|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-226 |
2.45e-121 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 343.56 E-value: 2.45e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MK-LIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPEL 79
Cdd:COG1136 1 MSpLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIRNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFV 159
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKIESDIR 226
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-221 |
1.11e-108 |
|
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: 311.35 E-value: 1.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-226 |
5.50e-90 |
|
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: 264.30 E-value: 5.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAwdSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKIESDIR 226
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-224 |
1.89e-76 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 229.55 E-value: 1.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIR 83
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:COG2884 79 -RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRkTGRTIILITHEESL-AKYARRLIRMKDGKIESD 224
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELvDRMPKRVLELEDGRLVRD 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-203 |
7.87e-71 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 219.56 E-value: 7.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIR 83
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:COG1135 82 -RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE 203
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE 200
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-222 |
1.46e-69 |
|
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: 212.83 E-value: 1.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKIE 222
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEVV 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-225 |
1.78e-69 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 212.37 E-value: 1.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKIESDI 225
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-221 |
2.33e-69 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 212.61 E-value: 2.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELAR 81
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRNEkIGFVFQAFNLLARSSVYENV---RLP----------LFYSNVPETAWDskiksAIDAVGISHRIVHEPGELSGGE 148
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLSVLTNVlagRLGrtstwrsllgLFPPEDRERALE-----ALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 149 KQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLArRYADRIIGLRDGRV 225
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-220 |
2.89e-67 |
|
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: 206.33 E-value: 2.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLA-KYARRLIRMKDGK 220
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVdRVAHRVIILDDGR 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-216 |
6.17e-66 |
|
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: 202.46 E-value: 6.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 6 VKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIRNE 85
Cdd:TIGR03608 1 LKNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 86 KIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMI 165
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 818736213 166 LADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLAKYARRLIRM 216
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-224 |
1.84e-64 |
|
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: 199.48 E-value: 1.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARir 83
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 neKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:COG1122 76 --KVGLVFQnPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHE-ESLAKYARRLIRMKDGKIESD 224
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDlDLVAELADRVIVLDDGRIVAD 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-227 |
2.92e-64 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 199.93 E-value: 2.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEysepela 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 riRNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:COG1116 78 --PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLAkYARRLIRMKD--GKIESDIRI 227
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHdvDEAVF-LADRVVVLSArpGRIVEEIDV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
1.04e-62 |
|
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: 203.60 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTV-ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELAR 81
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRnEKIGFVFQ----AFNllARSSVYENVRLPL-FYSNVPETAWDSKIKSAIDAVGISHRIVHE-PGELSGGEKQRVAIA 155
Cdd:COG1123 340 LR-RRVQMVFQdpysSLN--PRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 156 RSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKY-ARRLIRMKDGKI 221
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-221 |
4.62e-62 |
|
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: 193.94 E-value: 4.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIR 83
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENV---RLP----------LFYSNVPETAwdskiKSAIDAVGISHRIVHEPGELSGGEKQ 150
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVlsgRLGrrstwrslfgLFPKEEKQRA-----LAALERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 151 RVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAK-YARRLIRMKDGKI 221
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAReYADRIVGLKDGRI 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-224 |
2.51e-61 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 202.65 E-value: 2.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYARRLIRMKDGKIESD 224
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-221 |
2.62e-60 |
|
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: 188.87 E-value: 2.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEpELARI 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR-RLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKIGFVFQ----AFNllARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGI--SHRIVHE-PGELSGGEKQRVAIA 155
Cdd:cd03257 80 RRKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglPEEVLNRyPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 156 RSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKY-ARRLIRMKDGKI 221
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-227 |
3.38e-60 |
|
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: 188.45 E-value: 3.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEysepelariR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLAkYARRLIRM--KDGKIESDIRI 227
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHdiDEAVF-LADRVVVLsaRPGRIVAEVEV 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-221 |
1.56e-59 |
|
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: 186.46 E-value: 1.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIR 83
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03292 78 -RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNrKTGRTIILITHEESL-AKYARRLIRMKDGKI 221
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-221 |
3.61e-59 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 186.34 E-value: 3.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqsgESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:COG1127 5 MIEVRNLTKSF---GDRVV-LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQA---FNLLarsSVYENVRLPLF-YSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSF 158
Cdd:COG1127 81 R-RRIGMLFQGgalFDSL---TVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 159 VLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-221 |
1.42e-58 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 184.60 E-value: 1.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELAR 81
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLD 161
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 162 PEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-220 |
2.50e-58 |
|
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: 183.44 E-value: 2.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 5 EVKNLEKVYQSGESKtvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirn 84
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 85 eKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03225 76 -KVGLVFQnPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHE-ESLAKYARRLIRMKDGK 220
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-221 |
4.90e-58 |
|
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: 183.65 E-value: 4.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNLLARSSVYENVRLP-LFYSNVPETAW------DSKI-KSAIDAVGISHRIVHEPGELSGGEKQRVAI 154
Cdd:TIGR02315 78 R-RRIGMIFQHYNLIERLTVLENVLHGrLGYKPTWRSLLgrfseeDKERaLSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 155 ARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAK-YARRLIRMKDGKI 221
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKkYADRIVGLKAGEI 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-222 |
1.57e-57 |
|
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: 181.93 E-value: 1.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIR 83
Cdd:cd03261 1 IELRGLTKSF---GGRTV-LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NeKIGFVFQAFNLLARSSVYENVRLPLF-YSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:cd03261 77 R-RMGMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKIE 222
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-221 |
2.34e-57 |
|
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: 180.80 E-value: 2.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEySEPELARIR 83
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRLPLFY-SNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 163 EMILADEPTGNLDSkngEMIIKLLDELNR--KTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:cd03262 155 KVMLFDEPTSALDP---ELVGEVLDVMKDlaEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-221 |
1.12e-56 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 179.80 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEySEPELARI 82
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNLLARSSVYENVRLPLFYS-NVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLD 161
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 162 PEMILADEPTGNLDSkngEMIIKLLD---ELnRKTGRTIILITHEESLAKY-ARRLIRMKDGKI 221
Cdd:COG1126 155 PKVMLFDEPTSALDP---ELVGEVLDvmrDL-AKEGMTMVVVTHEMGFAREvADRVVFMDGGRI 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-222 |
2.52e-56 |
|
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: 178.10 E-value: 2.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEeySEPELARir 83
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 neKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03259 73 --NIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLAkYARRLIRMKDGKIE 222
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHdqEEALA-LADRIAVMNEGRIV 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-221 |
3.07e-56 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 181.92 E-value: 3.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIR 83
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:PRK11153 82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAK-YARRLIRMKDGKI 221
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKrICDRVAVIDAGRL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
9.31e-56 |
|
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: 185.11 E-value: 9.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGEskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDR--QTGGSYKFDGKSIEEYSEpel 79
Cdd:COG1123 4 LLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHggRISGEVLLDGRDLLELSE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 aRIRNEKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSF 158
Cdd:COG1123 79 -ALRGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 159 VLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRI 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-221 |
1.10e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 176.55 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARir 83
Cdd:COG4619 1 LELEGLSFRVGG----KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 neKIGFVFQAFNLLArSSVYENVRLPLFYSNVPETawDSKIKSAIDAVGISHRIVHEP-GELSGGEKQRVAIARSFVLDP 162
Cdd:COG4619 75 --QVAYVPQEPALWG-GTVRDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH-EESLAKYARRLIRMKDGKI 221
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-221 |
1.64e-55 |
|
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: 177.54 E-value: 1.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSgesKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARi 82
Cdd:COG1120 1 MLEAENLSVGYGG---RPV-LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQAFNLLARSSVYENV---RLPLFYSNVPETAWD-SKIKSAIDAVGISH---RIVHEpgeLSGGEKQRVAIA 155
Cdd:COG1120 76 ---RIAYVPQEPPAPFGLTVRELValgRYPHLGLFGRPSAEDrEAVEEALERTGLEHladRPVDE---LSGGERQRVLIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 156 RSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAaRYADRLVLLKDGRI 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
1.88e-55 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 180.29 E-value: 1.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEySEPELa 80
Cdd:COG3842 3 MPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-LPPEK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 riRNekIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:COG3842 77 --RN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLAkYARRLIRMKDGKIE 222
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHdqEEALA-LADRIAVMNDGRIE 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-225 |
6.62e-55 |
|
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: 175.76 E-value: 6.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARi 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQ----AFNllARSSVYENVRLPLFYSNVPETawDSKIKSAIDAVGISHRIVHE-PGELSGGEKQRVAIARS 157
Cdd:COG1124 80 ---RVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGLPDR--EERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 158 FVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKY-ARRLIRMKDGKIESDI 225
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-220 |
8.66e-54 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 170.45 E-value: 8.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeYSEPELARIR 83
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL--TDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARSSVYENVRLPlfysnvpetawdskiksaidavgishrivhepgeLSGGEKQRVAIARSFVLDPE 163
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGK 220
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-221 |
5.09e-52 |
|
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: 170.62 E-value: 5.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDR--QTGGSYKFDGKSIEEYSEPEL 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPpgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIRNEKIGFVFQ----AFNllARSSVYENVRLPLFYSN-VPETAWDSKIKSAIDAVGISH--RIVHE-PGELSGGEKQR 151
Cdd:COG0444 81 RKIRGREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIHGgLSKAEARERAIELLERVGLPDpeRRLDRyPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKY-ARRLIRMKDGKI 221
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVAVMYAGRI 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-221 |
3.33e-50 |
|
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: 164.35 E-value: 3.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVY-----------QSGESK---------TVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGS 63
Cdd:cd03294 1 IKIKGLYKIFgknpqkafkllAKGKSKeeilkktgqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 64 YKFDGKSIEEYSEPELARIRNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGE 143
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 144 LSGGEKQRVAIARSFVLDPEMILADEPTGNLDS-KNGEMIIKLLDeLNRKTGRTIILITH--EESLaKYARRLIRMKDGK 220
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPlIRREMQDELLR-LQAELQKTIVFITHdlDEAL-RLGDRIAIMKDGR 238
|
.
