE 220
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-217 |
7.55e-27 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 107.43 E-value: 7.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvr 81
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 msEIGFILQATNLVPFlTVKQQFTLLKKknknvmsNEDYQQLMSQL---GLTSLLNKLP-----------SEISGGQKQR 147
Cdd:TIGR01842 393 --HIGYLPQDVELFPG-TVAENIARFGE-------NADPEKIIEAAklaGVHELILRLPdgydtvigpggATLSGGQRQR 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 148 VAIAKALYTNPSIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIK-ALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-208 |
9.77e-27 |
|
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: 102.80 E-value: 9.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 11 FKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvrmseIGFIL- 89
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-----IGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 90 QATNLVPFLTVKQQFTLLKKKNKnvMSNEDYQQ----LMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADE 165
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAIYD--LPPARFKKrldeLSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 579537805 166 PTAALDTENAIEVIKILRDQAKKRKKACIIVTHDER-LKAYCDR 208
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARR 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-217 |
9.93e-27 |
|
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: 102.06 E-value: 9.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkqKALAKVRMSe 84
Cdd:cd03265 4 ENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 85 IGFILQATNLVPFLTVKQQFTLLKK--KNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIIL 162
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARlyGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 163 ADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRI 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-217 |
1.08e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 102.66 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKdGNRnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvr 81
Cdd:PRK10895 4 LTAKNLAKAYK-GRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQAT----------NLVPFLTVKQQFTLLKKKNKNvmsnedyQQLMSQLGLTSLLNKLPSEISGGQKQRVAIA 151
Cdd:PRK10895 78 -RGIGYLPQEAsifrrlsvydNLMAVLQIRDDLSAEQREDRA-------NELMEEFHIEHLRDSMGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 152 KALYTNPSIILADEPTAALDTENAIEVIKILrDQAKKRKKACIIVTHDERLK-AYCDRSYHMKDGVL 217
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRII-EHLRDSGLGVLITDHNVRETlAVCERAYIVSQGHL 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-212 |
1.16e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 102.26 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVkdtNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGV---TFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQATNLVPFLTVKQqftllkkknkNV--------MSNEDYQQLMS----QLGLTSLLNKLPSEISGGQKQRV 148
Cdd:PRK10908 78 R-RQIGMIFQDHHLLMDRTVYD----------NVaipliiagASGDDIRRRVSaaldKVGLLDKAKNFPIQLSGGEQQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 149 AIAKALYTNPSIILADEPTAALDTENAiEVIKILRDQAKKRKKACIIVTHDERLKAycDRSYHM 212
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALS-EGILRLFEEFNRVGVTVLMATHDIGLIS--RRSYRM 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-215 |
2.16e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 103.73 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 36 LVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkqkaLAKVRMSEIGFILQATNLVPFLTVKQQ--FTLLKKKNKN 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT------NVPPHLRHINMVFQSYALFPHMTVEENvaFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 114 VMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDtenaieviKILRDQAKKRKKA- 192
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD--------KKLRDQMQLELKTi 146
|
170 180 190
....*....|....*....|....*....|.
gi 579537805 193 -------CIIVTHDER-LKAYCDRSYHMKDG 215
Cdd:TIGR01187 147 qeqlgitFVFVTHDQEeAMTMSDRIAIMRKG 177
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-217 |
2.21e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.94 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGN-RNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITT-MKQKALAK 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRmSEIGFILQATNLVPFLTVKQQFTLLKKKNKNV----MSNEDYQQLMsQLGLT-SLLNKLPSEISGGQKQRVAIAKAL 154
Cdd:PRK13646 83 VR-KRIGMVFQFPESQLFEDTVEREIIFGPKNFKMnldeVKNYAHRLLM-DLGFSrDVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 155 YTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-171 |
2.83e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 103.77 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkDGNrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKAlakv 80
Cdd:PRK11650 3 GLKLQAVRKSY-DGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmsEIGFILQATNLVPFLTVKQQ--FTLlkkKNKNvMSNEDYQQLMSQ----LGLTSLLNKLPSEISGGQKQRVAIAKAL 154
Cdd:PRK11650 76 R--DIAMVFQNYALYPHMSVRENmaYGL---KIRG-MPKAEIEERVAEaariLELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170
....*....|....*..
gi 579537805 155 YTNPSIILADEPTAALD 171
Cdd:PRK11650 150 VREPAVFLFDEPLSNLD 166
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-215 |
3.17e-26 |
|
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: 98.67 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALqTPTSGHILINNQdittmkqkalakv 80
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLkLIAGEL-EPDEGIVTWGST------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmSEIGFilqatnlvpfltvkqqftllkkknknvmsnedYQQLmsqlgltsllnklpseiSGGQKQRVAIAKALYTNPSI 160
Cdd:cd03221 63 --VKIGY--------------------------------FEQL-----------------SGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 161 ILADEPTAALDtenaIEVIKILRDQAKKRKKACIIVTHDER-LKAYCDRSYHMKDG 215
Cdd:cd03221 92 LLLDEPTNHLD----LESIEALEEALKEYPGTVILVSHDRYfLDQVATKIIELEDG 143
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-224 |
3.53e-26 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 103.42 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 23 DTNFEIN-----KGdIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRMSEIGFILQATNLVPF 97
Cdd:PRK11144 12 DLCLTVNltlpaQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 98 LTVKQQftlLKKKNKNVMsNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIE 177
Cdd:PRK11144 91 YKVRGN---LRYGMAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 579537805 178 VIKILRDQAKKRKKACIIVTH--DERLkaycdrsyHMKDGVLNLENETV 224
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHslDEIL--------RLADRVVVLEQGKV 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-199 |
4.73e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 102.74 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 3 KFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTF---LTMagaLQTPTSGHILINNQDITTmKQKALAK 79
Cdd:PRK11308 13 KHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLarlLTM---IETPTGGELYYQGQDLLK-ADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRMSEIGFILQA--TNLVPFLTVKQQF-------TLLKKKNKNvmsnEDYQQLMSQLGL-TSLLNKLPSEISGGQKQRVA 149
Cdd:PRK11308 89 LLRQKIQIVFQNpyGSLNPRKKVGQILeepllinTSLSAAERR----EKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-220 |
7.65e-26 |
|
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: 98.92 E-value: 7.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTM-AGALQtPTSGHILINNQDITTMkQKALAKV 80
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLlTGDLK-PQQGEITLDGVPVSDL-EKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmseIGFILQAtnlvPFLtvkqqFTllkkknknvmsnedyqqlmsqlglTSLLNKLPSEISGGQKQRVAIAKALYTNPSI 160
Cdd:cd03247 77 ----ISVLNQR----PYL-----FD------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 161 ILADEPTAALDTENAIEVIKILRDQAKkrKKACIIVTHDERLKAYCDRSYHMKDGVLNLE 220
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
7.75e-26 |
|
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: 99.66 E-value: 7.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNrnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQkalakvr 81
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQATNLVPFLTVKQQ---FTLLKK-KNKNVMSNEDYqqLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:cd03269 70 -NRIGYLPEERGLYPKMKVIDQlvyLAQLKGlKKEEARRRIDE--WLERLELSEYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAKKrKKACIIVTHD-ERLKAYCDRSYHMKDGV 216
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQmELVEELCDRVLLLNKGR 205
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-220 |
7.98e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.91 E-value: 7.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNqdittmkqKALAKVR 81
Cdd:PRK11247 13 LLLNAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT--------APLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQATNLVPFLTVKQQFTL-LKKKNKnvmsnEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSI 160
Cdd:PRK11247 81 -EDTRLMFQDARLLPWKKVIDNVGLgLKGQWR-----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 161 ILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD--ERLkAYCDRSYHMKDGVLNLE 220
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvsEAV-AMADRVLLIEEGKIGLD 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-220 |
1.00e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.93 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIE--AVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDitTMKQKALA 78
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KVRmSEIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQL---MSQLGLTSLLNKLPSEISGGQKQRVAIAKALY 155
Cdd:PRK13633 82 DIR-NKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVdesLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 156 TNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTH--DERLKAycDRSYHMKDGVLNLE 220
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHymEEAVEA--DRIIVMDSGKVVME 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-215 |
1.25e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 103.71 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:PRK09700 5 YISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmsEIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSNE--DY-------QQLMSQLGLTSLLNKLPSEISGGQKQRVAIA 151
Cdd:PRK09700 81 ---GIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVNiiDWremrvraAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 152 KALYTNPSIILADEPTAALdTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-199 |
1.27e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 100.19 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkDGNRnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:COG4674 10 ILYVEDLTVSF-DGFK---ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmseIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSN----------EDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAI 150
Cdd:COG4674 86 G---IGRKFQKPTVFEELTVFENLELALKGDRGVFASlfarltaeerDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 579537805 151 AKALYTNPSIILADEPTAAL-DTENAiEVIKILRDQAKKRkkACIIVTHD 199
Cdd:COG4674 163 GMLLAQDPKLLLLDEPVAGMtDAETE-RTAELLKSLAGKH--SVVVVEHD 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-198 |
1.49e-25 |
|
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: 99.77 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTksFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGhilinnQDITTMKQKaLAKV 80
Cdd:COG1119 3 LLELRNVT--VRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG------NDVRLFGER-RGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSE----IGFI---LQAtNLVPFLTVK--------------QQFTllkkknknvmsNEDYQ---QLMSQLGLTSLLNKL 136
Cdd:COG1119 72 DVWElrkrIGLVspaLQL-RFPRDETVLdvvlsgffdsiglyREPT-----------DEQRErarELLELLGLAHLADRP 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 137 PSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTH 198
Cdd:COG1119 140 FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-198 |
2.03e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.60 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 17 NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGAL-----QTPTSGHILINNQDITTMKQKALAK-VRMseigfILQ 90
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRrVQM-----VFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 91 ATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQLM------SQL--GLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIIL 162
Cdd:PRK14247 90 IPNPIPNLSIFENVALGLKLNRLVKSKKELQERVrwalekAQLwdEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 579537805 163 ADEPTAALDTENAIEVIKILRDQakKRKKACIIVTH 198
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTH 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-224 |
2.32e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 99.76 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRmSEIGFILQ----ATNlvP 96
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFR-RDIQMVFQdsisAVN--P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 97 FLTVK-------QQFTLLKKKNKNVMSNEdyqqLMSQLGLT-SLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTA 168
Cdd:PRK10419 105 RKTVReiireplRHLLSLDKAERLARASE----MLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 169 ALDTENAIEVIKILRDQAKKRKKACIIVTHDERL-KAYCDRSYHMKDGVLnLENETV 224
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLvERFCQRVMVMDNGQI-VETQPV 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-199 |
3.64e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.65 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRMSEIGFILQATNLVPFLT 99
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 100 VKQQfTLLKKKNKNVMSNEDYQQLMS---QLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALD----T 172
Cdd:PRK10070 123 VLDN-TAFGMELAGINAEERREKALDalrQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirT 201
|
170 180
....*....|....*....|....*..
gi 579537805 173 ENAIEVIKIlrdQAkKRKKACIIVTHD 199
Cdd:PRK10070 202 EMQDELVKL---QA-KHQRTIVFISHD 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-208 |
3.68e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.16 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFK-----DG------------NRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTM-AGALqTPTSGHI 62
Cdd:COG4586 1 IIEVENLSKTYRvyekePGlkgalkglfrreYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMlTGIL-VPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 63 LINNQDITTmKQKALAKvrmsEIGFIL-QATNLVPFLTVKQQFTLLKKKNKnvMSNEDYQQLMSQ----LGLTSLLNKLP 137
Cdd:COG4586 80 RVLGYVPFK-RRKEFAR----RIGVVFgQRSQLWWDLPAIDSFRLLKAIYR--IPDAEYKKRLDElvelLDLGELLDTPV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 138 SEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD----ERLkayCDR 208
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmddiEAL---CDR 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-208 |
4.71e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.41 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkQKALAKv 80
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmseIGFILQATNLVPFLTVKQQ---FTLLKKKNKN-VMSNEDYqqLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYT 156
Cdd:COG4152 73 ----IGYLPEERGLYPKMKVGEQlvyLARLKGLSKAeAKRRADE--WLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 157 NPSIILADEPTAALDTENAiEVIK-ILRDQakKRKKACIIV-THD----ERLkayCDR 208
Cdd:COG4152 147 DPELLILDEPFSGLDPVNV-ELLKdVIREL--AAKGTTVIFsSHQmelvEEL---CDR 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-208 |
5.44e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.03 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQdittmkqkalaKV 80
Cdd:COG3845 5 ALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK-----------PV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSE--------IGFILQATNLVPFLTVKQQFTLLKKKNKNVMSN-----EDYQQLMSQLGLTSLLNKLPSEISGGQKQR 147
Cdd:COG3845 70 RIRSprdaialgIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDrkaarARIRELSERYGLDVDPDAKVEDLSVGEQQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 148 VAIAKALYTNPSIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTH--DErLKAYCDR 208
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILR-RLAAEGKSIIFITHklRE-VMAIADR 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-219 |
7.28e-25 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 101.88 E-value: 7.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 28 INKGDIIALVGPSGSGKSTFLT-MAGALQTPT-SGHILINNQDITtmkqkalaKVRMSEIGFILQATNLVPFLTVKQQ-- 103
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANNRKPT--------KQILKRTGFVTQDDILYPHLTVRETlv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 104 FTLLKKKNKNVMSNEDY---QQLMSQLGLTSLLNKLPSE-----ISGGQKQRVAIAKALYTNPSIILADEPTAALDTENA 175
Cdd:PLN03211 163 FCSLLRLPKSLTKQEKIlvaESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 579537805 176 IEVIKILRDQAKKRKKaciIVThdeRLKAYCDRSYHMKDGVLNL 219
Cdd:PLN03211 243 YRLVLTLGSLAQKGKT---IVT---SMHQPSSRVYQMFDSVLVL 280
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-217 |
8.53e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.75 E-value: 8.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNR-NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITT-MKQKALAK 79
Cdd:PRK13641 3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRmSEIGFILQATNLVPFltvkqQFTLLKK-----KNKNVMSNEDYQQL---MSQLGL-TSLLNKLPSEISGGQKQRVAI 150
Cdd:PRK13641 83 LR-KKVSLVFQFPEAQLF-----ENTVLKDvefgpKNFGFSEDEAKEKAlkwLKKVGLsEDLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 151 AKALYTNPSIILADEPTAALDTENAIEVIKILRDQaKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-215 |
1.27e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.27 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 10 SFK-DGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkQKALAKVRmSEIGFI 88
Cdd:PRK13650 11 TFKyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIR-HKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 89 LQ-ATNLVPFLTVKQQ--FTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADE 165
Cdd:PRK13650 87 FQnPDNQFVGATVEDDvaFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 579537805 166 PTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-185 |
1.56e-24 |
|
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: 96.35 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 18 IEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITtmKQKALAKVRMSeIGFILQATNLVP 96
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLkTIMG-LLPPRSGSIRFDGRDIT--GLPPHERARAG-IGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 97 FLTVKQQFTL---LKKKNKNVMSNEDYQQLMSQLGltSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALD-- 171
Cdd:cd03224 89 ELTVEENLLLgayARRRAKRKARLERVYELFPRLK--ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLApk 166
|
170
....*....|....*
gi 579537805 172 -TENAIEVIKILRDQ 185
Cdd:cd03224 167 iVEEIFEAIRELRDE 181
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
1.58e-24 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 100.90 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQtPTSGHILINNQDITTMKQKALAKV 80
Cdd:TIGR02868 335 LELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLaTLAGLLD-PLQGEVTLDGVPVSSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmseIGFILQATNLvpFLTVKQQFTLLKKKNknvMSNEDYQQLMSQLGLTSLLNKLP-----------SEISGGQKQRVA 149
Cdd:TIGR02868 411 ----VSVCAQDAHL--FDTTVRENLRLARPD---ATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILRdqAKKRKKACIIVTHDE 200
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLL--AALSGRTVVLITHHL 530
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-200 |
2.40e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.64 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDgNRNIEavkDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIT--TMKQKalak 79
Cdd:PRK11432 7 VVLKNITKRFGS-NTVID---NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrSIQQR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 vrmsEIGFILQATNLVPFLTVKQQ--FTLlkkKNKNVMSNEDYQQLMSQLGLTSLL---NKLPSEISGGQKQRVAIAKAL 154
Cdd:PRK11432 79 ----DICMVFQSYALFPHMSLGENvgYGL---KMLGVPKEERKQRVKEALELVDLAgfeDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 579537805 155 YTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDE 200
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQ 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-199 |
2.67e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 100.31 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKST-------FLTMAGAlqTPTSGHILI---NNQ--D 68
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGG--LVQCDKMLLrrrSRQviE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 69 ITTMKQKALAKVRMSEIGFILQA--TNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQLMSQLGLT------SLLNKLPSEI 140
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVripeaqTILSRYPHQL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 141 SGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHD 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-215 |
3.03e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.78 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 31 GDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvrmsEIGFILQATNLVPFLTVKQQFTLLKKK 110
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----KVAYLPQQLPAAEGMTVRELVAIGRYP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 111 NKNVM---SNEDYQQL---MSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRD 184
Cdd:PRK10575 113 WHGALgrfGAADREKVeeaISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
|
170 180 190
....*....|....*....|....*....|..