gi 818736213 221 I 221
Cdd:cd03294 239 L 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-222 |
8.28e-50 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 165.63 E-value: 8.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEySEPELa 80
Cdd:COG3839 1 MASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD-LPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 riRNekIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:COG3839 75 --RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 161 DPEMILADEPTGNLDSK-NGEMIIKlLDELNRKTGRTIILITH--EESLAkYARRLIRMKDGKIE 222
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKlRVEMRAE-IKRLHRRLGTTTIYVTHdqVEAMT-LADRIAVMNDGRIQ 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-221 |
4.25e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 160.64 E-value: 4.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQsgesKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLdRQTGGSYKFDGKSIEEysepel 79
Cdd:COG1121 4 MPAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPPRR------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ariRNEKIGFVFQAFNLLAR--SSVYENVRLPLfYSNVPETAWDSK-----IKSAIDAVGISHRIvHEP-GELSGGEKQR 151
Cdd:COG1121 73 ---ARRRIGYVPQRAEVDWDfpITVRDVVLMGR-YGRRGLFRRPSRadreaVDEALERVGLEDLA-DRPiGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
2.04e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.69 E-value: 2.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEysepELARIR 83
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRlplFYS---NVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLR---FFArlyGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITH--EEsLAKYARRLIRMKDGKI 221
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHylEE-AERLCDRVAIIDKGRI 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-220 |
6.05e-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: 155.23 E-value: 6.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKtvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQTGgSYKFDGKSIEEYSEPELARi 82
Cdd:cd03228 1 IEFKNVSFSYPGRPKP--VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLlRLYDPTSG-EILIDGVDLRDLDLESLRK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQAFNLLARSsVYENVrlplfysnvpetawdskiksaidavgishrivhepgeLSGGEKQRVAIARSFVLDP 162
Cdd:cd03228 77 ---NIAYVPQDPFLFSGT-IRENI-------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGK 220
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-221 |
1.38e-47 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 154.90 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 5 EVKNLEKVYQsgesKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirn 84
Cdd:cd03214 1 EVENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 85 eKIGFVFQAfnllarssvyenvrlplfysnvpetawdskiksaIDAVGISH---RIVHEpgeLSGGEKQRVAIARSFVLD 161
Cdd:cd03214 74 -KIAYVPQA----------------------------------LELLGLAHladRPFNE---LSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 162 PEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAaRYADRVILLKDGRI 176
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-224 |
3.62e-47 |
|
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: 156.44 E-value: 3.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQsgESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGksIEEYSEPELARIR 83
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQ---------------AFNLlarssvyENVRLPlfysnvPETAWdSKIKSAIDAVGISHRIVHEPGELSGGE 148
Cdd:TIGR04520 77 -KKVGMVFQnpdnqfvgatveddvAFGL-------ENLGVP------REEMR-KRVDEALKLVGMEDFRDREPHLLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 149 KQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EEslAKYARRLIRMKDGKIESD 224
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHdmEE--AVLADRVIVMNKGKIVAE 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-222 |
6.05e-47 |
|
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: 154.33 E-value: 6.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPElariR 83
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NekIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03301 73 D--IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE--ESLAkYARRLIRMKDGKIE 222
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqvEAMT-MADRIAVMNDGQIQ 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-222 |
6.94e-47 |
|
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: 154.70 E-value: 6.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPElarir 83
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03300 72 -RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLAkYARRLIRMKDGKIE 222
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHdqEEALT-MSDRIAVMNKGKIQ 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-221 |
1.18e-46 |
|
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: 162.24 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKtvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQtGGSYKFDGKSIEEYSEPELARi 82
Cdd:COG4987 334 LELEDVSFRYPGAGRP--VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLlRFLDPQ-SGSITLGGVDLRDLDEDDLRR- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQAFNLLArSSVYENVRLplfysnVPETAWDSKIKSAIDAVGISHRIVHEP-------GE----LSGGEKQR 151
Cdd:COG4987 410 ---RIAVVPQRPHLFD-TTLRENLRL------ARPDATDEELWAALERVGLGDWLAALPdgldtwlGEggrrLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-221 |
5.56e-46 |
|
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: 161.93 E-value: 5.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLekVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQTGgSYKFDGKSIEEYSEPELARi 82
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlGLYEPTSG-RILIDGIDLRQIDPASLRR- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQAFNLLARSsVYENVRLplFYSNVPetawDSKIKSAIDAVGIS----------HRIVHEPGE-LSGGEKQR 151
Cdd:COG2274 550 ---QIGVVLQDVFLFSGT-IRENITL--GDPDAT----DEEIIEAARLAGLHdfiealpmgyDTVVGEGGSnLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-224 |
2.54e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 151.01 E-value: 2.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELArI 82
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKiGFVFQAFNLLARSSVYENVRL-PLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLD 161
Cdd:PRK09493 76 RQEA-GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 162 PEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLA-KYARRLIRMKDGKIESD 224
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAeKVASRLIFIDKGRIAED 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-214 |
2.81e-45 |
|
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: 149.99 E-value: 2.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 5 EVKNLeKVYQSGEsktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLdRQTGGSYKFDGKSIEEysepelariR 83
Cdd:cd03235 1 EVEDL-TVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSGSIRVFGKPLEK---------E 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARS--SVYENVRLPLFYSNV----PETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARS 157
Cdd:cd03235 67 RKRIGYVPQRRSIDRDFpiSVRDVVLMGLYGHKGlfrrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 158 FVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHE-ESLAKYARRLI 214
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDlGLVLEYFDRVL 203
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-221 |
1.96e-44 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 156.07 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLdRQTGGSYKFDGKSIEEYSEPELARi 82
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNlLLGFL-PPYSGSILINGVDLSDLDPASWRR- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQAFNLLArSSVYENVRL--PlfysnvpeTAWDSKIKSAIDAVGISHRIVHEP-------GE----LSGGEK 149
Cdd:COG4988 412 ---QIAWVPQNPYLFA-GTIRENLRLgrP--------DASDEELEAALEAAGLDEFVAALPdgldtplGEggrgLSGGQA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 150 QRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-220 |
4.99e-44 |
|
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: 145.08 E-value: 4.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 5 EVKNLEKVYQSGesktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirn 84
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 85 eKIGFVFQafnllarssvyenvrlplfysnvpetawdskiksaidavgishrivhepgeLSGGEKQRVAIARSFVLDPEM 164
Cdd:cd00267 74 -RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 165 ILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLA-KYARRLIRMKDGK 220
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-221 |
4.45e-43 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 144.63 E-value: 4.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEkIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:PRK10908 78 RRQ-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRkTGRTIILITHEESL-AKYARRLIRMKDGKI 221
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLiSRRSYRMLTLSDGHL 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-221 |
6.83e-43 |
|
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: 142.54 E-value: 6.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQsgesKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLL-QLLGFLdRQTGGSYKFDGKSIEEysEPELARi 82
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIkIILGLL-KPDSGEIKVLGKDIKK--EPEEVK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rnEKIGFVFQAFNLLARSSVYENVRlplfysnvpetawdskiksaidavgishrivhepgeLSGGEKQRVAIARSFVLDP 162
Cdd:cd03230 73 --RRIGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITH-EESLAKYARRLIRMKDGKI 221
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHiLEEAERLCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-222 |
1.03e-42 |
|
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: 144.37 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARir 83
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 neKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGI-----SHRIvhePGELSGGEKQRVAIARSF 158
Cdd:cd03295 76 --KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpaefADRY---PHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 159 VLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLaKYARRLIRMKDGKIE 222
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHdiDEAF-RLADRIAIMKNGEIV 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-222 |
1.66e-42 |
|
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: 143.63 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSepelarIR 83
Cdd:cd03296 3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARSSVYENVRLPL----FYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFV 159
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLaKYARRLIRMKDGKIE 222
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHdqEEAL-EVADRVVVMNKGRIE 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-221 |
2.33e-42 |
|
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: 149.83 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKS----TLLQLLGFLDRQTGGSYKFDGKSIEEYSE 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 77 PELARIRNEKIGFVFQ----AFNLLAR--SSVYENVRLplfYSNVPETAWDSKIKSAIDAVGISH---RIVHEPGELSGG 147
Cdd:COG4172 84 RELRRIRGNRIAMIFQepmtSLNPLHTigKQIAEVLRL---HRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 148 EKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESL-AKYARRLIRMKDGKI 221
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVvRRFADRVAVMRQGEI 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-222 |
4.39e-41 |
|
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: 139.78 E-value: 4.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgesKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQL-LGFLDRQTGGSYkFDGKSIEEYSePElari 82
Cdd:cd03299 1 LKVENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETiAGFIKPDSGKIL-LNGKDITNLP-PE---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:cd03299 70 -KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKIE 222
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLI 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-221 |
7.24e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 146.46 E-value: 7.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDrQTGGSYKFDGKSIEEYSepeLARI 82
Cdd:COG1132 340 IEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLlRFYD-PTSGRILIDGVDIRDLT---LESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNLLARSsVYENVRlplfYSNvpETAWDSKIKSAIDAVGISHRIVHEP-------GE----LSGGEKQR 151
Cdd:COG1132 413 R-RQIGVVPQDTFLFSGT-IRENIR----YGR--PDATDEEVEEAAKAAQAHEFIEALPdgydtvvGErgvnLSGGQRQR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-222 |
1.11e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 141.82 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGksieeysepELARI- 82
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG---------RDLFTn 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 ---RNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFV 159
Cdd:COG1118 70 lppRERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLAkYARRLIRMKDGKIE 222
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHdqEEALE-LADRVVVMNQGRIE 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-221 |
1.38e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 139.77 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLekVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKsieEYSEPELAR 81
Cdd:PRK13635 4 EIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRnEKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:PRK13635 79 VR-RQVGMVFQnPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
3.14e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 138.34 E-value: 3.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSgesKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEY----SE 76
Cdd:PRK11264 1 MSAIEVKNLVKKFHG---QTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 77 PELARIRNEKIGFVFQAFNLLARSSVYENV-RLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIA 155
Cdd:PRK11264 77 KGLIRQLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 156 RSFVLDPEMILADEPTGNLDSK-NGEMI--IKLLDELNrktgRTIILITHEESLAK-YARRLIRMKDGKI 221
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPElVGEVLntIRQLAQEK----RTMVIVTHEMSFARdVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
1.40e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.04 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLekVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKsieEYSEPELAR 81
Cdd:PRK13632 6 VMIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRNeKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:PRK13632 81 IRK-KIGIIFQnPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-221 |
1.53e-39 |
|
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: 135.77 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQTG----GSYKFDGKSIEEYSEPE 78
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDLIPGapdeGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 79 LARIRneKIGFVFQAFNLLaRSSVYENVRLPLFYSNV-PETAWDSKIKSAIDAVGIsHRIVH---EPGELSGGEKQRVAI 154
Cdd:cd03260 77 LELRR--RVGMVFQKPNPF-PGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAAL-WDEVKdrlHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 155 ARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTgrTIILITHeeSLAKYAR---RLIRMKDGKI 221
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTH--NMQQAARvadRTAFLLNGRL 218
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-224 |
1.83e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 136.47 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIE---------EY 74
Cdd:COG4598 9 LEVRDLHKSFGDLE----VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 75 SEP-ELARIRNeKIGFVFQAFNLLARSSVYENV-RLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRV 152
Cdd:COG4598 85 ADRrQLQRIRT-RLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 153 AIARSFVLDPEMILADEPTGNLDSK-NGE---MIIKLLDElnrktGRTIILITHEESLAK-YARRLIRMKDGKIESD 224
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPElVGEvlkVMRDLAEE-----GRTMLVVTHEMGFARdVSSHVVFLHQGRIEEQ 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-216 |
2.29e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 136.15 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYKFDGKSIEEysePEL 79
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIaGFL-APSSGEITLDGVPVTG---PGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARirnekiGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFV 159
Cdd:COG4525 77 DR------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLAkYARRLIRM 216
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHsvEEALF-LATRLVVM 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
5.05e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.00 E-value: 5.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirneKIGFVFQAFNLLARSSV 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 103 YENVRLPLFYSNVPETAWDSKIKSAIDAVGISH----RIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
1.19e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.82 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTL-LQLLGFLdRQTGGSYKFDGKSIEeYSEPELAR 81
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGIL-KPTSGEVLIKGEPIK-YDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRnEKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:PRK13639 76 VR-KTVGIVFQnPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVpVYADKVYVMSDGKI 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-221 |
1.69e-38 |
|
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: 132.38 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 9 LEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEeysepelARIRNEKIG 88
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 89 FVFQAFNL-LARSSVYENVRLPL-FYSNVPETAwdSKIKSAIDAVGISHRivHePGELSGGEKQRVAIARSFVLDPEMIL 166
Cdd:cd03226 75 YVMQDVDYqLFTDSVREELLLGLkELDAGNEQA--ETVLKDLDLYALKER--H-PLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 167 ADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH-EESLAKYARRLIRMKDGKI 221
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHdYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-222 |
2.03e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 134.40 E-value: 2.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGES-KTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEySEPELARI 82
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNL-LARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHE--PGELSGGEKQRVAIARSFV 159
Cdd:PRK13637 82 R-KKVGLVFQYPEYqLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDksPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKIE 222
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-221 |
2.57e-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: 132.95 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsGEskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:cd03219 1 LEVRGLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFL-RPTSGSVLFDGEDITGLPPHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnekIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDS----------KIKSAIDAVGISHRIVHEPGELSGGEKQRV 152
Cdd:cd03219 76 G---IGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARarreereareRAEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 153 AIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-222 |
9.07e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 134.44 E-value: 9.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEpelariR 83
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARSSVYENVRLPLfySNVPE------TAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARS 157
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAFGL--TVLPRrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 158 FVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKIE 222
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAmEVADRVVVMSQGNIE 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-221 |
1.83e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 131.75 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKVYQSGESKT--VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEysEPEL 79
Cdd:PRK13633 3 EMIKCKNVSYKYESNEESTekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD--EENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIRNeKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSF 158
Cdd:PRK13633 81 WDIRN-KAGMVFQnPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 159 VLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-224 |
1.87e-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: 130.02 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQsgESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARir 83
Cdd:cd03245 3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 neKIGFVFQAFNLLArSSVYENVRLPLFYSNvpetawDSKIKSAIDAVGIS-----H-----RIVHEPGE-LSGGEKQRV 152
Cdd:cd03245 79 --NIGYVPQDVTLFY-GTLRDNITLGAPLAD------DERILRAAELAGVTdfvnkHpngldLQIGERGRgLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 153 AIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKIESD 224
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-221 |
5.61e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 130.19 E-value: 5.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSG------ESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEY 74
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhQHQTV-LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 75 SEPELARIRNEkIGFVFQ----AFNllARSSVYENVRLPLFY-SNVPETAWDSKIKSAIDAVGISHRIVHE-PGELSGGE 148
Cdd:PRK10419 80 NRAQRKAFRRD-IQMVFQdsisAVN--PRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 149 KQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQI 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-227 |
5.93e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.10 E-value: 5.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 27 SFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYKFDGKSIEEYSePElARirneKIGFVFQAFNLLARSSVYEN 105
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIaGFL-PPDSGRILWNGQDLTALP-PA-ER----PVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 106 V------RLPLfysNVPETAwdsKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLD-SKN 178
Cdd:COG3840 92 IglglrpGLKL---TAEQRA---QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 818736213 179 GEMiIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKIESDIRI 227
Cdd:COG3840 166 QEM-LDLVDELCRERGLTVLMVTHDpEDAARIADRVLLVADGRIAADGPT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-221 |
6.45e-37 |
|
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: 129.21 E-value: 6.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQsgesKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEysEPELARi 82
Cdd:COG4555 1 MIEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK--EPREAR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rnEKIGFVFQAFNLLARSSVYENVRlplFYS---NVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFV 159
Cdd:COG4555 74 --RQIGVLPDERGLYDRLTVRENIR---YFAelyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHImQEVEALCDRVVILHKGKV 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-210 |
1.10e-36 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 129.50 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEkvYQSGESKTvaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:PRK11831 7 LVDMRGVS--FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNLLARSSVYENVRLPLF-YSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLD 161
Cdd:PRK11831 83 R-KRMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818736213 162 PEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEE----SLAKYA 210
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVpevlSIADHA 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-219 |
2.01e-36 |
|
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: 127.55 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEK---VYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGS--YKFDGKSIE--EYS 75
Cdd:COG4778 4 LLEVENLSKtftLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVDlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 76 EPELARIRNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVH-EPGELSGGEKQRVAI 154
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 155 ARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH-EESLAKYARRLIRMKDG 219
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHdEEVREAVADRVVDVTPF 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-221 |
2.05e-36 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 128.77 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSG------ESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSE 76
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgakQRAPV-LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 77 PELARIRNEkIGFVFQ----AFNllARSSVYENVRLPL-FYSNVPETAWDSKIKSAIDAVGISHRIVHE-PGELSGGEKQ 150
Cdd:TIGR02769 81 KQRRAFRRD-VQLVFQdspsAVN--PRMTVRQIIGEPLrHLTSLDESEQKARIAELLDMVGLRSEDADKlPRQLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 151 RVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQI 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-221 |
2.63e-36 |
|
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: 127.73 E-value: 2.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGesKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQtGGSYKFDGKSIEEYSEPELARi 82
Cdd:cd03253 1 IEFENVTFAYDPG--RPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfRFYDVS-SGSILIDGQDIREVTLDSLRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQ---AFNllarSSVYENVRlplfYSNVpeTAWDSKIKSAIDAVGISHRIVHEP-------GE----LSGGE 148
Cdd:cd03253 76 ---AIGVVPQdtvLFN----DTIGYNIR----YGRP--DATDEEVIEAAKAAQIHDKIMRFPdgydtivGErglkLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 149 KQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnrKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-224 |
2.79e-36 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 128.21 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFL---DRQTGGSYKFDGKSIEEysEPEL 79