gi 579537805 185 QAKKRKKACIIVTHDERLKA-YCDRSYHMKDG 215
Cdd:PRK10575 193 LSQERGLTVIAVLHDINMAArYCDYLVALRGG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-215 |
3.55e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKS-TFLTMAGALQTP----TSGHILINNQDITTMKQK 75
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 76 ALAKVRMSEIGFILQA--TNLVPFLTVKQQFT---LLKKKNKNVMSNEDYQQLMSQLGL---TSLLNKLPSEISGGQKQR 147
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYevlSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 148 VAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERL-KAYCDRSYHMKDG 215
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIvRKLADRVAVMQNG 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-215 |
4.98e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.63 E-value: 4.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIT-TMKQKALAKVRmSEIGFILQatnlvpfL 98
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLR-KKVGIVFQ-------F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 99 TVKQQF--TLLKK-----KNKNVmSNEDYQQLMSQL----GLT-SLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEP 166
Cdd:PRK13634 94 PEHQLFeeTVEKDicfgpMNFGV-SEEDAKQKAREMielvGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 579537805 167 TAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKG 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-215 |
5.05e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.73 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNR-NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIT-TMKQKALA 78
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSsTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KVRmSEIGFILQ--ATNLVPFLTVK------QQFTLLKKKNKNVMSNEdyqqlMSQLGLT-SLLNKLPSEISGGQKQRVA 149
Cdd:PRK13643 81 PVR-KKVGVVFQfpESQLFEETVLKdvafgpQNFGIPKEKAEKIAAEK-----LEMVGLAdEFWEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILrDQAKKRKKACIIVTH-DERLKAYCDRSYHMKDG 215
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHlMDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-199 |
5.93e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.41 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVR 81
Cdd:PRK13640 6 VEFKHVSFTYPDSKK--PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQ-ATNLVPFLTVKQQ--FTLlkkKNKNVMSNED---YQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALY 155
Cdd:PRK13640 84 -EKVGIVFQnPDNQFVGATVGDDvaFGL---ENRAVPRPEMikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 579537805 156 TNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-199 |
6.05e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 99.11 E-value: 6.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVkdtnfEINKGDIIALVGPSGSGKSTFLTM-AGALqTPTSGHILINnQDITTMKQKALAK 79
Cdd:PRK13409 340 LVEYPDLTKKLGDFSLEVEGG-----EIYEGEVIGIVGPNGIGKTTFAKLlAGVL-KPDEGEVDPE-LKISYKPQYIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRMseigfilqatnlvpflTVKQqftLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPS 159
Cdd:PRK13409 413 YDG----------------TVED---LLRSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDAD 473
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 579537805 160 IILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-215 |
7.43e-24 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 93.65 E-value: 7.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTmkqKALAKVRMSEIGFIL---QATNLV 95
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAeALFG-LRPPASGEITLDGKPVTR---RSPRDAIRAGIAYVPedrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 96 PFLTVKQqftllkkknknvmsNedyqqlmsqLGLTSLLnklpseiSGGQKQRVAIAKALYTNPSIILADEPTAALDTENA 175
Cdd:cd03215 91 LDLSVAE--------------N---------IALSSLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 579537805 176 IEVIKILRDQAkKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:cd03215 141 AEIYRLIRELA-DAGKAVLLISSElDELLGLCDRILVMYEG 180
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-215 |
9.02e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.44 E-value: 9.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDI---TTMkqKALA 78
Cdd:PRK11288 5 LSFDGIGKTFP----GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTT--AALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 kvrmSEIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSNEdyQQLMSQLGLtsLLNKLPSEI---------SGGQKQRVA 149
Cdd:PRK11288 79 ----AGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNR--RLLNYEARE--QLEHLGVDIdpdtplkylSIGQRQMVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 150 IAKALYTNPSIILADEPTAAL---DTENAIEVIKILRDQAkkrkKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRAEG----RVILYVSHRmEEIFALCDAITVFKDG 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-217 |
1.20e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.38 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 25 NFEINKGDIIALVGPSGSGKSTFL-TMAGALqtPTSGHILINNQDITTMkqkALAKVRmSEIGFILQATNLvPFLTVKQQ 103
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLnALLGFL--PYQGSLKINGIELREL---DPESWR-KHLSWVGQNPQL-PHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 104 FTLLKKKnknvMSNEDYQQLMSQLGLTSLLNKLP-----------SEISGGQKQRVAIAKALYTNPSIILADEPTAALDT 172
Cdd:PRK11174 443 VLLGNPD----ASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 579537805 173 ENAIEVIKILRDQAkkRKKACIIVTHD-ERLKAyCDRSYHMKDGVL 217
Cdd:PRK11174 519 HSEQLVMQALNAAS--RRQTTLMVTHQlEDLAQ-WDQIWVMQDGQI 561
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-215 |
1.21e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.34 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGnRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILI-NNQDITTMKQKala 78
Cdd:COG4178 362 ALALEDLTLRTPDG-RPL--LEDLSLSLKPGERLLITGPSGSGKSTLLrAIAG-LWPYGSGRIARpAGARVLFLPQR--- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 kvrmseigfilqatnlvPFL---TVKQQftLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKL------PSEISGGQKQRVA 149
Cdd:COG4178 435 -----------------PYLplgTLREA--LLYPATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKkrKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP--GTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-215 |
1.81e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 97.57 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRN-IEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSG--HILINNQDITTMKQKAL 77
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 78 AKVRMSE-IGFILQATNLVPFLTVKQQFT----------LLKKKN----KNVMSNEDYQQlmsqlgltSLLNKLPSEISG 142
Cdd:TIGR03269 359 GRGRAKRyIGILHQEYDLYPHRTVLDNLTeaiglelpdeLARMKAvitlKMVGFDEEKAE--------EILDKYPDELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 143 GQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDG 504
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-208 |
2.48e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKSTFLTM-AGALQtPTSGHilinnqdittmkqkaLAKVRMSEIGFILQATNLVPFL 98
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVlAGVLR-PTSGT---------------VRRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 99 --TVKQQFTL-----------LKKKNKNVMSNEdyqqlMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADE 165
Cdd:NF040873 71 plTVRDLVAMgrwarrglwrrLTRDDRAAVDDA-----LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 579537805 166 PTAALDTENAIEVIKILRdQAKKRKKACIIVTHDERLKAYCDR 208
Cdd:NF040873 146 PTTGLDAESRERIIALLA-EEHARGATVVVVTHDLELVRRADP 187
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-207 |
2.87e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALqTPTSGHILINNQDITTMKQKALAK 79
Cdd:PRK09536 3 MIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLrAINGTL-TPTAGTVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 vrmsEIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSNED------YQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKA 153
Cdd:PRK09536 78 ----RVASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTetdraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 154 LYTNPSIILADEPTAALDTENAIEVIKILRDQAKKrKKACIIVTHDERLKA-YCD 207
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAArYCD 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-199 |
3.17e-23 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 97.16 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIEAVkdtnfEINKGDIIALVGPSGSGKSTFLTM-AGALqTPTSGHIlINNQDITTMKQKALAKV 80
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVEGG-----EIREGEVLGIVGPNGIGKTTFAKIlAGVL-KPDEGEV-DEDLKISYKPQYISPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMseigfilqatnlvpflTVKQqftLLKKKNKNVMSNEDYQ-QLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPS 159
Cdd:COG1245 415 DG----------------TVEE---FLRSANTDDFGSSYYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 579537805 160 IILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD 515
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-198 |
3.79e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.56 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKSTFL--------TMAGALqtpTSGHILINNQDITTmKQKALAKVRMsEIGFILQ 90
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmndLIPGAR---VEGEILLDGEDIYD-PDVDVVELRR-RVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 91 ATNlvPF-LTVKQQFT----LLKKKNKNVMSN--EdyqqlmsqlglTSL------------LNKLPSEISGGQKQRVAIA 151
Cdd:COG1117 100 KPN--PFpKSIYDNVAyglrLHGIKSKSELDEivE-----------ESLrkaalwdevkdrLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 579537805 152 KALYTNPSIILADEPTAALD---TENAIEVIKILRDQAkkrkkACIIVTH 198
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDpisTAKIEELILELKKDY-----TIVIVTH 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-205 |
4.18e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 92.71 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 22 KDTNFEINKGDIIALVGPSGSGKSTFLTM-AGALQ-TPTSGHILINNQDITTmkQKALAKvrmseigfilqatNLVPFLT 99
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLlAGALKgTPVAGCVDVPDNQFGR--EASLID-------------AIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 100 VKQQFTLLkkknknvmsnedyqqlmSQLGLTS--LLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIE 177
Cdd:COG2401 112 FKDAVELL-----------------NAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|....*...
gi 579537805 178 VIKILRDQAKKRKKACIIVTHDERLKAY 205
Cdd:COG2401 175 VARNLQKLARRAGITLVVATHHYDVIDD 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-215 |
4.31e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.90 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvr 81
Cdd:PRK10253 8 LRGEQLTLGY--GKYTV--AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 msEIGFILQATNLVPFLTVKQ-----------QFTLLKKKNKNVMSnedyqQLMSQLGLTSLLNKLPSEISGGQKQRVAI 150
Cdd:PRK10253 82 --RIGLLAQNATTPGDITVQElvargryphqpLFTRWRKEDEEAVT-----KAMQATGITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 151 AKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDerLKAYCDRSYH---MKDG 215
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHD--LNQACRYASHliaLREG 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-173 |
5.47e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.57 E-value: 5.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVTKSFkDGNRniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvrms 83
Cdd:PRK13657 337 FDDVSFSY-DNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR---- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 84 EIGFILQ---------ATNLV---PFLTVKQQFTLLKKKNKN--VMSNEDyqqlmsqlGLTSLLNKLPSEISGGQKQRVA 149
Cdd:PRK13657 410 NIAVVFQdaglfnrsiEDNIRvgrPDATDEEMRAAAERAQAHdfIERKPD--------GYDTVVGERGRQLSGGERQRLA 481
|
170 180
....*....|....*....|....
gi 579537805 150 IAKALYTNPSIILADEPTAALDTE 173
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVE 505
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-171 |
6.34e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.98 E-value: 6.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 25 NFEINKGDIIALVGPSGSGKSTFLT-MAGALqtPTSGHILINNQDITTMKQKALAKVRmseiGFILQATNLVPFLTVKQQ 103
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLArMAGLL--PGQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 104 FTLLKKKNKNVMSNED-YQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALY-----TNPS--IILADEPTAALD 171
Cdd:COG4138 90 LALHQPAGASSEAVEQlLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLD 165
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-215 |
9.53e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 95.66 E-value: 9.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVtkSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALaKVR 81
Cdd:PRK11160 339 LTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL-RQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIG---FILQAT---NLvpfltvkqqftLLKKKNKnvmSNEDYQQLMSQLGLTSLLNKLPS----------EISGGQK 145
Cdd:PRK11160 416 ISVVSqrvHLFSATlrdNL-----------LLAAPNA---SDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 146 QRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKkrKKACIIVTHdeRLKA--YCDRSYHMKDG 215
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH--RLTGleQFDRICVMDNG 549
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-203 |
9.61e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 91.76 E-value: 9.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKdgNR-NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKAL-AK 79
Cdd:cd03248 12 VKFQNVTFAYP--TRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLhSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRM-------------SEIGFILQAtnlVPFLTVKQqftLLKKKNKNvmsneDYQQLMsQLGLTSLLNKLPSEISGGQKQ 146
Cdd:cd03248 90 VSLvgqepvlfarslqDNIAYGLQS---CSFECVKE---AAQKAHAH-----SFISEL-ASGYDTEVGEKGSQLSGGQKQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 147 RVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKkaCIIVTHdeRLK 203
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRT--VLVIAH--RLS 210
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-189 |
1.43e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 95.27 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVtkSFK-DGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKV 80
Cdd:COG5265 358 VRFENV--SFGyDPERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmseIGfilqatnLVPfltvkqQFTLLkkKNKNVMSN------------------------------EDYQQLMSQLGLt 130
Cdd:COG5265 434 ----IG-------IVP------QDTVL--FNDTIAYNiaygrpdaseeeveaaaraaqihdfieslpDGYDTRVGERGL- 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 131 sllnKLpseiSGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKR 189
Cdd:COG5265 494 ----KL----SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR 544
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-215 |
1.74e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 27 EINKGDIIALVGPSGSGKSTFL-TMAGALQTPT--SGHILINNQDITTMKQKalakvRMSeiGFILQATNLVPFLTVKQQ 103
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMnALAFRSPKGVkgSGSVLLNGMPIDAKEMR-----AIS--AYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 104 FTL-----LKKKNKNVMSNEDYQQLMSQLGLTSLLNKL---PSE---ISGGQKQRVAIAKALYTNPSIILADEPTAALDT 172
Cdd:TIGR00955 120 LMFqahlrMPRRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 579537805 173 ENAIEVIKILRDQAKKRKKAcIIVTHDERLKAYC--DRSYHMKDG 215
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTI-ICTIHQPSSELFElfDKIILMAEG 243
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-217 |
1.81e-22 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 91.02 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMkqkALAKVR 81
Cdd:cd03244 3 IEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSeIGFILQ------AT---NLVPFltvkqqftllkkknkNVMSNEDYQQLMSQLGLTSLLNKLP-----------SEIS 141
Cdd:cd03244 78 SR-ISIIPQdpvlfsGTirsNLDPF---------------GEYSDEELWQALERVGLKEFVESLPggldtvveeggENLS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 142 GGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKrkkaCIIVTHDERLKAY--CDRSYHMKDGVL 217
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKD----CTVLTIAHRLDTIidSDRILVLDKGRV 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-217 |
1.93e-22 |
|
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: 91.05 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSF------------------KDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHIL 63
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 64 INNQDIttmkqkalakvrmSEIGFilqATNLVPFLTVKQqftllkkknkNV--------MSNEDYQQLM------SQLGl 129
Cdd:cd03220 81 VRGRVS-------------SLLGL---GGGFNPELTGRE----------NIylngrllgLSRKEIDEKIdeiiefSELG- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 130 tSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQaKKRKKACIIVTHDER-LKAYCDR 208
Cdd:cd03220 134 -DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSsIKRLCDR 211
|
....*....
gi 579537805 209 SYHMKDGVL 217
Cdd:cd03220 212 ALVLEKGKI 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-199 |
2.01e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKSTfLTMAGALQTPTSGHILINNQDITTMKQKALAKVRmSEIGFILQATN--LVPF 97
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKST-TGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNssLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 98 LTVKQQFTL-LKKKNKNVMSNEDYQQL---MSQLGL-TSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDT 172
Cdd:PRK15134 379 LNVLQIIEEgLRVHQPTLSAAQREQQViavMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
|
170 180
....*....|....*....|....*..
gi 579537805 173 ENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK15134 459 TVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-216 |
2.90e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.72 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFKDGNRnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKalaKVRmSE 84
Cdd:PRK13647 8 EDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---WVR-SK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 85 IGFILQATNLVPF-LTVKQQFTL------LKKKNKNVMSNEdyqqLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:PRK13647 81 VGLVFQDPDDQVFsSTVWDDVAFgpvnmgLDKDEVERRVEE----ALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILrDQAKKRKKACIIVTHDERLKA-YCDRSYHMKDGV 216
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDVDLAAeWADQVIVLKEGR 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-199 |
3.08e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.35 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVtkSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkQKALAKV 80
Cdd:PRK13648 7 IIVFKNV--SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQATNlVPFLTVKQQFTLLKKKNKNVMSNEDYQ----QLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYT 156
Cdd:PRK13648 82 R-KHIGIVFQNPD-NQFVGSIVKYDVAFGLENHAVPYDEMHrrvsEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 579537805 157 NPSIILADEPTAALDTENAIEVIKILRdQAKKRKKACII-VTHD 199
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVR-KVKSEHNITIIsITHD 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-225 |
4.03e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.00 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFK--DG---NRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQk 75
Cdd:PRK15112 4 LLEVRNLSKTFRyrTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 76 alaKVRMSEIGFILQ--ATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQLMSQLGLTSLL----NKLPSEISGGQKQRVA 149
Cdd:PRK15112 83 ---SYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLpdhaSYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVT-HDERLKaycdrsyHMKDGVLNLEN-ETVE 225
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMK-------HISDQVLVMHQgEVVE 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-195 |
4.70e-22 |
|
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: 89.63 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 6 NVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLtMAGALQTPT----SGHILINNQDITTMKQKAlakvr 81
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLL-KALANRTEGnvsvEGDIHYNGIPYKEFAEKY----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEIGFILQATNLVPFLTVKQ--QFTLLKKKNKNVmsnedyqqlmsqlgltsllnklpSEISGGQKQRVAIAKALYTNPS 159
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTVREtlDFALRCKGNEFV-----------------------RGISGGERKRVSIAEALVSRAS 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 579537805 160 IILADEPTAALDTENAIEVIKILRDQAKKRKKACII 195
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFV 174
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-219 |
4.85e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.34 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVTKSFKDGNR-NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIT-TMKQKALAKVR 81
Cdd:PRK13649 5 LQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITsTSKNKDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQatnlvpfLTVKQQF--TLLKK-----KNKNVmSNEDYQQL----MSQLGLT-SLLNKLPSEISGGQKQRVA 149
Cdd:PRK13649 85 -KKVGLVFQ-------FPESQLFeeTVLKDvafgpQNFGV-SQEEAEALarekLALVGISeSLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTH--DErLKAYCDRSYHMKDGVLNL 219
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFK-KLHQSGMTIVLVTHlmDD-VANYADFVYVLEKGKLVL 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-198 |
5.61e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.63 E-value: 5.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVtkSFKDGNR-NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKv 80
Cdd:TIGR00958 479 IEFQDV--SFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmsEIGFILQAtnlvPFL---TVKQQFT--LLKKKNKNVMSN------EDYQQLMSQlGLTSLLNKLPSEISGGQKQRVA 149
Cdd:TIGR00958 556 ---QVALVGQE----PVLfsgSVRENIAygLTDTPDEEIMAAakaanaHDFIMEFPN-GYDTEVGEKGSQLSGGQKQRIA 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 579537805 150 IAKALYTNPSIILADEPTAALDTEnaievIKILRDQAKKRK-KACIIVTH 198
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAE-----CEQLLQESRSRAsRTVLLIAH 672
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-207 |
7.20e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.39 E-value: 7.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 11 FKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKvrmsEIGFILQ 90
Cdd:PRK10247 15 YLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ----QVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 91 AtnlvPFL---TVKQQFTLLKKKNKNVMSNEDYQQLMSQLGL-TSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEP 166
Cdd:PRK10247 89 T----PTLfgdTVYDNLIFPWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 579537805 167 TAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCD 207
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHAD 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-215 |
7.36e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.63 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 17 NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkQKALAKVRMSeIGFILQATNLVP 96
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENIREVRKF-VGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 97 FLTVKQQFTLLKKKNKNvMSNEDYQQLMSQ----LGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDT 172
Cdd:PRK13652 92 FSPTVEQDIAFGPINLG-LDEETVAHRVSSalhmLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 579537805 173 ENAIEVIKILRDQAKKRKKACIIVTHDERLKA-YCDRSYHMKDG 215
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPeMADYIYVMDKG 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
10-199 |
7.42e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.59 E-value: 7.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 10 SFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRmSEIGFIL 89
Cdd:PRK11831 14 SFTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 90 QATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQLMSQL---GLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEP 166
Cdd:PRK11831 91 QSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLeavGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190
....*....|....*....|....*....|...
gi 579537805 167 TAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK11831 171 FVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-185 |
8.26e-22 |
|
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: 89.66 E-value: 8.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITtmKQKALAK 79
Cdd:COG0410 3 MLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLkAISG-LLPPRSGSIRFDGEDIT--GLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRMSeIGFILQATNLVPFLTVKQQFTL---LKKKNKNVMSNEDY--------QQLMSQLGlTSLlnklpseiSGGQKQRV 148
Cdd:COG0410 76 ARLG-IGYVPEGRRIFPSLTVEENLLLgayARRDRAEVRADLERvyelfprlKERRRQRA-GTL--------SGGEQQML 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 579537805 149 AIAKALYTNPSIILADEPTAALD---TENAIEVIKILRDQ 185
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLApliVEEIFEIIRRLNRE 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-217 |
1.52e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQtPTSGHILINnqdiTTMKqkalak 79
Cdd:COG0488 315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLkLLAGELE-PDSGTVKLG----ETVK------ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 vrmseIGFILQA-TNLVPFLTVKQQFtllkkknKNVMSNEDYQQLMSQLGltSLL------NKLPSEISGGQKQRVAIAK 152
Cdd:COG0488 380 -----IGYFDQHqEELDPDKTVLDEL-------RDGAPGGTEQEVRGYLG--RFLfsgddaFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 153 ALYTNPSIILADEPTAALDtenaIEVIKILRDQAKKRKKACIIVTHDER-LKAYCDRSYHMKDGVL 217
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHDRYfLDRVATRILEFEDGGV 507
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-217 |
2.87e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.21 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRN------------------IEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQtPTSGH 61
Cdd:COG1134 4 MIEVENVSKSYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLkLIAGILE-PTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 62 ILINnqdittmkqkalakvrmSEIGFILQ-ATNLVPFLTVKQqftllkkknkNVMSNedyqqlMSQLGLTS--LLNKLP- 137
Cdd:COG1134 83 VEVN-----------------GRVSALLElGAGFHPELTGRE----------NIYLN------GRLLGLSRkeIDEKFDe 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 138 ----SEI-----------SGGQKQRVAIAKALYTNPSIILADEPTAALDT---ENAIEVIKILRDQAkkrkKACIIVTHD 199
Cdd:COG1134 130 ivefAELgdfidqpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqKKCLARIRELRESG----RTVIFVSHS 205
|
250
....*....|....*....
gi 579537805 200 ER-LKAYCDRSYHMKDGVL 217
Cdd:COG1134 206 MGaVRRLCDRAIWLEKGRL 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-199 |
7.40e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.45 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkalakvrmSEIGFILQATNLVPFLT 99
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG---------AERGVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 100 VKQ------QFTLLKKKNKNVMSnedyQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALD-- 171
Cdd:PRK11248 87 VQDnvafglQLAGVEKMQRLEIA----HQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDaf 162
|
170 180 190
....*....|....*....|....*....|
gi 579537805 172 TENAIE--VIKILRDQAKKrkkaCIIVTHD 199
Cdd:PRK11248 163 TREQMQtlLLKLWQETGKQ----VLLITHD 188
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-215 |
8.78e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 8.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQTPT-SGHILINNQdittmKQKAlA 78
Cdd:PRK13549 5 LLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMkVLSGVYPHGTyEGEIIFEGE-----ELQA-S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KVRMSE---IGFILQATNLVPFLTVKQQFTLLKKKNKNVMSNED-----YQQLMSQLGLTSLLNKLPSEISGGQKQRVAI 150
Cdd:PRK13549 75 NIRDTEragIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDamylrAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 151 AKALYTNPSIILADEPTAALdTENAIEV-IKILRDqAKKRKKACIIVTH--DErLKAYCDRSYHMKDG 215
Cdd:PRK13549 155 AKALNKQARLLILDEPTASL-TESETAVlLDIIRD-LKAHGIACIYISHklNE-VKAISDTICVIRDG 219
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-183 |
9.87e-21 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 86.68 E-value: 9.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkQKALAKvr 81
Cdd:TIGR03740 1 LETKNLSKRFG----KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT---RKDLHK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mseIGFILQA----TNLVPFLTVKQQFTLLKkknknvMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:TIGR03740 72 ---IGSLIESpplyENLTARENLKVHTTLLG------LPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNH 142
|
170 180
....*....|....*....|....*.
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILR 183
Cdd:TIGR03740 143 PKLLILDEPTNGLDPIGIQELRELIR 168
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-185 |
1.17e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 86.42 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkALAKVRMSeIGFILQATNLVPFL 98
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP--PHERARAG-IAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 99 TVKQQ----FTLLKKKNKNVMsnEDYQQLMSQLglTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAAL---- 170
Cdd:TIGR03410 91 TVEENlltgLAALPRRSRKIP--DEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIqpsi 166
|
170
....*....|....*..
gi 579537805 171 --DTEnaiEVIKILRDQ 185
Cdd:TIGR03410 167 ikDIG---RVIRRLRAE 180
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-215 |
2.28e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 86.04 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALqTPTSGHILINNQD-----ITTMKQ 74
Cdd:TIGR02323 3 LLQVSGLSKSYG----GGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLgCLAGRL-APDHGTATYIMRSgaeleLYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 75 KALAKVRMSEIGFILQAtnlvPFLTVKQQFTLLKKKNKNVMS---------NEDYQQLMSQLGL-TSLLNKLPSEISGGQ 144
Cdd:TIGR02323 78 AERRRLMRTEWGFVHQN----PRDGLRMRVSAGANIGERLMAigarhygniRATAQDWLEEVEIdPTRIDDLPRAFSGGM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579537805 145 KQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD---ERLKAycDRSYHMKDG 215
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDlgvARLLA--QRLLVMQQG 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-199 |
2.71e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.76 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 16 RNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRmSEIGFILQA--TN 93
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 94 LVPFLTVKqqFTLLKK-KNKNVMSNEDYQQ----LMSQLGLTSLLN-KLPSEISGGQKQRVAIAKALYTNPSIILADEPT 167
Cdd:PRK10261 414 LDPRQTVG--DSIMEPlRVHGLLPGKAAAArvawLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190
....*....|....*....|....*....|..
gi 579537805 168 AALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHD 523
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-225 |
4.31e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.94 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQT--PTSGHILIN-------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 66 --------------NQDITTMK-QKALAKVRMSEIGFILQATnlvpfltvkqqFTLLKKKN--KNVM-SNED--YQ---- 121
Cdd:TIGR03269 77 kvgepcpvcggtlePEEVDFWNlSDKLRRRIRKRIAIMLQRT-----------FALYGDDTvlDNVLeALEEigYEgkea 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 122 -----QLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIV 196
Cdd:TIGR03269 146 vgravDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLT 225
|
250 260 270
....*....|....*....|....*....|
gi 579537805 197 TH-DERLKAYCDRSYHMKDGVLNLENETVE 225
Cdd:TIGR03269 226 SHwPEVIEDLSDKAIWLENGEIKEEGTPDE 255
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-198 |
5.19e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.44 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRN-IEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILI----NNQDITTMKQ- 74
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENeLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 75 --------KALAKVRMSeIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQ---LMSQLGL-TSLLNKLPSEISG 142
Cdd:PRK13631 101 tnpyskkiKNFKELRRR-VSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLakfYLNKMGLdDSYLERSPFGLSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 143 GQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDqAKKRKKACIIVTH 198
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITH 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-198 |
8.31e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.51 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGAL-----QTPTSGHILINNQDITTMKQKALaKVRmSEIGFILQATN 93
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPI-EVR-REVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 94 LVPFLTVKQQFTLLKKKNKNVMSNEDYQQLMS-QLGLTSL-------LNKLPSEISGGQKQRVAIAKALYTNPSIILADE 165
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALwdevkdrLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190
....*....|....*....|....*....|...