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQR--EGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 AR-IRNEK--IGFVFQAFNLLARSSVYENVRL------PLFYSNVpetAWDSKIKS-----AIDAVGISHRIVHEPGELS 145
Cdd:PRK09984 78 ARdIRKSRanTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCF---SWFTREQKqralqALTRVGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 146 GGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKIESD 224
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHVFYD 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-224 |
3.03e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 130.84 E-value: 3.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqsgESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeysepelARI 82
Cdd:PRK09452 14 LVELRGISKSF---DGKEV-ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI--------THV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEK--IGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:PRK09452 82 PAENrhVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 161 DPEMILADEPTGNLDSK-NGEMIIKlLDELNRKTGRTIILITH--EESLAkYARRLIRMKDGKIESD 224
Cdd:PRK09452 162 KPKVLLLDESLSALDYKlRKQMQNE-LKALQRKLGITFVFVTHdqEEALT-MSDRIVVMRDGRIEQD 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-216 |
4.03e-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: 133.18 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDrQTGGSYKFDGKSIEEYSEPELARi 82
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNlLLGFVD-PTEGSIAVNGVPLADADADSWRD- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQAFNLLArSSVYENVRLPLfysnvPEtAWDSKIKSAIDAVGIS----------HRIVHEPGE-LSGGEKQR 151
Cdd:TIGR02857 397 ---QIAWVPQHPFLFA-GTIAENIRLAR-----PD-ASDAEIREALERAGLDefvaalpqglDTPIGEGGAgLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRM 216
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
9.03e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 126.28 E-value: 9.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIR 83
Cdd:COG4161 3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 --NEKIGFVFQAFNLLARSSVYEN-VRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:COG4161 79 llRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNrKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFArKVASQVVYMEKGRI 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-221 |
1.49e-35 |
|
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: 125.97 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqsgESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLgfldrqTGGSYKFDGKSI----EEYSEPE 78
Cdd:COG1119 3 LLELRNVTVRR---GGKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLI------TGDLPPTYGNDVrlfgERRGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 79 LARIRnEKIGFVFQAfnLLARSSVYENVR---LPLFYSNV-----PETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQ 150
Cdd:COG1119 73 VWELR-KRIGLVSPA--LQLRFPRDETVLdvvLSGFFDSIglyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 151 RVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLAKYARRLIrMKDGKI 221
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhvEEIPPGITHVLL-LKDGRV 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-221 |
2.67e-35 |
|
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: 123.10 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLekVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIr 83
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nekIGFVFQAFNLLArSSVYENVrlplfysnvpetawdskiksaidavgishrivhepgeLSGGEKQRVAIARSFVLDPE 163
Cdd:cd03246 78 ---VGYLPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-221 |
2.90e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.16 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQ------SGESKTV-ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYS 75
Cdd:COG4608 7 LLEVRDLKKHFPvrgglfGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 76 EPELARIRnEKIGFVFQ----AFNllARSSVYENVRLPLFYSNV-PETAWDSKIKSAIDAVGIS----HRIvhePGELSG 146
Cdd:COG4608 87 GRELRPLR-RRMQMVFQdpyaSLN--PRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpehaDRY---PHEFSG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 147 GEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKY-ARRLIRMKDGKI 221
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKI 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-221 |
3.65e-35 |
|
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: 124.65 E-value: 3.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQtGGSYKFDGKSIEEYSEPELari 82
Cdd:cd03254 3 IEFENVNFSYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLmRFYDPQ-KGQILIDGIDIRDISRKSL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rNEKIGFVFQAFNLLARsSVYENVRlplfYSNvpETAWDSKIKSAIDAVGISHRIVHEP-----------GELSGGEKQR 151
Cdd:cd03254 76 -RSMIGVVLQDTFLFSG-TIMENIR----LGR--PNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
4.34e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.90 E-value: 4.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGES-KTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIE-EYSEPELAR 81
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRnEKIGFVFQafnlLARSSVYENVRL------PLFYSnVPETAWDSKIKSAIDAVGISHRIVHE-PGELSGGEKQRVAI 154
Cdd:PRK13634 83 LR-KKVGIVFQ----FPEHQLFEETVEkdicfgPMNFG-VSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 155 ARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKGTV 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-224 |
5.14e-35 |
|
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: 123.76 E-value: 5.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 21 VALDGVSFL-----------VDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGksiEEYSEPELARirnEKIGF 89
Cdd:cd03298 1 VRLDKIRFSygeqpmhfdltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPAD---RPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 90 VFQAFNLLARSSVYENVRLPLfYSNVPETAWD-SKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILAD 168
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGL-SPGLKLTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 169 EPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKIESD 224
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
5.36e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 124.81 E-value: 5.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARir 83
Cdd:COG4604 2 IEIKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 neKIGFVFQAFNLLARSSVYENV---RLPlfYSNVPETAWD-SKIKSAIDAVG---ISHRIVHepgELSGGEKQRVAIAR 156
Cdd:COG4604 76 --RLAILRQENHINSRLTVRELVafgRFP--YSKGRLTAEDrEIIDEAIAYLDledLADRYLD---ELSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 157 SFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFAsCYADHIVAMKDGRV 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-227 |
5.63e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 124.79 E-value: 5.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 6 VKNLEKVYqsGEsKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSykfdgksIEEYSEPeLARIRnE 85
Cdd:PRK11247 15 LNAVSKRY--GE-RTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-------LLAGTAP-LAEAR-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 86 KIGFVFQAFNLLARSSVYENVRLPLfysnvpETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMI 165
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 166 LADEPTGNLDS-KNGEMiIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKIESDIRI 227
Cdd:PRK11247 156 LLDEPLGALDAlTRIEM-QDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKIGLDLTV 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-202 |
8.96e-35 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 124.00 E-value: 8.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYqsGesKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYKFDGKSIEEYSEPEL 79
Cdd:COG0411 2 DPLLEVRGLTKRF--G--GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFY-RPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIrnekiGFV--FQAFNLLARSSVYENVR---------------LPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPG 142
Cdd:COG0411 77 ARL-----GIArtFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 143 ELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH 202
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEH 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
1.05e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.46 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPElarIR 83
Cdd:PRK13647 5 IEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NeKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:PRK13647 79 S-KVGLVFQdPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAaEWADQVIVLKEGRV 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-213 |
1.46e-34 |
|
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: 122.20 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQsgesKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPelari 82
Cdd:COG4133 2 MLEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKIGFVFQAFNLLARSSVYENVRlplFYSNVPETAWD-SKIKSAIDAVGISHRIvHEP-GELSGGEKQRVAIARSFVL 160
Cdd:COG4133 73 YRRRLAYLGHADGLKPELTVRENLR---FWAALYGLRADrEAIDEALEAVGLAGLA-DLPvRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYARRL 213
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELAAARVL 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-221 |
1.94e-34 |
|
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: 128.26 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVY-------QSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTL-LQLLGFLDrqTGGSYKFDGKSIEEY 74
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIP--SEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 75 SEPELARIRNEkIGFVFQ----AFNllARSSVYENVRLPL--FYSNVPETAWDSKIKSAIDAVGISHRIVHE-PGELSGG 147
Cdd:COG4172 353 SRRALRPLRRR-MQVVFQdpfgSLS--PRMTVGQIIAEGLrvHGPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 148 EKQRVAIARSFVLDPEMILADEPTGNLDskngeM-----IIKLLDELNRKTGRTIILITHEESLAKY-ARRLIRMKDGKI 221
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALD-----VsvqaqILDLLRDLQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKV 504
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
2.10e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.19 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEeYSEPELARI 82
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQA-FNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHrIVHEPGE-LSGGEKQRVAIARSFVL 160
Cdd:PRK13636 81 R-ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRV 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-223 |
3.50e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.30 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGksiEEYSEPELA 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 RIRnEKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFV 159
Cdd:PRK13650 78 DIR-HKIGMVFQnPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKIES 223
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVES 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-224 |
5.62e-34 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 120.86 E-value: 5.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 32 KGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIRNEKIGFVFQAFNLLARSSVYENVRLPL- 110
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 111 FYSNVPETAWDSKIksaIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELN 190
Cdd:cd03297 102 RKRNREDRISVDEL---LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIK 178
|
170 180 190
....*....|....*....|....*....|....*
gi 818736213 191 RKTGRTIILITHEESLAKY-ARRLIRMKDGKIESD 224
Cdd:cd03297 179 KNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYI 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-219 |
8.01e-34 |
|
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: 121.03 E-value: 8.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeySEPELARIrnekigFVFQAFNLLARSSV 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---TEPGPDRM------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 103 YENVRLPL--FYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGE 180
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 818736213 181 MIIKLLDELNRKTGRTIILITHEESLAKY-ARRLIRMKDG 219
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNG 191
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-224 |
8.82e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 121.80 E-value: 8.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLekVYQSGeSKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYKFDGKSIEEYSEPELAR 81
Cdd:PRK13548 2 MLEARNL--SVRLG-GRTL-LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IR-----NEKIGFVFqafnllarsSVYENVRL---PLFYSNVPETAwdsKIKSAIDAVGISH---RIVHepgELSGGEKQ 150
Cdd:PRK13548 77 RRavlpqHSSLSFPF---------TVEEVVAMgraPHGLSRAEDDA---LVAAALAQVDLAHlagRDYP---QLSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 151 RVAIARsfVL--------DPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:PRK13548 142 RVQLAR--VLaqlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAaRYADRIVLLHQGRL 219
|
...