gi 579537805 166 PTAALDTENAIEVIKILRDQakKRKKACIIVTH 198
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFEL--KKEYTIVLVTH 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-208 |
9.11e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.04 E-value: 9.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILInnQDITTMKQKALAKVR 81
Cdd:PRK13536 42 IDLAGVSKSY--GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--LGVPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mseIGFILQATNLVPFLTVKQQFTLLKKKNKnvMSNEDYQQLMSQL----GLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:PRK13536 116 ---IGVVPQFDNLDLEFTVRENLLVFGRYFG--MSTREIEAVIPSLlefaRLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTH----DERLkayCDR 208
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHfmeeAERL---CDR 241
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-171 |
1.07e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.21 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 24 TNFEINKGDIIALVGPSGSGKSTFLT-MAGALqtPTSGHILINNQDITTMKQKALAKVRmseiGFILQATNLVPFLTVKQ 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArMAGLL--PGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 103 QFTL-LKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALY-----TNPS--IILADEPTAALD 171
Cdd:PRK03695 89 YLTLhQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLD 165
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-217 |
1.44e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.98 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKStfLTMAGALQ------TPTSGHILINNQDIttmkqkALAKVRMSEIGFILQ---- 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPV------APCALRGRKIATIMQnprs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 91 ATNLVPFLTVKQQFTLL---KKKNKNVMSnedyqQLMSQLGLTS---LLNKLPSEISGGQKQRVAIAKALYTNPSIILAD 164
Cdd:PRK10418 91 AFNPLHTMHTHARETCLalgKPADDATLT-----AALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579537805 165 EPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYC-DRSYHMKDGVL 217
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRI 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
26-201 |
1.54e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 82.79 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 26 FEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTmkqkaLAKVRMSEIGFILQATNLVPFLTVKQQF 104
Cdd:TIGR01189 21 FTLNAGEALQVTGPNGIGKTTLLrILAG-LLRPDSGEVRWNGTPLAE-----QRDEPHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 105 TLLkkknknvmsNEDYQ-------QLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDtENAIE 177
Cdd:TIGR01189 95 HFW---------AAIHGgaqrtieDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-KAGVA 164
|
170 180
....*....|....*....|....
gi 579537805 178 VIKILRDQAKKRKKACIIVTHDER 201
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-215 |
1.60e-19 |
|
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: 86.42 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGAL--QTPTSGHILINNQDIttmKQKALA 78
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPL---KASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KVRMSEIGFILQATNLVPFLTVKQQFTL---LKKKNKNVMSNEDY---QQLMSQLGLTSLLNKLP-SEISGGQKQRVAIA 151
Cdd:TIGR02633 74 DTERAGIVIIHQELTLVPELSVAENIFLgneITLPGGRMAYNAMYlraKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 152 KALYTNPSIILADEPTAALdTENAIEV-IKILRDqAKKRKKACIIVTHD-ERLKAYCDRSYHMKDG 215
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSL-TEKETEIlLDIIRD-LKAHGVACVYISHKlNEVKAVCDTICVIRDG 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-215 |
2.27e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.19 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 22 KDTNFEINKGDIIALVGPSGSGKSTF-LTMAG-ALQTPTSGHILINNQDITTMK--QKALAKVRMS-----EIgfilqat 92
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLaKVLMGhPKYEVTSGSILLDGEDILELSpdERARAGIFLAfqypvEI------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 93 nlvPFLTVKQqF--TLLKKKNKNVMSNEDYQ----QLMSQLGL-TSLLNK-LPSEISGGQKQRVAIAKALYTNPSIILAD 164
Cdd:COG0396 90 ---PGVSVSN-FlrTALNARRGEELSAREFLkllkEKMKELGLdEDFLDRyVNEGFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 165 EPTAALDtenaIEVIKILRD---QAKKRKKACIIVTHDERLKAY--CDRSYHMKDG 215
Cdd:COG0396 166 ETDSGLD----IDALRIVAEgvnKLRSPDRGILIITHYQRILDYikPDFVHVLVDG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-215 |
2.91e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 82.07 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkaLAKVRmSEIGFILQATNLvpfl 98
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLR-SSLTIIPQDPTL---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 99 tvkqqFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLpseiSGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEV 178
Cdd:cd03369 94 -----FSGTIRSNLDPFDEYSDEEIYGALRVSEGGLNL----SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 579537805 179 IKILRDQAKkrKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:cd03369 165 QKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAG 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-215 |
3.41e-19 |
|
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: 81.80 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGnrniEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAG-ALQTPTSGHILINNQDIT--TMKQKAL 77
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAkTIMGhPKYEVTEGEILFKGEDITdlPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 78 AKVRMSeigfiLQATNLVPFLTVKqqfTLLKKKNKNvmsnedyqqlmsqlgltsllnklpseISGGQKQRVAIAKALYTN 157
Cdd:cd03217 77 LGIFLA-----FQYPPEIPGVKNA---DFLRYVNEG--------------------------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 158 PSIILADEPTAALDTEN---AIEVIKILRDQakkrKKACIIVTHDERLKAYC--DRSYHMKDG 215
Cdd:cd03217 123 PDLAILDEPDSGLDIDAlrlVAEVINKLREE----GKSVLIITHYQRLLDYIkpDRVHVLYDG 181
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-222 |
4.16e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.11 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDitTMKQKALAKV 80
Cdd:PRK13644 1 MIRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQ--ATNLVPfLTVKQQFTlLKKKNKNVMSNEDYQQL---MSQLGLTSLLNKLPSEISGGQKQRVAIAKALY 155
Cdd:PRK13644 76 R-KLVGIVFQnpETQFVG-RTVEEDLA-FGPENLCLPPIEIRKRVdraLAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 156 TNPSIILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHD-ERLKAyCDRSYHMKDGVLNLENE 222
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIK-KLHEKGKTIVYITHNlEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-215 |
1.23e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 81.51 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNRNieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKAL--A 78
Cdd:PRK11701 6 LLSVRGLTKLY--GPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KVRM---SEIGFILQ--ATNLVPFLTVkqqftllkkkNKNV----MS--NEDYQQL-------MSQLGL-TSLLNKLPSE 139
Cdd:PRK11701 82 ERRRllrTEWGFVHQhpRDGLRMQVSA----------GGNIgerlMAvgARHYGDIratagdwLERVEIdAARIDDLPTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 140 ISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD---ERLKAycDRSYHMKDG 215
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDlavARLLA--HRLLVMKQG 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-223 |
1.74e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.98 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGAL-----QTPTSGHILINNQDITTMKQKALaKVRmSEIGFILQATN 93
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTV-DLR-KEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 94 LVPFL---TVKQQFTLLKKKNKNVMSnedyQQLMSQLGLTSLLNKLPSEI-------SGGQKQRVAIAKALYTNPSIILA 163
Cdd:PRK14239 97 PFPMSiyeNVVYGLRLKGIKDKQVLD----EAVEKSLKGASIWDEVKDRLhdsalglSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 164 DEPTAALDTENAIEVIKILrdQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVLNLENET 223
Cdd:PRK14239 173 DEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSmQQASRISDRTGFFLDGDLIEYNDT 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-208 |
4.68e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.62 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVr 81
Cdd:PRK13537 8 IDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mseiGFILQATNLVPFLTVKQQFTLLKKKNKnvMSNEDYQQLMSQL----GLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:PRK13537 83 ----GVVPQFDNLDPDFTVRENLLVFGRYFG--LSAAAARALVPPLlefaKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAkKRKKACIIVTH----DERLkayCDR 208
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHfmeeAERL---CDR 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-215 |
5.90e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.59 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKAlakV 80
Cdd:PRK10762 4 LLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS---S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATNLVPFLTVKQQFtLLKKKNKNVMSNEDYQQ-------LMSQLGLTSLLNKLPSEISGGQKQRVAIAKA 153
Cdd:PRK10762 77 QEAGIGIIHQELNLIPQLTIAENI-FLGREFVNRFGRIDWKKmyaeadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 154 LYTNPSIILADEPTAAL-DTENA--IEVIKILRDQakkrkkACIIVTHDERLK---AYCDRSYHMKDG 215
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTETEslFRVIRELKSQ------GRGIVYISHRLKeifEICDDVTVFRDG 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-198 |
6.32e-18 |
|
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: 78.69 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 26 FEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQdittmkqkALAKVRMS---EIGFILQATNLVPFLTVKQ 102
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG--------PLDFQRDSiarGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 103 QFTLLKKKNknvmSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDtENAIEVIKIL 182
Cdd:cd03231 93 NLRFWHADH----SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGVARFAEA 167
|
170
....*....|....*.
gi 579537805 183 RDQAKKRKKACIIVTH 198
Cdd:cd03231 168 MAGHCARGGMVVLTTH 183
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-195 |
8.60e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.22 E-value: 8.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTksFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIttmKQKALAKVR 81
Cdd:PRK11176 342 IEFRNVT--FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQ---------ATNLVpfLTVKQQFTLLKKKNKNVMSNE-DYQQLMSQlGLTSLLNKLPSEISGGQKQRVAIA 151
Cdd:PRK11176 417 -NQVALVSQnvhlfndtiANNIA--YARTEQYSREQIEEAARMAYAmDFINKMDN-GLDTVIGENGVLLSGGQRQRIAIA 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 579537805 152 KALYTNPSIILADEPTAALDTENAIEVIKILrDQAKKRKKACII 195
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAAL-DELQKNRTSLVI 535
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-217 |
2.51e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKS-TFLTMAGALQtPTSGHILINNQDITTMK-QKALAKvrmseiGFIL-----QA 91
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTeLARALFGADP-ADSGEIRLDGKPVRIRSpRDAIRA------GIAYvpedrKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 92 TNLVPFLTVKQQFTL--LKKKNKN-VMS----NEDYQQLMSQLGL-TSLLNKLPSEISGGQKQRVAIAKALYTNPSIILA 163
Cdd:COG1129 339 EGLVLDLSIRENITLasLDRLSRGgLLDrrreRALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 164 DEPTAALDTENAIEVIKILRDQAkKRKKACIIVT--HDErLKAYCDRSYHMKDGVL 217
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELA-AEGKAVIVISseLPE-LLGLSDRILVMREGRI 472
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
7-215 |
5.69e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 76.22 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 7 VTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQTpTSGHILINNQDITTMKQKALAKVRMSEI 85
Cdd:cd03290 3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 86 GFILQATNLVPfLTVKQQFTLLKKKNKnvmsnEDYQQLMSQLGLTSLLNKLP----SEI-------SGGQKQRVAIAKAL 154
Cdd:cd03290 82 AYAAQKPWLLN-ATVEENITFGSPFNK-----QRYKAVTDACSLQPDIDLLPfgdqTEIgerginlSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 155 YTNPSIILADEPTAALD---TENAIE--VIKILRDQakkrKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:cd03290 156 YQNTNIVFLDDPFSALDihlSDHLMQegILKFLQDD----KRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-214 |
6.62e-17 |
|
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: 74.88 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNieaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHIlinnqdittmkqkalAKV 80
Cdd:cd03223 1 IELENLSLATPDGRVL---LKDLSFEIKPGDRLLITGPSGTGKSSLFrALAG-LWPWGSGRI---------------GMP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATnLVPFLTVKQQftllkkknknvmsnedyqqlmsqlgltsLLNKLPSEISGGQKQRVAIAKALYTNPSI 160
Cdd:cd03223 62 EGEDLLFLPQRP-YLPLGTLREQ----------------------------LIYPWDDVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579537805 161 ILADEPTAALDTENAIEVIKILRDqakkRKKACIIVTHDERLKAYCDRSYHMKD 214
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKE----LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-199 |
1.46e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVTKSF-KDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITT--MKQKALAKV 80
Cdd:PRK13645 9 LDNVSYTYaKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmSEIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQLMSQLGLTSL----LNKLPSEISGGQKQRVAIAKALYT 156
Cdd:PRK13645 89 R-KEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 579537805 157 NPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHN 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-204 |
1.69e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFLTMAGAL------QTPTSGHILINNQDITTMKQKALAKvrmsEIGFILQATNL 94
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 95 VPFLTVKQQFTLlKKKNKNVMSNEDYQQLMSQ----LGL----TSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEP 166
Cdd:PRK14246 102 FPHLSIYDNIAY-PLKSHGIKEKREIKKIVEEclrkVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 579537805 167 TAALDTENAIEVIKILRDQakKRKKACIIVTHDERLKA 204
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVA 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-198 |
1.72e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.76 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINnqDITTMKQKALAKVR 81
Cdd:PTZ00265 383 IQFKNVRFHY-DTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mSEIGFILQAtnlvPFL---TVKQ--QFTLLKKKNKNVMSNE------------------------DYQQLMSQLGLTSL 132
Cdd:PTZ00265 460 -SKIGVVSQD----PLLfsnSIKNniKYSLYSLKDLEALSNYynedgndsqenknkrnscrakcagDLNDMSNTTDSNEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 133 L---------------------------NKLP-----------SEISGGQKQRVAIAKALYTNPSIILADEPTAALDTEN 174
Cdd:PTZ00265 535 IemrknyqtikdsevvdvskkvlihdfvSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260
....*....|....*....|....
gi 579537805 175 AIEVIKILRDQAKKRKKACIIVTH 198
Cdd:PTZ00265 615 EYLVQKTINNLKGNENRITIIIAH 638
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-208 |
2.26e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.48 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFltmAGAL--QTPTSGHI-----LINNQDITTMK 73
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLI---AKAIcgITKDNWHVtadrfRWNGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 74 QKALAKVRMSEIGFILQ--ATNLVPFLTVKQQFtllkkknKNVMSNEDY---------------QQLMSQLGL---TSLL 133
Cdd:COG4170 80 PRERRKIIGREIAMIFQepSSCLDPSAKIGDQL-------IEAIPSWTFkgkwwqrfkwrkkraIELLHRVGIkdhKDIM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 134 NKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDR 208
Cdd:COG4170 153 NSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADT 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-199 |
2.46e-16 |
|
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: 75.48 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 31 GDIIALVGPSGSGKSTFLTMAGALQTPTSGHiLINNQDITTMK--------QKALAKVRMSEIGFIL--QATNLVPfltv 100
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILdefrgselQNYFTKLLEGDVKVIVkpQYVDLIP---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 101 kQQFT-----LLKKKNKNVMSNEdyqqLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENA 175
Cdd:cd03236 101 -KAVKgkvgeLLKKKDERGKLDE----LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|....
gi 579537805 176 IEVIKILRDQAKKrKKACIIVTHD 199
Cdd:cd03236 176 LNAARLIRELAED-DNYVLVVEHD 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-172 |
2.95e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 16 RNIEAV-KDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITtmkqkaLAKVRmSEIGFILQATN 93
Cdd:PRK13539 12 RGGRVLfSGLSFTLAAGEALVLTGPNGSGKTTLLrLIAG-LLPPAAGTIKLDGGDID------DPDVA-EACHYLGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 94 LVPFLTVKQ--QFTllkkknKNVMSNEDYQ--QLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAA 169
Cdd:PRK13539 84 MKPALTVAEnlEFW------AAFLGGEELDiaAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
...
gi 579537805 170 LDT 172
Cdd:PRK13539 158 LDA 160
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-202 |
6.63e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHIlinnqdittmkqKALAKV 80
Cdd:PRK09544 4 LVSLENVSVSF--GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RmseIGFILQATNLVPF--LTVKQqFTLLKKKNKNvmsnEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:PRK09544 68 R---IGYVPQKLYLDTTlpLTVNR-FLRLRPGTKK----EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 579537805 159 SIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERL 202
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-214 |
6.89e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 75.70 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVTKSFKDGNRnieavkdtnfeinkgdiIALVGPSGSGKSTFLTMAGALQTPTSGHILI-NNQDITTMKQKALAKVRM 82
Cdd:PRK15064 17 FENISVKFGGGNR-----------------YGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQFAFEEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 SEIGFILQA-TNLvpfLTVKQQ----FTLLKkknknvMSNEDYQ----------------------QLMSQLGL-TSLLN 134
Cdd:PRK15064 80 TVLDTVIMGhTEL---WEVKQErdriYALPE------MSEEDGMkvadlevkfaemdgytaearagELLLGVGIpEEQHY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 135 KLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDtenaIEVIKILRDQAKKRKKACIIVTHDER-LKAYCDrsyHMK 213
Cdd:PRK15064 151 GLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----INTIRWLEDVLNERNSTMIIISHDRHfLNSVCT---HMA 223
|
.
gi 579537805 214 D 214
Cdd:PRK15064 224 D 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-215 |
7.03e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.87 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAK---VRMseigfiLQATNLVP 96
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARmgvVRT------FQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 97 FLTVKQQftLLKKKNKNVMSN-------------------EDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:PRK11300 94 EMTVIEN--LLVAQHQQLKTGlfsgllktpafrraesealDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 158 PSIILADEPTAAL---DTENAIEVIKILRDQakkRKKACIIVTHDERL-KAYCDRSYHMKDG 215
Cdd:PRK11300 172 PEILMLDEPAAGLnpkETKELDELIAELRNE---HNVTVLLIEHDMKLvMGISDRIYVVNQG 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-215 |
1.12e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.97 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKv 80
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 rmsEIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLN---KLPSEISGGQKQRVAIAKALYTN 157
Cdd:PRK13642 82 ---KIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDfktREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAG 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-217 |
1.23e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.76 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFKDGNrniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIT-TMKQKALAKVRMS 83
Cdd:PRK15056 10 NDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 84 E---IGFILQATNLVPFLTVKQQFTLLKKKNKNvmsNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSI 160
Cdd:PRK15056 87 EevdWSFPVLVEDVVMMGRYGHMGWLRRAKKRD---RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 161 ILADEPTAALDTENAIEVIKILRdQAKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLR-ELRDEGKTMLVSTHNlGSVTEFCDYTVMVKGTVL 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-199 |
2.46e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQ--TPT---SGHILINNQDITTmKQKALAKVRmSEIGFILQATNL 94
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlIPGfrvEGKVTFHGKNLYA-PDVDPVEVR-RRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 95 VPfltvkqqftllkkknKNVMSN-------EDYQQLMSQLGLTSL------------LNKLPSEISGGQKQRVAIAKALY 155
Cdd:PRK14243 103 FP---------------KSIYDNiaygariNGYKGDMDELVERSLrqaalwdevkdkLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 579537805 156 TNPSIILADEPTAALD---TENAIEVIKILrdqakKRKKACIIVTHD 199
Cdd:PRK14243 168 VQPEVILMDEPCSALDpisTLRIEELMHEL-----KEQYTIIIVTHN 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-198 |
4.47e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 73.62 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVrmseIGFILQAtnlvPFL 98
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF----INYLPQE----PYI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 99 TVKQQFTLLKKKNKNVMSNEDYQQLMS-----------QLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPT 167
Cdd:TIGR01193 560 FSGSILENLLLGAKENVSQDEIWAACEiaeikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190
....*....|....*....|....*....|.
gi 579537805 168 AALDTenaIEVIKILRDQAKKRKKACIIVTH 198
Cdd:TIGR01193 640 SNLDT---ITEKKIVNNLLNLQDKTIIFVAH 667
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-225 |
5.53e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQkalAKV 80
Cdd:PRK15439 11 LLCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP---AKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQATNLVPFLTVKQQFTL-LKKKNKnvmSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPS 159
Cdd:PRK15439 84 HQLGIYLVPQEPLLFPNLSVKENILFgLPKRQA---SMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 160 IILADEPTAAL---DTENAIEVIKILRDQAkkrkKACIIVTHDER-LKAYCDRSYHMKDGVLNLENETVE 225
Cdd:PRK15439 161 ILILDEPTASLtpaETERLFSRIRELLAQG----VGIVFISHKLPeIRQLADRISVMRDGTIALSGKTAD 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
7.79e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.06 E-value: 7.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQTpTSGHILINNQDITtmkQKALAK 79
Cdd:PRK11614 5 MLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLgTLCGDPRA-TSGRIVFDGKDIT---DWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 VRMSEIGFILQATNLVPFLTVKQQFTLlkkkNKNVMSNEDYQQLMSQL-GLTSLLNKLPSE----ISGGQKQRVAIAKAL 154
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEENLAM----GGFFAERDQFQERIKWVyELFPRLHERRIQragtMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 155 YTNPSIILADEPTAALdteNAIEVIKILRDQAKKRKKACIIV----THDERLKaYCDRSYHMKDGVLNLEN 221
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQLREQGMTIFlveqNANQALK-LADRGYVLENGHVVLED 219
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-217 |
1.17e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.31 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVr 81
Cdd:PRK10522 323 LELRNVTFAYQDNGF---SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mseigfilqatnlvpFLTVkqqFT-------LLKKKNKNVmSNEDYQQLMSQLGLTSLL----NKLPS-EISGGQKQRVA 149
Cdd:PRK10522 399 ---------------FSAV---FTdfhlfdqLLGPEGKPA-NPALVEKWLERLKMAHKLeledGRISNlKLSKGQKKRLA 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-223 |
1.35e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.90 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 33 IIALVGPSGSGKSTFLTMAGALQTPTSGH-----ILINNQDITTMKQKALAKVRmseIGFILQATNlvPFLTVKQQFTLL 107
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRR---VGMLFQRPN--PFPMSIMDNVLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 108 KKKNKNVMSNEDY----QQLMSQLGL----TSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALD---TENAI 176
Cdd:PRK14271 124 GVRAHKLVPRKEFrgvaQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDpttTEKIE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 579537805 177 EVIKILRDqakkrKKACIIVTHDERLKA-YCDRSYHMKDGVLNLENET 223
Cdd:PRK14271 204 EFIRSLAD-----RLTVIIVTHNLAQAArISDRAALFFDGRLVEEGPT 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-218 |
1.71e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKQKA-LAK--VRMSE----IGFILQ 90
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAeTLYG-LRPARGGRIMLNGKEINALSTAQrLARglVYLPEdrqsSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 91 AT---NLVPFLTVKQQFTLLKKKNKNVMsnEDYQQlmsQLGLT-SLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEP 166
Cdd:PRK15439 356 APlawNVCALTHNRRGFWIKPARENAVL--ERYRR---ALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 579537805 167 TAALDTENAIEVIKILRDQAKKrKKACIIVTHD-ERLKAYCDRSYHMKDGVLN 218
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDlEEIEQMADRVLVMHQGEIS 482
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-171 |
8.11e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.04 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFKDGNRniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTmkqkALAKVRMSe 84
Cdd:TIGR01257 932 KNLVKIFEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQS- 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 85 IGFILQATNLVPFLTVKQQ---FTLLKKKNKNVMSNEdYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSII 161
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHilfYAQLKGRSWEEAQLE-MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170
....*....|
gi 579537805 162 LADEPTAALD 171
Cdd:TIGR01257 1084 VLDEPTSGVD 1093
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-185 |
1.08e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.36 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 4 FENVTKSFKDGNRnieAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAK-VRM 82
Cdd:PRK10790 343 IDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQgVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 seigfiLQATNLVPFLTVKQQFTLLKKknknvMSNEDYQQLMSQLGLTSLLNKLPSEI-----------SGGQKQRVAIA 151
Cdd:PRK10790 420 ------VQQDPVVLADTFLANVTLGRD-----ISEEQVWQALETVQLAELARSLPDGLytplgeqgnnlSVGQKQLLALA 488
|
170 180 190
....*....|....*....|....*....|....*..
gi 579537805 152 KALYTNPSIILADEPTAALD--TENAIE-VIKILRDQ 185
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDsgTEQAIQqALAAVREH 525
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-199 |
2.20e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkDGNRNIEAVkdtNFEINKGDIIALVGPSGSGKSTFLTMAGAL-----QTPTSGHILINNQDITTmKQKA 76
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGV---SMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYE-RRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 77 LAKVRmSEIGFILQATNLVP---FLTVKQQFTLLKKKNK---------NVMSNEDYQQLMSQLGLTSLlnklpsEISGGQ 144
Cdd:PRK14258 83 LNRLR-RQVSMVHPKPNLFPmsvYDNVAYGVKIVGWRPKleiddivesALKDADLWDEIKHKIHKSAL------DLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 145 KQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-215 |
3.87e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAG-ALQTPTSGHILINNQDITTMKQKALA 78
Cdd:CHL00131 7 ILEIKNLHASVNE----NEILKGLNLSINKGEIHAIMGPNGSGKSTLSkVIAGhPAYKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KvrmseIGFILQATNLVPFLTV-KQQFTLLKKKNKNVMSN-------EDYQQLMSQLGLTSL----LNKLPSE-ISGGQK 145
Cdd:CHL00131 83 H-----LGIFLAFQYPIEIPGVsNADFLRLAYNSKRKFQGlpeldplEFLEIINEKLKLVGMdpsfLSRNVNEgFSGGEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 146 QRVAIAKALYTNPSIILADEPTAALDTEnAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSY-H-MKDG 215
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDID-ALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYvHvMQNG 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-198 |
3.99e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.51 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQTPT-SGHILINNQdittmkQKALA 78
Cdd:NF040905 1 ILEMRGITKTFP----GVKALDDVNLSVREGEIHALCGENGAGKSTLMkVLSGVYPHGSyEGEILFDGE------VCRFK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KVRMSE---IGFILQATNLVPFLTVKQQFTLLKKKNKN-VMS----NEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAI 150
Cdd:NF040905 71 DIRDSEalgIVIIHQELALIPYLSIAENIFLGNERAKRgVIDwnetNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 579537805 151 AKALYTNPSIILADEPTAAL---DTENAIEVIKILRDQAkkrkKACIIVTH 198
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALneeDSAALLDLLLELKAQG----ITSIIISH 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-217 |
4.43e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 16 RNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVRMSEIGFILQATNLV 95
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 96 PFLTVKQQFTLLK-------KKNKNVMSNEDYQQLM-SQLGLTSL----LNKLPSEISGGQKQRVAIAKALYTNPSIILA 163
Cdd:PRK09700 354 PNFSIAQNMAISRslkdggyKGAMGLFHEVDEQRTAeNQRELLALkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579537805 164 DEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-186 |
4.54e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.83 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGAL---QTPTSGHILINNQDITTMKqkalaKVRMSEIGFILQATNLVP 96
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTdgfHIGVEGVITYDGITPEEIK-----KHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 97 FLTVKQqfTL-----LKKKNKNVM--SNEDYQQ-----LMSQLGL-----TSLLNKLPSEISGGQKQRVAIAKALYTNPS 159
Cdd:TIGR00956 152 HLTVGE--TLdfaarCKTPQNRPDgvSREEYAKhiadvYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAK 229
|
170 180
....*....|....*....|....*..
gi 579537805 160 IILADEPTAALDTENAIEVIKILRDQA 186
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSA 256
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-217 |
4.70e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.84 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 10 SFKDGNRNIEA------VKDTNFEINKGDIIALVGPSGSGKSTFLT-MAGALQTPTSGHILInnqdittmkQKALAKVrm 82
Cdd:PLN03130 616 SIKNGYFSWDSkaerptLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI---------RGTVAYV-- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 SEIGFILQAT---NLV---PFLTVKqqftllkkknknvmsnedYQQLMSQLGLTSLLNKLPS-----------EISGGQK 145
Cdd:PLN03130 685 PQVSWIFNATvrdNILfgsPFDPER------------------YERAIDVTALQHDLDLLPGgdlteigergvNISGGQK 746
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 146 QRVAIAKALYTNPSIILADEPTAALDTENAIEVI-KILRDQAkkRKKACIIVTHDERLKAYCDRSYHMKDGVL 217
Cdd:PLN03130 747 QRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDEL--RGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-202 |
4.96e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIttmkQKALAKVRmSEIGFILQATNLVPFLTV 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 101 KQQ--FTLLKKKnknvmSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDtENAIEV 178
Cdd:PRK13540 92 RENclYDIHFSP-----GAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-ELSLLT 165
|
170 180
....*....|....*....|....
gi 579537805 179 IkILRDQAKKRKKACIIVTHDERL 202
Cdd:PRK13540 166 I-ITKIQEHRAKGGAVLLTSHQDL 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-199 |
5.03e-13 |
|
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: 67.27 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNqditTMKqkaLAKVR 81
Cdd:TIGR03719 323 IEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE----TVK---LAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 MSEigfilqaTNLVPFLTVKQQFT----LLKKKNKNVMS----------NEDYQQLMSQLgltsllnklpseiSGGQKQR 147
Cdd:TIGR03719 392 QSR-------DALDPNKTVWEEISggldIIKLGKREIPSrayvgrfnfkGSDQQKKVGQL-------------SGGERNR 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 579537805 148 VAIAKALYTNPSIILADEPTAALDtenaIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHD 499
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-202 |
6.29e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 67.19 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 22 KDTNFEINKGDIIALVGPSGSGKSTFLTM-AGALQtPTSGHILINnqdittmkqkalAKVRMSEI------GFILQATnl 94
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLiSGELQ-PSSGTVFRS------------AKVRMAVFsqhhvdGLDLSSN-- 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 95 vPFLTVKQQFTLLKKknknvmsnedyQQLMSQLGLTSLLNKLPSE----ISGGQKQRVAIAKALYTNPSIILADEPTAAL 170
Cdd:PLN03073 591 -PLLYMMRCFPGVPE-----------QKLRAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180 190
....*....|....*....|....*....|..