gi 818736213 222 ESD 224
Cdd:PRK13548 220 VAD 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-203 |
1.32e-33 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 122.91 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKS-TLLQLLGFLDR--QTGGSYKFDGKSIEEYSEP 77
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 78 ELARIRNEKIGFVFQ----AFNLLARSS--VYENVRLPLFYSNvpETAWDSKIKsAIDAVGISH---RIVHEPGELSGGE 148
Cdd:PRK09473 90 ELNKLRAEQISMIFQdpmtSLNPYMRVGeqLMEVLMLHKGMSK--AEAFEESVR-MLDAVKMPEarkRMKMYPHEFSGGM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 149 KQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE 203
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
2.12e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 121.73 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKlIEVKNLEKVYQSGESKTV-ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKF---------DGKS 70
Cdd:PRK13651 1 MQ-IKVKNIVKIFNKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 71 IEEYSE------PELARIRNEK-----IGFVFQ-AFNLLARSSVYENVRL-PLFYSNVPETAwDSKIKSAIDAVGISHRI 137
Cdd:PRK13651 80 KEKVLEklviqkTRFKKIKKIKeirrrVGVVFQfAEYQLFEQTIEKDIIFgPVSMGVSKEEA-KKRAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 138 VHE-PGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNrKTGRTIILITHE-ESLAKYARRLIR 215
Cdd:PRK13651 159 LQRsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDlDNVLEWTKRTIF 237
|
....*....
gi 818736213 216 MKDGKIESD 224
Cdd:PRK13651 238 FKDGKIIKD 246
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-221 |
3.28e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 119.73 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGS-----YKFDGKSieEYSEPE 78
Cdd:PRK11124 3 IQLNGINCFYGA----HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlniagNHFDFSK--TPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 79 LARIRnEKIGFVFQAFNLLARSSVYEN-VRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARS 157
Cdd:PRK11124 77 IRELR-RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 158 FVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVArKTASRVVYMENGHI 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-202 |
5.84e-33 |
|
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: 124.40 E-value: 5.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 21 VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQtGGSYKFDGKSIEEYSEPELARIrnekIGFVFQAFNLLAr 99
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLaGLLDPL-QGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFD- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 100 SSVYENVRLplfysnVPETAWDSKIKSAIDAVGIS----------HRIVHEPGE-LSGGEKQRVAIARSFVLDPEMILAD 168
Cdd:TIGR02868 423 TTVRENLRL------ARPDATDEELWAALERVGLAdwlralpdglDTVLGEGGArLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 818736213 169 EPTGNLDSKNG-EMIIKLLDELnrkTGRTIILITH 202
Cdd:TIGR02868 497 EPTEHLDAETAdELLEDLLAAL---SGRTVVLITH 528
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-221 |
7.94e-33 |
|
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: 118.80 E-value: 7.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLG-FLDrQTGGSYKFDGKSIEEYSEPELARi 82
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErFYD-PTSGEILLDGVDIRDLNLRWLRS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQAFNLLARSsVYENVRLPLFYSNVPEtawdskIKSAIDAVGISHRIVHEP-----------GELSGGEKQR 151
Cdd:cd03249 78 ---QIGLVSQEPVLFDGT-IAENIRYGKPDATDEE------VEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnrKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
8.39e-33 |
|
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: 118.24 E-value: 8.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeYSEPELARir 83
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPREVR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGI---SHRIVhepGELSGGEKQRVAIARSFVL 160
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLleaADRLV---KTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESlAKYARRLIRMKDGKI 221
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHymEEA-EQLCDRVAIIDHGRI 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-223 |
8.70e-33 |
|
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: 121.37 E-value: 8.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDgVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIRNEKIGFVFQAFNLLARSS 101
Cdd:TIGR02142 13 SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 102 VYENVRLPLFYSNVPET--AWDSkiksAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNG 179
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERriSFER----VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 818736213 180 EMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKIES 223
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGRVAA 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-221 |
9.23e-33 |
|
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: 117.68 E-value: 9.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGesktVALDGVSFLVDKGeFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEpelaRIR 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNrkTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHIvEDVESLCNQVAVLNKGKL 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
9.26e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.47 E-value: 9.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTvaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeySEPELARI 82
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLD 161
Cdd:PRK13648 82 R-KHIGIVFQnPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 162 PEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-222 |
1.19e-32 |
|
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: 123.70 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLekVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:COG4618 331 LSVENL--TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rnekIGFVFQAFNLLArSSVYENV-RLPlfysnvpeTAWDSKIKSAIDAVGISHRIVHEP-------GE----LSGGEKQ 150
Cdd:COG4618 408 ----IGYLPQDVELFD-GTIAENIaRFG--------DADPEKVVAAAKLAGVHEMILRLPdgydtriGEggarLSGGQRQ 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 151 RVAIARSFVLDPEMILADEPTGNLDSkNGE-MIIKLLDELnRKTGRTIILITHEESLAKYARRLIRMKDGKIE 222
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDD-EGEaALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-221 |
1.49e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.16 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGES-KTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIE-EYSEPELAR 81
Cdd:PRK13641 3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRnEKIGFVFQ-AFNLLARSSVYENVRL-PLFYSNVPETAwDSKIKSAIDAVGISHRIV-HEPGELSGGEKQRVAIARSF 158
Cdd:PRK13641 83 LR-KKVSLVFQfPEAQLFENTVLKDVEFgPKNFGFSEDEA-KEKALKWLKKVGLSEDLIsKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 159 VLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-200 |
2.03e-32 |
|
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: 117.15 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsGESktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLdRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:cd03224 1 LEVENLNAGY--GKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLL-PPRSGSIRFDGRDITGLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQAFNLLARSSVYENVRLPLFysnvpeTAWDSKIKSAIDAV----GISHRIVHEP-GELSGGEKQRVAIARS 157
Cdd:cd03224 76 ---GIGYVPEGRRIFPELTVEENLLLGAY------ARRRAKRKARLERVyelfPRLKERRKQLaGTLSGGEQQMLAIARA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 818736213 158 FVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILI 200
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLV 188
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-222 |
2.75e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 119.95 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYqsgESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYsEPela 80
Cdd:PRK11650 1 MAGLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL-EP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 riRNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:PRK11650 74 --ADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 161 DPEMILADEPTGNLDSK-NGEMIIKLLdELNRKTGRTIILITHEESLA-KYARRLIRMKDGKIE 222
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKlRVQMRLEIQ-RLHRRLKTTSLYVTHDQVEAmTLADRVVVMNGGVAE 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-220 |
2.99e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 120.33 E-value: 2.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQsGESktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEE---YSEPel 79
Cdd:PRK11607 19 LLEIRNLTKSFD-GQH---AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvppYQRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 arirnekIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFV 159
Cdd:PRK11607 93 -------INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 160 LDPEMILADEPTGNLDSK-NGEMIIKLLDELNRkTGRTIILITHEESLA-KYARRLIRMKDGK 220
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKlRDRMQLEVVDILER-VGVTCVMVTHDQEEAmTMAGRIAIMNRGK 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-221 |
8.20e-32 |
|
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: 115.54 E-value: 8.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGksIEEYSEPELARI 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnekIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:cd03266 79 R---LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHImQEVERLCDRVVVLHRGRV 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-224 |
3.57e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.07 E-value: 3.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIE---------EY 74
Cdd:PRK10619 6 LNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 75 SEPELARIRNEKIGFVFQAFNLLARSSVYENV-RLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHE-PGELSGGEKQRV 152
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 153 AIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLAKY-ARRLIRMKDGKIESD 224
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-206 |
3.90e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.80 E-value: 3.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQtGGSYKFDGKSIEEysePELARirnekiGFVFQAFNLLARS 100
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIaGFVPYQ-HGSITLDGKPVEG---PGAER------GVVFQNEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 101 SVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGE 180
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180
....*....|....*....|....*...