gi 579537805 171 DTENAIEVIKILrdqaKKRKKACIIVTHDERL 202
Cdd:PLN03073 659 DLDAVEALIQGL----VLFQGGVLMVSHDEHL 686
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-199 |
7.88e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 66.73 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 30 KGDIIALVGPSGSGKSTFLTM-AGALqTPTSGhilinNQDITTMKQKALAKVRMSEIGFIL--------------QATNL 94
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKIlSGEL-KPNLG-----DYDEEPSWDEVLKRFRGTELQDYFkklangeikvahkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 95 VPFL---TVKQqftLLKKKNKNVMSNEdyqqLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALD 171
Cdd:COG1245 172 IPKVfkgTVRE---LLEKVDERGKLDE----LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180
....*....|....*....|....*...
gi 579537805 172 TENAIEVIKILRDQAKKrKKACIIVTHD 199
Cdd:COG1245 245 IYQRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-208 |
8.67e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 14 GNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINNQDITTMKQkalAKVRMSEIGFIL--- 89
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAeALAG-LRPPASGSIRLDGEDITGLSP---RERRRLGVAYIPedr 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 90 QATNLVPFLTVKQQFTL----LKKKNKNVMSNEDY-----QQLMSQLGLtsllnKLPSE------ISGGQKQRVAIAKAL 154
Cdd:COG3845 343 LGRGLVPDMSVAENLILgryrRPPFSRGGFLDRKAirafaEELIEEFDV-----RTPGPdtparsLSGGNQQKVILAREL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 155 YTNPSIILADEPTAALDtENAIEVI-KILRDQAKKRkKACIIVTHD-ERLKAYCDR 208
Cdd:COG3845 418 SRDPKLLIAAQPTRGLD-VGAIEFIhQRLLELRDAG-AAVLLISEDlDEILALSDR 471
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-198 |
1.19e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.51 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 25 NFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQdITTMKQKALakvrmseigfiLQATNLvpfltvkQQF 104
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQAW-----------IQNDSL-------REN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 105 TLLKKKnknvMSNEDYQQLMSQLGLTSLLNKLPS-----------EISGGQKQRVAIAKALYTNPSIILADEPTAALDTE 173
Cdd:TIGR00957 719 ILFGKA----LNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180
....*....|....*....|....*.
gi 579537805 174 NAIEVI-KILRDQAKKRKKACIIVTH 198
Cdd:TIGR00957 795 VGKHIFeHVIGPEGVLKNKTRILVTH 820
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-199 |
1.25e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 30 KGDIIALVGPSGSGKSTFLT-MAGALqTPTSGhiliNNQDITTMK-----------QKALAKVRMSEIGFIL--QATNLV 95
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKiLSGEL-IPNLG----DYEEEPSWDevlkrfrgtelQNYFKKLYNGEIKVVHkpQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 96 PFL---TVKQqftLLKKKNKNVMSNEdyqqLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDT 172
Cdd:PRK13409 173 PKVfkgKVRE---LLKKVDERGKLDE----VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*..
gi 579537805 173 ENAIEVIKILRDQAKkrKKACIIVTHD 199
Cdd:PRK13409 246 RQRLNVARLIRELAE--GKYVLVVEHD 270
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-183 |
1.49e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 63.80 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTP--TSGHILINNQDITtmkqKALAK 79
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 vrmsEIGFILQATNLVPFLTVKQQftllkkknknvmsnedyqqlmsqLGLTSLLNklpsEISGGQKQRVAIAKALYTNPS 159
Cdd:cd03232 80 ----STGYVEQQDVHSPNLTVREA-----------------------LRFSALLR----GLSVEQRKRLTIGVELAAKPS 128
|
170 180
....*....|....*....|....
gi 579537805 160 IILADEPTAALDTENAIEVIKILR 183
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-197 |
1.66e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTkSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLT-MAGALQTPTSGHILINNQ--DITTMKQKAL 77
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKpvDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 78 AKVRMseIGFILQATNLVPFLTVKQQFTL--LKKKNKNVMSNEDYQQ-----LMSQLGLTSLLNKLP-SEISGGQKQRVA 149
Cdd:TIGR02633 336 AGIAM--VPEDRKRHGIVPILGVGKNITLsvLKSFCFKMRIDAAAELqiigsAIQRLKVKTASPFLPiGRLSGGNQQKAV 413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENAIEVIKILrDQAKKRKKACIIVT 197
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLI-NQLAQEGVAIIVVS 460
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
3-199 |
2.31e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 62.97 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 3 KFENVTKSFKDGNRNIEAVkdtnfEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHIlinnqdittmkqkALAKVRM 82
Cdd:cd03222 2 LYPDCVKRYGVFFLLVELG-----VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------EWDGITP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 SeigfilqatnlvpfltVKQQFTllkkknknvmsnedyqqlmsqlgltsllnklpsEISGGQKQRVAIAKALYTNPSIIL 162
Cdd:cd03222 64 V----------------YKPQYI---------------------------------DLSGGELQRVAIAAALLRNATFYL 94
|
170 180 190
....*....|....*....|....*....|....*..
gi 579537805 163 ADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:cd03222 95 FDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHD 131
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-216 |
2.52e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 19 EAVKDTNFEINKGDIIALVGPSGSGKST-FLTMAGALQtPTSGHILINNQDITTMKQKALAkVRmSEIGFILQATNLVPF 97
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTlFMNLSGLLR-PQKGAVLWQGKPLDYSKRGLLA-LR-QQVATVFQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 98 LTVKQQFTLLKKKNKNVMSNEDYQQLMSQLGLTSL--LNKLPSE-ISGGQKQRVAIAKALYTNPSIILADEPTAALDTEN 174
Cdd:PRK13638 92 YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAqhFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 579537805 175 AIEVIKILRDQAKKRKKAcIIVTHDerlkayCDRSYHMKDGV 216
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHV-IISSHD------IDLIYEISDAV 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-199 |
4.27e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.57 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 6 NVTKSFkDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGaLQTPTSGHILINnQDITtmkqkalakvrmse 84
Cdd:TIGR03719 9 RVSKVV-PPKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLLrIMAG-VDKDFNGEARPQ-PGIK-------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 85 IGFILQATNLVPFLTVKQQFTLLKKKNKNVMS------------NEDYQQLMSQLG-------------LTSLLN----- 134
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVEEGVAEIKDALDrfneisakyaepDADFDKLAAEQAelqeiidaadawdLDSQLEiamda 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579537805 135 -KLP------SEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENaievIKILRDQAKKRKKACIIVTHD 199
Cdd:TIGR03719 150 lRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-209 |
6.41e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 64.35 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 20 AVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQdittmkqkALAKVRMSEIGFILQATNLVPFL- 98
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI--------PLTKLQLDSWRSRLAVVSQTPFLf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 99 --TVKQQFTLLK-----------KKNKNVMSN-----EDYQQLMSQLGLTsllnklpseISGGQKQRVAIAKALYTNPSI 160
Cdd:PRK10789 402 sdTVANNIALGRpdatqqeiehvARLASVHDDilrlpQGYDTEVGERGVM---------LSGGQKQRISIARALLLNAEI 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 579537805 161 ILADEPTAALDTENAIEVIKILRDQAKKRkkACIIVTHdeRLKAYCDRS 209
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAH--RLSALTEAS 517
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-204 |
1.39e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.39 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTpTSGHILIN--NQDITTMKQKALAKVRM 82
Cdd:TIGR01271 1221 QGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDgvSWNSVTLQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 SEIGFILQAT---NLVPFltvkQQFtllkkknknvmSNEDYQQLMSQLGLTSLLNKLPSEI-----------SGGQKQRV 148
Cdd:TIGR01271 1298 PQKVFIFSGTfrkNLDPY----EQW-----------SDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLM 1362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 149 AIAKALYTNPSIILADEPTAALDTenaiEVIKILRDQAKKRKKACIIVTHDERLKA 204
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDP----VTLQIIRKTLKQSFSNCTVILSEHRVEA 1414
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-199 |
1.80e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFLTMA-GALQTpTSGHILINNQDITTMK-QKALAK--VRMSEIgfiLQATNLVP 96
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSpQDGLANgiVYISED---RKRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 97 FLTVKQQFTL--LKKKNKNVMSNEDYQQLMSQLGLTSLLN-KLPS------EISGGQKQRVAIAKALYTNPSIILADEPT 167
Cdd:PRK10762 344 GMSVKENMSLtaLRYFSRAGGSLKHADEQQAVSDFIRLFNiKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190
....*....|....*....|....*....|..
gi 579537805 168 AALDTeNAIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK10762 424 RGVDV-GAKKEIYQLINQFKAEGLSIILVSSE 454
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
22-213 |
2.14e-11 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 60.70 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 22 KDTNFEINKGdIIALVGPSGSGKSTFLTmagALQTPTSGHiLINNQDITTMKQKALAKVRMSeigfilqatnlvpfLTVK 101
Cdd:cd03240 14 ERSEIEFFSP-LTLIVGQNGAGKTTIIE---ALKYALTGE-LPPNSKGGAHDPKLIREGEVR--------------AQVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 102 QQFTLLKKKNKNV---MSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQ------RVAIAKALYTNPSIILADEPTAALDT 172
Cdd:cd03240 75 LAFENANGKKYTItrsLAILENVIFCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 579537805 173 EN-AIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMK 213
Cdd:cd03240 155 ENiEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-215 |
2.22e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQTPT-------SGHILINNQDITTMKQKALAKVR-----MSEIGF 87
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRavlpqAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 88 ILQATNLVpfltvkqqftLLKK----KNKNVMSNEDYQ---QLMSQLGLTSLLNKLPSEISGGQKQRVAIAKAL------ 154
Cdd:PRK13547 97 AFSAREIV----------LLGRyphaRRAGALTHRDGEiawQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 155 ---YTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKA-YCDRSYHMKDG 215
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADG 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-200 |
2.28e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDgNRNIEAVKDTNFEINKGDIIALVGPSGSGKS-TFLTMAGALQTPTSGHILINNQDITTMK-QKALA 78
Cdd:PRK13549 259 ILEVRNLTAWDPV-NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKIRNpQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KvrmseiGFIL-----QATNLVPFLTVKQQFTL--LKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPS------EISGGQK 145
Cdd:PRK13549 338 Q------GIAMvpedrKRDGIVPVMGVGKNITLaaLDRFTGGSRIDDAAELKTILESIQRLKVKTASpelaiaRLSGGNQ 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 146 QRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKkrKKACIIVTHDE 200
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ--QGVAIIVISSE 464
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-208 |
2.41e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 60.03 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 17 NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLtmagalqtptsghilinNQDITTMKQKALAKvrmseigfilqatnlvp 96
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----------------NEGLYASGKARLIS----------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 97 fltvkqqftLLKKKNKNVMSNEDYQQLMSQLGLTSL-LNKLPSEISGGQKQRVAIAKALYTNP--SIILADEPTAAL--- 170
Cdd:cd03238 53 ---------FLPKFSRNKLIFIDQLQFLIDVGLGYLtLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLhqq 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 579537805 171 DTENAIEVIKILRDQakkrKKACIIVTHDERLKAYCDR 208
Cdd:cd03238 124 DINQLLEVIKGLIDL----GNTVILIEHNLDVLSSADW 157
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-197 |
3.35e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 25 NFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIttmkqkalAKVR---MSEIGFILQATNLVPFLTVK 101
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--------RRQRdeyHQDLLYLGHQPGIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 102 QQFTLLKKKNKNVmSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKI 181
Cdd:PRK13538 93 ENLRFYQRLHGPG-DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
170
....*....|....*.
gi 579537805 182 LRDQAkkRKKACIIVT 197
Cdd:PRK13538 172 LAQHA--EQGGMVILT 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-171 |
6.28e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFKDgnrnIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHIL-----INNQDITTMKQkalak 79
Cdd:NF033858 270 RGLTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIATRRR----- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 80 vrmseIGFILQATNLVPFLTVKQQ-------FTLLKKKnknvmSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAK 152
Cdd:NF033858 341 -----VGYMSQAFSLYGELTVRQNlelharlFHLPAAE-----IAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170
....*....|....*....
gi 579537805 153 ALYTNPSIILADEPTAALD 171
Cdd:NF033858 411 AVIHKPELLILDEPTSGVD 429
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-215 |
7.51e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVTKSFKdgnrNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDI--TTMKQKALAKVRM 82
Cdd:PRK10982 2 SNISKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 83 seigfILQATNLVPFLTVKQQFTLLKKKNKNVMSNE-----DYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTN 157
Cdd:PRK10982 78 -----VHQELNLVLQRSVMDNMWLGRYPTKGMFVDQdkmyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 158 PSIILADEPTAALDTENAIEVIKILRdqaKKRKKACIIV--THD-ERLKAYCDRSYHMKDG 215
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIR---KLKERGCGIVyiSHKmEEIFQLCDEITILRDG 210
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-213 |
1.29e-10 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 57.75 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 27 EINKGDIIALVGPSGSGKSTFLTMAGAlqtptsghilinnqdITTMKQKALAKVRMSEIGFILQATNLVPFLTVKQqftl 106
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIGL---------------ALGGAQSATRRRSGVKAGCIVAAVSAELIFTRLQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 107 lkkknknvmsnedyqqlmsqlgltsllnklpseISGGQKQRVAIAKAL----YTNPSIILADEPTAALDTENAIEVIKIL 182
Cdd:cd03227 78 ---------------------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAI 124
|
170 180 190
....*....|....*....|....*....|.
gi 579537805 183 RDQAKKRKKAcIIVTHDERLKAYCDRSYHMK 213
Cdd:cd03227 125 LEHLVKGAQV-IVITHLPELAELADKLIHIK 154
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-225 |
4.14e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 23 DTNFEINKGDIIALVGPSGSGKSTFLT-MAGALQTPTSGHILInnqdittmkQKALAKVrmSEIGFILQATnlvpfltVK 101
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI---------RGSVAYV--PQVSWIFNAT-------VR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 102 QQFTLLKKknknvMSNEDYQQLMSQLGLTSLLNKLPSE-----------ISGGQKQRVAIAKALYTNPSIILADEPTAAL 170
Cdd:PLN03232 697 ENILFGSD-----FESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 171 DTENAIEVI-KILRDQAKKRKKacIIVTHDERLKAYCDRSYHMKDGVLNLENETVE 225
Cdd:PLN03232 772 DAHVAHQVFdSCMKDELKGKTR--VLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE 825
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-173 |
5.18e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 16 RNIEAV-KDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKqkalakvRMSEIGFILQATNL 94
Cdd:PRK13543 21 RNEEPVfGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 95 VPFLTVKQQFTLLkkknkNVMSNEDYQQL----MSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAAL 170
Cdd:PRK13543 94 KADLSTLENLHFL-----CGLHGRRAKQMpgsaLAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
...