gi 818736213 181 MIIKLLDELNRKTGRTIILITH--EESL 206
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITHdiEEAV 193
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-221 |
4.11e-31 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.74 E-value: 4.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSepelarIR 83
Cdd:PRK11432 7 VVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS------IQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSA---IDAVGISHRIVHEpgeLSGGEKQRVAIARSFVL 160
Cdd:PRK11432 77 QRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEAlelVDLAGFEDRYVDQ---ISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKI 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-221 |
7.17e-31 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 119.05 E-value: 7.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKtvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSepeLARI 82
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRP--ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEkIGFVFQAFNLLaRSSVYENVRlplfYSNvPETAWDSKIKSAIDAV-----------GISHRIVHEPGELSGGEKQR 151
Cdd:TIGR02203 405 RRQ-VALVSQDVVLF-NDTIANNIA----YGR-TEQADRAEIERALAAAyaqdfvdklplGLDTPIGENGVLLSGGQRQR 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-221 |
7.43e-31 |
|
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: 113.48 E-value: 7.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKtvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLG-FLDrQTGGSYKFDGKSIEEYSEPELARi 82
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrFYD-VDSGRILIDGHDVRDYTLASLRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQ---AFNllarSSVYENVRlplfYSNVPETawDSKIKSAIDAVGISHRIVHEP-------GE----LSGGE 148
Cdd:cd03251 77 ---QIGLVSQdvfLFN----DTVAENIA----YGRPGAT--REEVEEAARAANAHEFIMELPegydtviGErgvkLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 149 KQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-204 |
2.17e-30 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 115.13 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYqsGE---SKTVALDgvsflVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYsEP 77
Cdd:PRK11000 1 MASVTLRNVTKAY--GDvviSKDINLD-----IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV-PP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 78 ElarirNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARS 157
Cdd:PRK11000 73 A-----ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 818736213 158 FVLDPEMILADEPTGNLDSK-NGEMIIKlLDELNRKTGRTIILITHEE 204
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAAlRVQMRIE-ISRLHKRLGRTMIYVTHDQ 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
3.53e-30 |
|
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: 111.06 E-value: 3.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEeySEPELARir 83
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRlplFYS---NVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLR---FYArlkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELnrKTGRTIILITHE----ESLAKyarRLIRMKDGKI 221
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSmdeaEALCD---RIAIMSDGKL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-220 |
5.37e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 116.34 E-value: 5.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVY-QSGESKTVaLDGVSFLVDKGEFIAIMGPSGSGKS-TLLQLLGFLDRQ----TGGSYKFDGKSIEEY 74
Cdd:PRK15134 3 QPLLAIENLSVAFrQQQTVRTV-VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 75 SEPELARIRNEKIGFVFQ----AFNLL--ARSSVYENVRLplfYSNVPETAWDSKIKSAIDAVGISH---RIVHEPGELS 145
Cdd:PRK15134 82 SEQTLRGVRGNKIAMIFQepmvSLNPLhtLEKQLYEVLSL---HRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 146 GGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGK 220
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNGR 234
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-221 |
5.98e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 111.75 E-value: 5.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEkvYQSGeSKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYKFDGKSIEEYSEPELAR 81
Cdd:COG4559 1 MLEAENLS--VRLG-GRTL-LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IR-----NEKIGFVFqafnllarsSVYENVRLPLfYSNVPETAWDSKI-KSAIDAVGISH---RIVHEpgeLSGGEKQRV 152
Cdd:COG4559 76 RRavlpqHSSLAFPF---------TVEEVVALGR-APHGSSAAQDRQIvREALALVGLAHlagRSYQT---LSGGEQQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 153 AIARsfVL---------DPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESL-AKYARRLIRMKDGKI 221
Cdd:COG4559 143 QLAR--VLaqlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLaAQYADRILLLHQGRL 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-221 |
6.40e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.11 E-value: 6.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKVYQSgESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELAR 81
Cdd:PRK13642 3 KILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 irneKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:PRK13642 82 ----KIGMVFQnPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-202 |
9.54e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 110.90 E-value: 9.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL--------GFldrQTGGSYKFDGKSI--EE 73
Cdd:COG1117 12 IEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipGA---RVEGEILLDGEDIydPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 74 YSEPELARirneKIGFVFQAFNLLArSSVYENVRLPLFYSNVpetawdsKIKSAIDAvgishrIV--------------- 138
Cdd:COG1117 85 VDVVELRR----RVGMVFQKPNPFP-KSIYDNVAYGLRLHGI-------KSKSELDE------IVeeslrkaalwdevkd 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 139 --HEPG-ELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnrKTGRTIILITH 202
Cdd:COG1117 147 rlKKSAlGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTH 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-221 |
1.01e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.82 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQsgESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFL--DRQTGGSYKFDGKSIeeySEPELA 80
Cdd:PRK13640 6 VEFKHVSFTYP--DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLlpDDNPNSKITVDGITL---TAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 RIRnEKIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFV 159
Cdd:PRK13640 81 DIR-EKVGIVFQnPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-202 |
1.02e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.77 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFL-----DRQTGGSYKFDGKSIEEYS 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 76 EPELARirneKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWD--SKIKSAIDAVG----ISHRIVHEPGELSGGEK 149
Cdd:PRK14247 77 VIELRR----RVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818736213 150 QRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnrKTGRTIILITH 202
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTH 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-221 |
1.12e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 111.23 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 18 SKTVAlDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirneKIGFVFQAFNLL 97
Cdd:PRK10253 19 KYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 98 ARSSVYENV------RLPLFysnvpeTAW----DSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILA 167
Cdd:PRK10253 94 GDITVQELVargrypHQPLF------TRWrkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 168 DEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKI 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-221 |
1.37e-29 |
|
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: 107.90 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSePELARir 83
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS-PRDAR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQafnllarssvyenvrlplfysnvpetawdskiksaidavgishrivhepgeLSGGEKQRVAIARSFVLDPE 163
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH--EEsLAKYARRLIRMKDGKI 221
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHrlDE-VFEIADRVTVLRDGRV 160
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-223 |
1.73e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 110.40 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGesktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKS-----IEEYSEP 77
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 78 ELARIRNEKIGFVFQ--AFNLLARSSVYENVRLPLF------YSNVPETA--WDSKIKsaIDAvgisHRIVHEPGELSGG 147
Cdd:PRK11701 82 ERRRLLRTEWGFVHQhpRDGLRMQVSAGGNIGERLMavgarhYGDIRATAgdWLERVE--IDA----ARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 148 EKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAK-YARRLIRMKDGK-IES 223
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLAHRLLVMKQGRvVES 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-221 |
2.22e-29 |
|
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: 114.92 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDrQTGGSYKFDGKSIEEYSEPELARIrnekIGFVFQ---AFNlla 98
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfRFYD-VTSGRILIDGQDIRDVTQASLRAA----IGIVPQdtvLFN--- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 99 rSSVYENVRlplfYSNvPEtAWDSKIKSAIDAVGISHRIVHEP-------GE----LSGGEKQRVAIARSFVLDPEMILA 167
Cdd:COG5265 446 -DTIAYNIA----YGR-PD-ASEEEVEAAARAAQIHDFIESLPdgydtrvGErglkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 818736213 168 DEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRI 570
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-221 |
3.53e-29 |
|
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: 113.98 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 17 ESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirneKIGFVFQAFNL 96
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK----HIGYLPQDVEL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 97 LArSSVYENVrlplfySNVPETAWDSKIKSAIDAVGISHRIVHEP-----------GELSGGEKQRVAIARSFVLDPEMI 165
Cdd:TIGR01842 404 FP-GTVAENI------ARFGENADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 166 LADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
6.67e-29 |
|
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: 112.97 E-value: 6.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-----------------------GFLDRQT 60
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhvalcekcGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 61 ---------GGSYKFDGKSIEEYSEPELARIRnEKIGFVFQ-AFNLLARSSVYENVRLPLfysnvPETAWDSK--IKSA- 127
Cdd:TIGR03269 77 kvgepcpvcGGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEAL-----EEIGYEGKeaVGRAv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 128 --IDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH-EE 204
Cdd:TIGR03269 151 dlIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwPE 230
|
250
....*....|....*..