gi 579537805 171 DTE 173
Cdd:PRK13543 169 DLE 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-217 |
5.63e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.87 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRniEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTmkqkALAKV 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSeIGFILQATNLVPFLTVKQQFTLLKKKNKnvMSNEDYQQL----MSQLGLTSLLNKLPSEISGGQKQRVAIAKALYT 156
Cdd:TIGR01257 2011 HQN-MGYCPQFDAIDDLLTGREHLYLYARLRG--VPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 157 NPSIILADEPTAALDTE------NAIevIKILRDQakkrkKACIIVTHD-ERLKAYCDRSYHMKDGVL 217
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQarrmlwNTI--VSIIREG-----RAVVLTSHSmEECEALCTRLAIMVKGAF 2148
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-198 |
5.73e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 17 NIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILI------------------NNQDITTMKQKALA 78
Cdd:PTZ00265 1180 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfknehtndmtneqdyqgdEEQNVGMKNVNEFS 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 KVRMSEIG-----------FILQATNLVP---------FLTVKQQFTLLK-------KKNKNVMSNEDYQQLMSQLGLTS 131
Cdd:PTZ00265 1260 LTKEGGSGedstvfknsgkILLDGVDICDynlkdlrnlFSIVSQEPMLFNmsiyeniKFGKEDATREDVKRACKFAAIDE 1339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 132 LLNKLPSE-----------ISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTH 198
Cdd:PTZ00265 1340 FIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-177 |
1.26e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFkdGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNqditTMKqkalakvr 81
Cdd:PRK11819 325 IEAENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE----TVK-------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 82 mseIGFILQA-TNLVPFLTVKQQFT----LLKKKNKNVMS----------NEDYQQLMSQLgltsllnklpseiSGGQKQ 146
Cdd:PRK11819 389 ---LAYVDQSrDALDPNKTVWEEISggldIIKVGNREIPSrayvgrfnfkGGDQQKKVGVL-------------SGGERN 452
|
170 180 190
....*....|....*....|....*....|....*..
gi 579537805 147 RVAIAKALYTNPSIILADEPTAALDT------ENAIE 177
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVetlralEEALL 489
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-208 |
1.28e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.53 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 126 QLGLTSL-LNKLPSEISGGQKQRVAIAKALYTNPSII--LADEPTAAL---DTENAIEVIKILRDQAkkrkKACIIVTHD 199
Cdd:PRK00635 462 DLGLPYLtPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLhpqDTHKLINVIKKLRDQG----NTVLLVEHD 537
|
....*....
gi 579537805 200 ERLKAYCDR 208
Cdd:PRK00635 538 EQMISLADR 546
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-205 |
1.91e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGnrniEAVKDTNFEINKGDIIALVGPSGSGKSTF-LTMAGALQ-TPTSGHILINNQDITTMKQKAla 78
Cdd:PRK09580 1 MLSIKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREDyEVTGGTVEFKGKDLLELSPED-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 79 kvRMSEiGFILQATNLVPFLTVKQQFTL-------LKKKNKNVMSNEDYQQLMSQlglTSLLNKLPSEI---------SG 142
Cdd:PRK09580 75 --RAGE-GIFMAFQYPVEIPGVSNQFFLqtalnavRSYRGQEPLDRFDFQDLMEE---KIALLKMPEDLltrsvnvgfSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 143 GQKQRVAIAKALYTNPSIILADEPTAALDtenaIEVIKI-------LRDQakkrKKACIIVTHDERLKAY 205
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLD----IDALKIvadgvnsLRDG----KRSFIIVTHYQRILDY 210
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-208 |
2.05e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.35 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTfltMAGALQTPTSGHILI-------NNQDITTMK 73
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSL---IAKAICGVTKDNWRVtadrmrfDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 74 QKALAKVRMSEIGFILQ--------ATNL-------VPFLTVK----QQFTLLKKKNKNVMSN---EDYQQLMSQLglts 131
Cdd:PRK15093 80 PRERRKLVGHNVSMIFQepqscldpSERVgrqlmqnIPGWTYKgrwwQRFGWRKRRAIELLHRvgiKDHKDAMRSF---- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 132 llnklPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHD-ERLKAYCDR 208
Cdd:PRK15093 156 -----PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADK 228
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-201 |
2.11e-09 |
|
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: 54.30 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 30 KGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQdittmkqkalakvrmseigfilqatnlvpfltvkqqftllkk 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 110 knknvmsnEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKR 189
Cdd:smart00382 39 --------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
170
....*....|....*..
gi 579537805 190 KKA-----CIIVTHDER 201
Cdd:smart00382 111 LKSeknltVILTTNDEK 127
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-217 |
2.58e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 56.34 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 25 NFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITtmkqkalakvrmseigfilqATNLvpfltvkqqf 104
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT--------------------ADNR---------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 105 tllkkknknvmsnEDYQQLMSQ-----------LGLTS---------LLNKLpsEI----------------SGGQKQRV 148
Cdd:COG4615 402 -------------EAYRQLFSAvfsdfhlfdrlLGLDGeadparareLLERL--ELdhkvsvedgrfsttdlSQGQRKRL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 149 AIAKALYTNPSIILADEPTAaldtenaievikilrDQ---------------AKKRKKACIIVTHDERlkaY---CDRSY 210
Cdd:COG4615 467 ALLVALLEDRPILVFDEWAA---------------DQdpefrrvfytellpeLKARGKTVIAISHDDR---YfdlADRVL 528
|
....*..
gi 579537805 211 HMKDGVL 217
Cdd:COG4615 529 KMDYGKL 535
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-184 |
2.69e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 31 GDIIALVGPSGSGKSTFL-TMAGalqTPTSGHIlinNQDIT----TMKQKALAKVRmseiGFILQATNLVPFLTVKQQ-- 103
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMdVLAG---RKTGGYI---EGDIRisgfPKKQETFARIS----GYCEQNDIHSPQVTVRESli 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 104 FTLLKKKNKNVMSNEDY---QQLMSQLGLTSLLNK---LP--SEISGGQKQRVAIAKALYTNPSIILADEPTAALDTENA 175
Cdd:PLN03140 976 YSAFLRLPKEVSKEEKMmfvDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
....*....
gi 579537805 176 IEVIKILRD 184
Cdd:PLN03140 1056 AIVMRTVRN 1064
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-215 |
2.76e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTksfkdgNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTmkQKALAKV 80
Cdd:PRK10982 250 ILEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINN--HNANEAI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMseiGFIL-----QATNLVPFLTV------------KQQFTLLKkkNKNVMSNedyqqlmSQLGLTSLLNKLPSE---- 139
Cdd:PRK10982 322 NH---GFALvteerRSTGIYAYLDIgfnslisnirnyKNKVGLLD--NSRMKSD-------TQWVIDSMRVKTPGHrtqi 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 140 --ISGGQKQRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMKDG 215
Cdd:PRK10982 390 gsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-187 |
2.99e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 31 GDIIALVGPSGSGKSTFL-TMAGALQTP--TSGHILINNQDITTMKQKAlakvrmseIGFILQATNLVPFLTVKQ--QFT 105
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLnVLAERVTTGviTGGDRLVNGRPLDSSFQRS--------IGYVQQQDLHLPTSTVREslRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 106 LLKKKNKNVMSNE--DY-QQLMSQLGLTSLLNKLPSEISGG----QKQRVAIAKALYTNP-SIILADEPTAALDTENAIE 177
Cdd:TIGR00956 861 AYLRQPKSVSKSEkmEYvEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWS 940
|
170
....*....|
gi 579537805 178 VIKILRDQAK 187
Cdd:TIGR00956 941 ICKLMRKLAD 950
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-199 |
3.80e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 5 ENVtkSFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLT-MAGALQtPTSGHIlinnqdittmkqKALAKVrms 83
Cdd:PRK11147 323 ENV--NYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRI------------HCGTKL--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 84 EIGFILQ-ATNLVPFLTV-------KQQFTLLKKKnKNVMSnedYQQ--LMSQLGLTSLLNKLpseiSGGQKQRVAIAKa 153
Cdd:PRK11147 383 EVAYFDQhRAELDPEKTVmdnlaegKQEVMVNGRP-RHVLG---YLQdfLFHPKRAMTPVKAL----SGGERNRLLLAR- 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 579537805 154 LYTNPS--IILaDEPTAALDtenaIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK11147 454 LFLKPSnlLIL-DEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-199 |
4.36e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 34 IALVGPSGSGKSTFL-TMAGaLQTPTSGhilinnqdittmkqkalaKVRMSE---IGFILQATNLVPFLTVKQ------- 102
Cdd:PRK11819 36 IGVLGLNGAGKSTLLrIMAG-VDKEFEG------------------EARPAPgikVGYLPQEPQLDPEKTVREnveegva 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 103 -QFTLLKKKNK--NVMSNE--DYQQLMSQLG-------------LTSLLN------KLP------SEISGGQKQRVAIAK 152
Cdd:PRK11819 97 eVKAALDRFNEiyAAYAEPdaDFDALAAEQGelqeiidaadawdLDSQLEiamdalRCPpwdakvTKLSGGERRRVALCR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 579537805 153 ALYTNPSIILADEPTAALDTENAIEVIKILRDQakkrKKACIIVTHD 199
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY----PGTVVAVTHD 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-176 |
5.89e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.69 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPT------SGHILINNQDI----TTMKQKALAKVRMSEIGFilq 90
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSegkikhSGRISFSPQTSwimpGTIKDNIIFGLSYDEYRY--- 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 91 aTNLVPFLTVKQQFTLLKKKNKNVMSNEdyqqlmsqlGLTsllnklpseISGGQKQRVAIAKALYTNPSIILADEPTAAL 170
Cdd:TIGR01271 519 -TSVIKACQLEEDIALFPEKDKTVLGEG---------GIT---------LSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
....*...
gi 579537805 171 D--TENAI 176
Cdd:TIGR01271 580 DvvTEKEI 587
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-215 |
7.33e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.48 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 6 NVTKSFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTpTSGHILIN--NQDITTMKQKALAKVRMS 83
Cdd:cd03289 7 DLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDgvSWNSVPLQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 84 EIGFILQAT---NLVPFltvkqqftllkkknkNVMSNEDYQQLMSQLGLTSLLNKLPSEI-----------SGGQKQRVA 149
Cdd:cd03289 84 QKVFIFSGTfrkNLDPY---------------GKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMC 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579537805 150 IAKALYTNPSIILADEPTAALDTENaievIKILRDQAKKRKKACIIVTHDERLKAY--CDRSYHMKDG 215
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPIT----YQVIRKTLKQAFADCTVILSEHRIEAMleCQRFLVIEEN 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-199 |
8.03e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 8.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGnrniEAVKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQtPTSGhilinnqdittmkqkalaKV 80
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLrTLVGELE-PDSG------------------TV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSE---IGFILQATNlvpfltvkQQF----TLLKKKNKNVMSNEDYQQLMSQLGltSLL------NKLPSEISGGQKQR 147
Cdd:PRK15064 377 KWSEnanIGYYAQDHA--------YDFendlTLFDWMSQWRQEGDDEQAVRGTLG--RLLfsqddiKKSVKVLSGGEKGR 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 579537805 148 VAIAKALYTNPSIILADEPTAALDTEnAIEVikiLRDQAKKRKKACIIVTHD 199
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDME-SIES---LNMALEKYEGTLIFVSHD 494
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
121-199 |
2.13e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 2.13e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 121 QQLMSQLGLTSllNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDtenaIEVIKILRDQAKKRKKACIIVTHD 199
Cdd:PRK11147 140 NEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHD 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-176 |
2.39e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.94 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQdIT-----------TMKQKALAKVRMSEIGF-- 87
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISfssqfswimpgTIKENIIFGVSYDEYRYks 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 88 ILQATNLvpfltvKQQFTLLKKKNKNVMSnedyqqlmsQLGLTsllnklpseISGGQKQRVAIAKALYTNPSIILADEPT 167
Cdd:cd03291 132 VVKACQL------EEDITKFPEKDNTVLG---------EGGIT---------LSGGQRARISLARAVYKDADLYLLDSPF 187
|
170
....*....|.
gi 579537805 168 AALD--TENAI 176
Cdd:cd03291 188 GYLDvfTEKEI 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-208 |
2.65e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 26 FEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTMKQKALAKVrmseIGFILQAT---------NLVP 96
Cdd:PLN03130 1260 FEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV----LGIIPQAPvlfsgtvrfNLDP 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 97 FLTVKQQ---FTLLKKKNKNVMSNedyqqlmSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDTE 173
Cdd:PLN03130 1336 FNEHNDAdlwESLERAHLKDVIRR-------NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
170 180 190
....*....|....*....|....*....|....*....
gi 579537805 174 NAIEVIKILRDQAkkrkKAC--IIVTHdeRLKAY--CDR 208
Cdd:PLN03130 1409 TDALIQKTIREEF----KSCtmLIIAH--RLNTIidCDR 1441
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-200 |
3.52e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.26 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 22 KDTNFEINKGDIIALVGPSGSGKST--FLTMAGALQTPTsghilinNQDITTMKQKALAKVRMSEIGFIlqaTNLVPFLT 99
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSlaFDTIYAEGQRRY-------VESLSAYARQFLGQMDKPDVDSI---EGLSPAIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 100 VKQQFTllkkkNKNVMSN-------EDYQQL-------------MSQLGLTSL-LNKLPSEISGGQKQRVAIAKALYTNP 158
Cdd:cd03270 82 IDQKTT-----SRNPRSTvgtvteiYDYLRLlfarvgirerlgfLVDVGLGYLtLSRSAPTLSGGEAQRIRLATQIGSGL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 579537805 159 SIIL--ADEPTAAL---DTENAIEVIKILRDQAkkrkKACIIVTHDE 200
Cdd:cd03270 157 TGVLyvLDEPSIGLhprDNDRLIETLKRLRDLG----NTVLVVEHDE 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-171 |
9.55e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFL-TMAGALQTpTSGHILINnQDITTMKQKAlakvrmseigFILQAT---NLVP 96
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQFEI-SEGRVWAE-RSIAYVPQQA----------WIMNATvrgNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 97 FltvkqqftllkkknknvmSNEDYQQL-----MSQL--GLTSLLNKLPSEI-------SGGQKQRVAIAKALYTNPSIIL 162
Cdd:PTZ00243 744 F------------------DEEDAARLadavrVSQLeaDLAQLGGGLETEIgekgvnlSGGQKARVSLARAVYANRDVYL 805
|
....*....