gi 818736213 205 SLAKYARRLIRMKDGKI 221
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEI 247
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-221 |
7.01e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.66 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVY-----------QSGESKTVALD------GV---SFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGS 63
Cdd:PRK10070 5 LEIKNLYKIFgehpqrafkyiEQGLSKEQILEktglslGVkdaSLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 64 YKFDGKSIEEYSEPELARIRNEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGE 143
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 144 LSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEV 243
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-221 |
7.05e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 7.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGES-KTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKIGFVFQafnlLARSSVYE------------NVRLPLfySNVPETAWDSKIKsaidaVGISHRIVHE-PGELSGGEK 149
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFEdtvereiifgpkNFKMNL--DEVKNYAHRLLMD-----LGFSRDVMSQsPFQMSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 150 QRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-211 |
9.56e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.39 E-value: 9.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFL-----DRQTGGSYKFDGKSIeeYSePE 78
Cdd:PRK14267 5 IETVNLRVYYGSNH----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YS-PD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 79 LARIR-NEKIGFVFQAFNLLARSSVYENVRLPLFYSNV--PETAWDSKIKSAIDAVG----ISHRIVHEPGELSGGEKQR 151
Cdd:PRK14267 78 VDPIEvRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAAlwdeVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnrKTGRTIILITHeeSLAKYAR 211
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTH--SPAQAAR 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-221 |
1.62e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 112.23 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKtvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLG-FLDRQTgGSYKFDGKSIEEYSEPELar 81
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQP--VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQ-GEILLNGQPIADYSEAAL-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 iRNeKIGFVFQAFNLLArSSVYENVRLPLfysnvpETAWDSKIKSAIDAVGISHRIVHEPG----------ELSGGEKQR 151
Cdd:PRK11160 413 -RQ-AISVVSQRVHLFS-ATLRDNLLLAA------PNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-222 |
1.99e-28 |
|
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: 105.47 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEkvYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQTGgSYKFDGKSIEEYSEpelarI 82
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLKPQQG-EITLDGVPVSDLEK-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKIGFVFQAFNLLArSSVYENVRLPLfysnvpetawdskiksaidavgishrivhepgelSGGEKQRVAIARSFVLDP 162
Cdd:cd03247 73 LSSLISVLNQRPYLFD-TTLRNNLGRRF----------------------------------SGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKIE 222
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-209 |
2.23e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 109.03 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLeKVY---QSGES------KTV-ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIE 72
Cdd:PRK15079 8 LLEVADL-KVHfdiKDGKQwfwqppKTLkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 73 EYSEPELARIRNEkIGFVFQafNLLA----RSSVYENVRLPL--FYSNVPETAWDSKIKSAIDAVGISHRIVHE-PGELS 145
Cdd:PRK15079 87 GMKDDEWRAVRSD-IQMIFQ--DPLAslnpRMTIGEIIAEPLrtYHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 146 GGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKY 209
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKH 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-222 |
4.69e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.35 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARi 82
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPDVPV-LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rneKIGFVFQAFNLLARsSVYENVRLPLFYSNVPETAWDSKIKSAIDAV-GISHRIVHEPGE----LSGGEKQRVAIARS 157
Cdd:TIGR00958 556 ---QVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFImEFPNGYDTEVGEkgsqLSGGQKQRIAIARA 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 158 FVLDPEMILADEPTGNLDSKngemIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKIE 222
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-221 |
5.31e-28 |
|
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: 105.63 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 20 TVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELarirNEKIGFVFQAFNLLAR 99
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 100 SsVYENVRLPLfysnvpETAWDSKIKSAIDAVG-------ISHRIVHEPGE----LSGGEKQRVAIARSFVLDPEMILAD 168
Cdd:cd03248 103 S-LQDNIAYGL------QSCSFECVKEAAQKAHahsfiseLASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818736213 169 EPTGNLDSKNGEMIIKLLDELNRKtgRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-202 |
1.53e-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: 103.78 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTVA--LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDR-QTGGSYKFDGKSIeeySEPEL 79
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGlGVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIrnekIGFVFQAFNLLARSSVYENvrlpLFYSnvpetawdSKIKSaidavgishrivhepgeLSGGEKQRVAIARSFV 159
Cdd:cd03213 81 RKI----IGYVPQDDILHPTLTVRET----LMFA--------AKLRG-----------------LSGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH 202
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-221 |
2.68e-27 |
|
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: 103.45 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPelarir 83
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPetawDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEES-LAKYARRLIRMKDGKI 221
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSeIQKVADRIGIINKGKL 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-221 |
8.77e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 8.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeEYSEPELAri 82
Cdd:COG1129 4 LLEMRGISKSF-GG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKIGFVFQAFNLLARSSVYENV---RLPLFYSNVPETAWDSKIKSAIDAVGIS---HRIVhepGELSGGEKQRVAIAR 156
Cdd:COG1129 77 QAAGIAIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDidpDTPV---GDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 157 SFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH--EEsLAKYARRLIRMKDGKI 221
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHrlDE-VFEIADRVTVLRDGRL 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-221 |
1.14e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.67 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSG---ESKtvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSE-PEL 79
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGR--ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIRnEKIGFVFQafnlLARSSVYENVRL------PLFYSNVPETAwDSKIKSAIDAVGISHRIVHE-PGELSGGEKQRV 152
Cdd:PRK13649 81 KQIR-KKVGLVFQ----FPESQLFEETVLkdvafgPQNFGVSQEEA-EALAREKLALVGISESLFEKnPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 153 AIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITH-EESLAKYARRLIRMKDGKI 221
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHlMDDVANYADFVYVLEKGKL 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-216 |
1.42e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.16 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 21 VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSykfdgksieeysepeLARIRNEKIGFVFQafnllaRS 100
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT---------------VRRAGGARVAYVPQ------RS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 101 SVYEnvRLPLFYSNV-------------PETAWD-SKIKSAIDAVGI---SHRIVhepGELSGGEKQRVAIARSFVLDPE 163
Cdd:NF040873 65 EVPD--SLPLTVRDLvamgrwarrglwrRLTRDDrAAVDDALERVGLadlAGRQL---GELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYARRLIRM 216
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-224 |
1.73e-26 |
|
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: 102.03 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQ----------------SGESKTV-ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKF 66
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfKRKYREVeALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 67 DGKSIEEYSEPELARIrnekiGFVFQ-----AFNLLARSSVYENVRLplfYsNVPETAWDSKIKSAIDAVGISHrIVHEP 141
Cdd:cd03267 81 AGLVPWKRRKKFLRRI-----GVVFGqktqlWWDLPVIDSFYLLAAI---Y-DLPPARFKKRLDELSELLDLEE-LLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 142 -GELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDG 219
Cdd:cd03267 151 vRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKG 230
|
....*
gi 818736213 220 KIESD 224
Cdd:cd03267 231 RLLYD 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-214 |
2.25e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.33 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 9 LEKV-YQSGEskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSePELARirnEKI 87
Cdd:PRK10247 10 LQNVgYLAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK-PEIYR---QQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 88 GFVFQAFNLLArSSVYENVRLP-LFYSNVPETAwdsKIKSAIDAVGISHRIVHEP-GELSGGEKQRVAIARSFVLDPEMI 165
Cdd:PRK10247 84 SYCAQTPTLFG-DTVYDNLIFPwQIRNQQPDPA---IFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 818736213 166 LADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLI 214
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-221 |
2.34e-26 |
|
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: 104.03 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDgVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGK----SIEEYSEPELARirneKIGFVFQAFNLL 97
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRR----RIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 98 ARSSVYENVRlplF-YSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDS 176
Cdd:COG4148 90 PHLSVRGNLL---YgRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 818736213 177 KNGEMIIKLLDELNRKTGRTIILITH--EEsLAKYARRLIRMKDGKI 221
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHslDE-VARLADHVVLLEQGRV 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-175 |
2.53e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.02 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDR--QTGGSYKFDGKSIEEYsePELARirneKIGFVFQAFNLLAR 99
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPafSASGEVLLNGRRLTAL--PAEQR----RIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 100 SSVYENVR--LPlfySNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLD 175
Cdd:COG4136 91 LSVGENLAfaLP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-201 |
2.97e-26 |
|
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: 101.47 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIr 83
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 neKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHrIVHEPG-ELSGGEKQRVAIARSFVLDP 162
Cdd:cd03218 76 --GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITH-LRKSKAsSLSGGERRRVEIARALATNP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDEL-NRKTGrtiILIT 201
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILkDRGIG---VLIT 189
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
5.30e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.80 E-value: 5.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGESktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELA 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKE---ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 RIrnekIGFVFQ-AFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFV 159
Cdd:PRK13652 78 KF----VGLVFQnPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESL-AKYARRLIRMKDGKI 221
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLvPEMADYIYVMDKGRI 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-221 |
6.61e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.04 E-value: 6.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSepeLARIRNeKIGFVFQAFNLLARsS 101
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRR-NIAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 102 VYENVRLPlfysnvPETAWDSKIKSAIDAVGISHRIVHEP-------GE----LSGGEKQRVAIARSFVLDPEMILADEP 170
Cdd:PRK13657 425 IEDNIRVG------RPDATDEEMRAAAERAQAHDFIERKPdgydtvvGErgrqLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 818736213 171 TGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-202 |
1.37e-25 |
|
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: 99.27 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQ---TGGSYKFDGKSieeySEPELARirnEKIGFVFQAFNLLAR 99
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP----RKPDQFQ---KCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 100 SSVYENvrlpLFYSNV---PETAwDSKIKSAIDAVGISHRIVHEP------GELSGGEKQRVAIARSFVLDPEMILADEP 170
Cdd:cd03234 96 LTVRET----LTYTAIlrlPRKS-SDAIRKKRVEDVLLRDLALTRiggnlvKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|..