gi 579537805 163 ADEPTAALD 171
Cdd:PTZ00243 806 LDDPLSALD 814
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-198 |
9.95e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 7 VTKSFKDGNRNIEAVKDTNFEINKG--DII-------------ALVGPSGSGKSTFL---TMAGALQTPTSGHILINNQD 68
Cdd:PLN03073 164 VNHDGNGGGPAIKDIHMENFSISVGgrDLIvdasvtlafgrhyGLVGRNGTGKTTFLrymAMHAIDGIPKNCQILHVEQE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 69 ITTMKQKALAKVRMSEI---------GFILQATNLVPFLTVKQQFTLLKKK--NKNVMSN---EDYQQL----------- 123
Cdd:PLN03073 244 VVGDDTTALQCVLNTDIertqlleeeAQLVAQQRELEFETETGKGKGANKDgvDKDAVSQrleEIYKRLelidaytaear 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 124 ----MSQLGLTS-LLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALDtenaIEVIKILRDQAKKRKKACIIVTH 198
Cdd:PLN03073 324 aasiLAGLSFTPeMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD----LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-215 |
1.06e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.67 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIEavkDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQtPTSGHILinnqdittmkqkalAKV 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIE---SLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRL--------------TKP 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILQAtnlvPFLTV---KQQF----TLLKKKNKNvMSNEDYQQLMSQLGLTSLLNKLPS---------EISGGQ 144
Cdd:TIGR00954 513 AKGKLFYVPQR----PYMTLgtlRDQIiypdSSEDMKRRG-LSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGE 587
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579537805 145 KQRVAIAKALYTNPSIILADEPTAALdtenAIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRSYHMkDG 215
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYM-DG 653
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-174 |
5.46e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVtkSFKDGNRNIeavKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDITTmkqkaLAKV 80
Cdd:PRK13541 1 MLSLHQL--QFNIEQKNL---FDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-----IAKP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 81 RMSEIGFILqatNLVPFLTVkqqFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSI 160
Cdd:PRK13541 71 YCTYIGHNL---GLKLEMTV---FENLKFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170
....*....|....
gi 579537805 161 ILADEPTAALDTEN 174
Cdd:PRK13541 145 WLLDEVETNLSKEN 158
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-207 |
7.71e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.17 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIttmkqkalAKVRMSEIGFILQATNLVPFLtv 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI--------AKIGLHDLRFKITIIPQDPVL-- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 101 kqqFTLLKKKNKNVMSNEDYQQLMSQLGLTSL---LNKLPSE-----------ISGGQKQRVAIAKALYTNPSIILADEP 166
Cdd:TIGR00957 1372 ---FSGSLRMNLDPFSQYSDEEVWWALELAHLktfVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 579537805 167 TAALDTENAIEVIKILRDQAKKrkkaCIIVTHDERLKAYCD 207
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFED----CTVLTIAHRLNTIMD 1485
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-225 |
1.18e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFKDGNRNIeaVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILINNQDIT----TMKQKA 76
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfglTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 77 LAKVRMSEIGFilQAT---NLVPFLTVKQQ---FTLLKKKNKNVMSNedyqqlmSQLGLTSLLNKLPSEISGGQKQRVAI 150
Cdd:PLN03232 1312 LSIIPQSPVLF--SGTvrfNIDPFSEHNDAdlwEALERAHIKDVIDR-------NPFGLDAEVSEGGENFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 151 AKALYTNPSIILADEPTAALDTENAIEVIKILRDQAkkrkKACIIVTHDERLKAY--CDRSYHMKDGVLnLENETVE 225
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIREEF----KSCTMLVIAHRLNTIidCDKILVLSSGQV-LEYDSPQ 1454
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-215 |
1.87e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKsTFLTMA---GALQTPTSGHILINNQDITTMK-QKA----LAKVrmSE----IGFI 88
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGR-TELAMSvfgRSYGRNISGTVFKDGKEVDVSTvSDAidagLAYV--TEdrkgYGLN 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 89 LQATnlvpfltVKQQFTL--LKK--------KNKNVMSNEDYQqlmsqlglTSLLNKLPS------EISGGQKQRVAIAK 152
Cdd:NF040905 353 LIDD-------IKRNITLanLGKvsrrgvidENEEIKVAEEYR--------KKMNIKTPSvfqkvgNLSGGNQQKVVLSK 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 153 ALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRKkaCIIVTHDE--RLKAYCDRSYHMKDG 215
Cdd:NF040905 418 WLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGK--GVIVISSElpELLGMCDRIYVMNEG 480
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-209 |
1.91e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVTKSFKDGNRNIEAVKD----------------TNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHILIn 65
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKDlffrskdgeyhyalnnISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 66 nqdittmkqKALAKVRMSEIGFILQATNLVPFLTVKQQFTLLKKKNKNVMSnedyqQLMSQLGLTSLLNKLPSEISGGQK 145
Cdd:PRK13545 84 ---------KGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIP-----EIIEFADIGKFIYQPVKTYSSGMK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 146 QRVAIAKALYTNPSIILADEPTAALDTENAIEVIKILrDQAKKRKKACIIVTHD-ERLKAYCDRS 209
Cdd:PRK13545 150 SRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM-NEFKEQGKTIFFISHSlSQVKSFCTKA 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-188 |
2.63e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 25 NFEINKGDIIALVGPSGSGKSTF-LTMAGALqTPTSGHILINNQDITTMKQKALAKVrmseigfilqatnlvpfltVKQQ 103
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALaRALAGEL-PLLSGERQSQFSHITRLSFEQLQKL-------------------VSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 104 FtllKKKNKNVMS--------------------NEDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILA 163
Cdd:PRK10938 83 W---QRNNTDMLSpgeddtgrttaeiiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180
....*....|....*....|....*
gi 579537805 164 DEPTAALDTENAIEVIKILRDQAKK 188
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQS 184
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-62 |
9.14e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 9.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579537805 2 LKFENVTKSF----------------KDGNRNIEAVKDTNFEINKGDIIALVGPSGSGKSTFLTMAGALQTPTSGHI 62
Cdd:PRK13546 5 VNIKNVTKEYriyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
9-210 |
1.51e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.99 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 9 KSFkdgnrnieaVKDTNFEINKGdIIALVGPSGSGKSTFL------------------TM-----AGALQTPTSGH---- 61
Cdd:cd03278 10 KSF---------ADKTTIPFPPG-LTAIVGPNGSGKSNIIdairwvlgeqsakslrgeKMsdvifAGSETRKPANFaevt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 62 ILINNQDittmkqKALAKVRMSEIGFILQATNlvpfltvkqqftllkKKNKNVmsnedyqqlmsqlgltSLLnklpseiS 141
Cdd:cd03278 80 LTFDNSD------GRYSIISQGDVSEIIEAPG---------------KKVQRL----------------SLL-------S 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 142 GGQKQRVAIAK--ALY-TNPS-IILADEPTAALDTENAIEVIKILRDQAKKRKkaCIIVTHDERLKAYCDRSY 210
Cdd:cd03278 116 GGEKALTALALlfAIFrVRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQ--FIVITHRKGTMEAADRLY 186
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-215 |
2.47e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 1 MLKFENVTKSFkdGNRNI-EAVKdtnFEINKGDIIALVGPSGSGKSTFLTM-AGALQtPTSGHI-LINNQDITTMKQKAL 77
Cdd:PRK10636 312 LLKMEKVSAGY--GDRIIlDSIK---LNLVPGSRIGLLGRNGAGKSTLIKLlAGELA-PVSGEIgLAKGIKLGYFAQHQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 78 AKVRMSEigfilqatnlvpflTVKQQFTLLKKKnknvmsnEDYQQLMSQLGLTSLLNKLPSEI----SGGQKQRVAIAKA 153
Cdd:PRK10636 386 EFLRADE--------------SPLQHLARLAPQ-------ELEQKLRDYLGGFGFQGDKVTEEtrrfSGGEKARLVLALI 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579537805 154 LYTNPSIILADEPTAALDtenaIEVIKILRDQAKKRKKACIIVTHDERL-KAYCDRSYHMKDG 215
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDRHLlRSTTDDLYLVHDG 503
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
141-209 |
3.30e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 3.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579537805 141 SGGQKQ------RVAIAKALYTNPSIILADEPTAALDTEN----AIEVIKILRDQAKKRKKACIIVTHDERLKAYCDRS 209
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRS 1279
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
107-186 |
6.50e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 107 LKKKNKNVMSNEdyqqLMSQLGLTSLLNKLPSEISGGQKQRVAIAKALYTNPSIILADEPTAALD--TENAI--EVIKIL 182
Cdd:NF000106 116 LSRKDARARADE----LLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDprTRNEVwdEVRSMV 191
|
....
gi 579537805 183 RDQA 186
Cdd:NF000106 192 RDGA 195
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
21-185 |
1.45e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 21 VKDTNFEINKGDIIALVGPSGSGKSTFL--TMAGALQTPT--SGHILINNQDITTMKqkALAKVRM---SEIGFILQ--- 90
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndTLYPALARRLhlKKEQPGNHDRIEGLE--HIDKVIVidqSPIGRTPRsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 91 ATNLVPFLTVKQQF------------TL-LKKKNKNV-----MSNED-------------YQQLMSQLGLTSL-LNKLPS 138
Cdd:cd03271 89 ATYTGVFDEIRELFcevckgkrynreTLeVRYKGKSIadvldMTVEEaleffenipkiarKLQTLCDVGLGYIkLGQPAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 579537805 139 EISGGQKQRVAIAKALY---TNPSIILADEPTAAL---DTENAIEVIKILRDQ 185
Cdd:cd03271 169 TLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLhfhDVKKLLEVLQRLVDK 221
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
127-200 |
2.30e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 127 LGLTSL-LNKLPSEISGGQKQRVAIAK--------ALYtnpsiILaDEPTAAL---DTENAIEVIKILRDQAkkrkKACI 194
Cdd:TIGR00630 475 VGLDYLsLSRAAGTLSGGEAQRIRLATqigsgltgVLY-----VL-DEPSIGLhqrDNRRLINTLKRLRDLG----NTLI 544
|
....*.
gi 579537805 195 IVTHDE 200
Cdd:TIGR00630 545 VVEHDE 550
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-218 |
2.42e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 28 INKGDIIALVGPSGSGKSTFLTM--------AGALQTPTSGHILINNQDITTMKQKALAKV-----RMSEIGFILQATN- 93
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALlkneisadGGSYTFPGNWQLAWVNQETPALPQPALEYVidgdrEYRQLEAQLHDANe 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 94 ---------LVPFLTVKQQFTLLKKKnknvmsnedyQQLMSQLGLTS-LLNKLPSEISGGQKQRVAIAKALYTNPSIILA 163
Cdd:PRK10636 104 rndghaiatIHGKLDAIDAWTIRSRA----------ASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579537805 164 DEPTAALDTENAIEVIKILrdqaKKRKKACIIVTHD-ERLKAYCDRSYHMKDGVLN 218
Cdd:PRK10636 174 DEPTNHLDLDAVIWLEKWL----KSYQGTLILISHDrDFLDPIVDKIIHIEQQSLF 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
121-174 |
1.07e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 121 QQLMSQLGLTSLLNKLP-SEISGGQKQRVAIAKALYTNPSIILADEPTAALDTEN 174
Cdd:PRK10938 382 QQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN 436
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-199 |
1.13e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 2 LKFENVtKSFKDGnrnieavkdTNFEINKGdIIALVGPSGSGKSTFL---TMA--GALQTPTSGHILINNQDITTM---- 72
Cdd:COG0419 5 LRLENF-RSYRDT---------ETIDFDDG-LNLIVGPNGAGKSTILeaiRYAlyGKARSRSKLRSDLINVGSEEAsvel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 73 ----------------KQKALAKVRMSEIGFILQA-TNLVPFLTVKQQFTLLKKKNKNVMSNEDYQQLMSQLGLTSLLNK 135
Cdd:COG0419 74 efehggkryrierrqgEFAEFLEAKPSERKEALKRlLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579537805 136 LPSE-ISGGQKQRVAIAKALytnpSIILaDepTAALDTENAIEVIKILRDQAkkrkkaciIVTHD 199
Cdd:COG0419 154 DPIEtLSGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
28-225 |
1.36e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 38.74 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 28 INKGDIIALVGPSGSGKSTFLT--MAGALQTPTSGHILINNQDITTMKQkalakvRMSEIGFILQAtnlvpfltvkqqft 105
Cdd:COG0467 17 LPRGSSTLLSGPPGTGKTTLALqfLAEGLRRGEKGLYVSFEESPEQLLR------RAESLGLDLEE-------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 106 LLKKKNKNVMsneDYQQLMSQLGLTSLLNKLPSEISGGQKQRVAI--AKALYtnpsiiladepTAALDTENAIEVIKILR 183
Cdd:COG0467 77 YIESGLLRII---DLSPEELGLDLEELLARLREAVEEFGAKRVVIdsLSGLL-----------LALPDPERLREFLHRLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 579537805 184 DQAKKRKKACIIVTHDERLKAycDRSY----HMKDGVLNLENETVE 225
Cdd:COG0467 143 RYLKKRGVTTLLTSETGGLED--EATEgglsYLADGVILLRYVELG 186
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
30-48 |
6.92e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 35.96 E-value: 6.92e-03
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
117-213 |
6.95e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 37.19 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 117 NEDYQQLMSQLGLTSLLNKLpseiSGGQKQ------RVAIAKALYTNPSIILADEPTAALDTENAIEVIKILRDQAKKRK 190
Cdd:PRK01156 783 DQDFNITVSRGGMVEGIDSL----SGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSS 858
|
90 100
....*....|....*....|....*
gi 579537805 191 --KACIIVTHDERLKAYCDRSYHMK 213
Cdd:PRK01156 859 diPQVIMISHHRELLSVADVAYEVK 883
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
105-185 |
7.11e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.30 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579537805 105 TL-LKKKNKNV-----MSNED-------------YQQLMSQLGLTSL-LNKLPSEISGGQKQRVAIAKALY---TNPSII 161
Cdd:TIGR00630 775 TLeVKYKGKNIadvldMTVEEayeffeavpsisrKLQTLCDVGLGYIrLGQPATTLSGGEAQRIKLAKELSkrsTGRTLY 854
|
90 100
....*....|....*....|....*..
gi 579537805 162 LADEPTAAL---DTENAIEVIKILRDQ 185
Cdd:TIGR00630 855 ILDEPTTGLhfdDIKKLLEVLQRLVDK 881
|
|
| |