gi 818736213 171 TGNLDSKNGEMIIKLLDELNRKtGRTIILITH 202
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-221 |
1.80e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.77 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRQtgGSYKFDGksiEEYSEPELARI 82
Cdd:PRK11174 350 IEAEDLEILSPDG---KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFLPYQ--GSLKING---IELRELDPESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNLLArSSVYENVRLplfySNVpeTAWDSKIKSAIDAVGIS-------HRIVHEPGE----LSGGEKQR 151
Cdd:PRK11174 422 R-KHLSWVGQNPQLPH-GTLRDNVLL----GNP--DASDEQLQQALENAWVSeflpllpQGLDTPIGDqaagLSVGQAQR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHE-ESLAKYARRLIrMKDGKI 221
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQlEDLAQWDQIWV-MQDGQI 561
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
9-221 |
2.09e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.06 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 9 LEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTL-LQLLGFLDRQTGgsyKFDGKSIEEYSEPELARIRnEKI 87
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLLRPQKG---KVLVSGIDTGDFSKLQGIR-KLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 88 GFVFQ--AFNLLARSsVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMI 165
Cdd:PRK13644 80 GIVFQnpETQFVGRT-VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 166 LADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-220 |
2.84e-25 |
|
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: 97.93 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTV-ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRqTGGSYKFDGKsieeysepelar 81
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 irnekIGFVFQ-AFnlLARSSVYENVrlpLFYSNvpetaWDS-KIKSAIDAVGI-------SHRIVHEPGE----LSGGE 148
Cdd:cd03250 68 -----IAYVSQePW--IQNGTIRENI---LFGKP-----FDEeRYEKVIKACALepdleilPDGDLTEIGEkginLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 149 KQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIK--LLDELnrKTGRTIILITHEESLAKYARRLIRMKDGK 220
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-221 |
5.41e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.55 E-value: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQsgesKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARir 83
Cdd:PRK11231 3 LRTENLTVGYG----TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 neKIGFVFQafNLLARSSVyeNVRLPLFYSNVPE-TAW-------DSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIA 155
Cdd:PRK11231 77 --RLALLPQ--HHLTPEGI--TVRELVAYGRSPWlSLWgrlsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 156 RSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQAsRYCDHLVVLANGHV 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-221 |
6.72e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.22 E-value: 6.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 5 EVKNLE-KVyqsgESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLD-RQTGGSYKFDGKSIEEYSEPELAR 81
Cdd:COG0396 2 EIKNLHvSV----EGKEI-LKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHPKyEVTSGSILLDGEDILELSPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 irnEKIGFVFQA---------FNLLARSsvYENVRLPlfysNVPETAWDSKIKSAIDAVGIS----HRIVHEpgELSGGE 148
Cdd:COG0396 77 ---AGIFLAFQYpveipgvsvSNFLRTA--LNARRGE----ELSAREFLKLLKEKMKELGLDedflDRYVNE--GFSGGE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 149 KQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKY--ARRLIRMKDGKI 221
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHYQRILDYikPDFVHVLVDGRI 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-224 |
7.11e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.73 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 27 SFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYKFDGksiEEYSEPELARirnEKIGFVFQAFNLLARSSVYEN 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIaGFL-TPASGSLTLNG---QDHTTTPPSR---RPVSMLFQENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 106 VRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLD-SKNGEMiIK 184
Cdd:PRK10771 92 IGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpALRQEM-LT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 818736213 185 LLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKIESD 224
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSlEDAARIAPRSLVVADGRIAWD 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-221 |
7.11e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.93 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQTG----GSYKFDG--KSIEEysepeLARIRNEkIGFVFQ-- 92
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTnGLIISETGqtivGDYAIPAnlKKIKE-----VKRLRKE-IGLVFQfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 93 AFNLLARSSVYENVRLPLFYSNVPETAWdSKIKSAIDAVGISHRIV-HEPGELSGGEKQRVAIARSFVLDPEMILADEPT 171
Cdd:PRK13645 100 EYQLFQETIEKDIAFGPVNLGENKQEAY-KKVPELLKLVQLPEDYVkRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 818736213 172 GNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-200 |
7.14e-25 |
|
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: 97.75 E-value: 7.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYqsGESKtvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLdRQTGGSYKFDGKSIEEYSEPEL 79
Cdd:COG0410 1 MPMLEVENLHAGY--GGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARirnEKIGFVFQAFNLLARSSVYENVRLPLFYSNvpetaWDSKIKSAIDAVgishrivHE--P----------GELSGG 147
Cdd:COG0410 76 AR---LGIGYVPEGRRIFPSLTVEENLLLGAYARR-----DRAEVRADLERV-------YElfPrlkerrrqraGTLSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818736213 148 EKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRkTGRTIILI 200
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLV 192
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-202 |
9.30e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.11 E-value: 9.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsGEskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeysePELARIR 83
Cdd:PRK13537 8 IDFRNVEKRY--GD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-----PSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH 202
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTH 196
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
9.69e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 99.43 E-value: 9.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKS-TLLQLLGFLD---RQTGGSYKFDGKSIEEYSE 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 77 PELARIRNEKIGFVFQ------------AFNLLARSSVYE--NVRlplfysnvpetawdSKIKSAID---AVGI---SHR 136
Cdd:PRK11022 81 KERRNLVGAEVAMIFQdpmtslnpcytvGFQIMEAIKVHQggNKK--------------TRRQRAIDllnQVGIpdpASR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 137 IVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESL-AKYARRLIR 215
Cdd:PRK11022 147 LDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIV 226
|
....*.
gi 818736213 216 MKDGKI 221
Cdd:PRK11022 227 MYAGQV 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-202 |
3.48e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 97.73 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQ------SGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSE 76
Cdd:PRK11308 5 LLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 77 PELARIRnEKIGFVFQafN----LLARSSVYENVRLPLFYsNVPETAWD--SKIKSAIDAVGIshRIVHE---PGELSGG 147
Cdd:PRK11308 85 EAQKLLR-QKIQIVFQ--NpygsLNPRKKVGQILEEPLLI-NTSLSAAErrEKALAMMAKVGL--RPEHYdryPHMFSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 148 EKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH 202
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISH 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-203 |
4.42e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.39 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 21 VALDGVSFLVDKGEFIAIMGPSGSGKSTL-LQLLGFLDRQtgGSYKFDGKSIEEYSEPELARIRNeKIGFVFQAFN--LL 97
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLINSQ--GEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPNssLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 98 ARSSVYENVR--LPLFYSNVPETAWDSKIKSAIDAVGISHRIVHE-PGELSGGEKQRVAIARSFVLDPEMILADEPTGNL 174
Cdd:PRK15134 377 PRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180
....*....|....*....|....*....
gi 818736213 175 DSKNGEMIIKLLDELNRKTGRTIILITHE 203
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-202 |
4.70e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 6 VKNLEKVYqsgESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGsykfdgksieeysepELARIRNE 85
Cdd:COG0488 1 LENLSKSF---GGRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG---------------EVSIPKGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 86 KIGFVFQAFNLLARSSVYENV------------RLPLFYSNVPET------------------AW--DSKIKSAIDAVGI 133
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVldgdaelraleaELEELEAKLAEPdedlerlaelqeefealgGWeaEARAEEILSGLGF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 134 SHRIVHEP-GELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSkngEMIIKLLDELNRKTGrTIILITH 202
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNYPG-TVLVVSH 207
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-221 |
5.78e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 95.68 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQtgGSYKFDGKSIEEYSEPELARIR-----NEKIGFVFQAFNL 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLLPGQ--GEILLNGRPLSDWSAAELARHRaylsqQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 97 LArssvyenvrlpLFY-SNVPETAWDSKIKSAIDAVGIS---HRIVHepgELSGGEKQRVAIARSFV-----LDPE--MI 165
Cdd:COG4138 90 LA-----------LHQpAGASSEAVEQLLAQLAEALGLEdklSRPLT---QLSGGEWQRVRLAAVLLqvwptINPEgqLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 166 LADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTlRHADRVWLLKQGKL 211
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-213 |
5.90e-24 |
|
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: 94.35 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLekVYQSGEskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeysePELARIR 83
Cdd:TIGR01189 1 LAARNL--ACSRGE--RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARSSVYENVRlplFYSNVPETAwDSKIKSAIDAVG---ISHRIVHepgELSGGEKQRVAIARSFVL 160
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSALENLH---FWAAIHGGA-QRTIEDALAAVGltgFEDLPAA---QLSAGQQRRLALARLWLS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDElNRKTGRTIILITHEESLAKYARRL 213
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLRA-HLARGGIVLLTTHQDLGLVEAREL 196
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-201 |
5.99e-24 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 95.42 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 6 VKNLEKVYQSgesKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIrne 85
Cdd:TIGR04406 4 AENLIKSYKK---RKV-VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 86 KIGFVFQAFNLLARSSVYENVRLPL-FYSNVPETAWDSKIKSAIDAVGISHrIVHEPG-ELSGGEKQRVAIARSFVLDPE 163
Cdd:TIGR04406 77 GIGYLPQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISH-LRDNKAmSLSGGERRRVEIARALATNPK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 818736213 164 MILADEPTGNLDS---KNGEMIIKLLDElnRKTGrtiILIT 201
Cdd:TIGR04406 156 FILLDEPFAGVDPiavGDIKKIIKHLKE--RGIG---VLIT 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-221 |
1.10e-23 |
|
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: 93.75 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLekvYQSGESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLD-RQTGGSYKFDGKSIEEYSEPELAR 81
Cdd:cd03217 1 LEIKDL---HVSVGGKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 irnEKIGFVFQafnllaRSSVYENVRLPLFYSNVPETawdskiksaidavgishrivhepgeLSGGEKQRVAIARSFVLD 161
Cdd:cd03217 77 ---LGIFLAFQ------YPPEIPGVKNADFLRYVNEG-------------------------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 162 PEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYAR--RLIRMKDGKI 221
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIKpdRVHVLYDGRI 183
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-221 |
1.10e-23 |
|
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: 94.86 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 21 VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirneKIGFVFQAfNLLARS 100
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR----QVGVVLQE-NVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 101 SVYENVRLPLFYSNVPETAWDSKIKSAIDAV-----GIShRIVHEPGE-LSGGEKQRVAIARSFVLDPEMILADEPTGNL 174
Cdd:cd03252 91 SIRDNIALADPGMSMERVIEAAKLAGAHDFIselpeGYD-TIVGEQGAgLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 818736213 175 DSKNGEMIIKLLDELNrkTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:cd03252 170 DYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-221 |
1.14e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 5 EVKNLEKVYQSGESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSI---EEYSEPELAR 81
Cdd:PRK14246 9 DVFNISRLYLYINDKAI-LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRNEkIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKI-KSAIDAVG----ISHRIVHEPGELSGGEKQRVAIAR 156
Cdd:PRK14246 88 LRKE-VGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIvEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 157 SFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTgrTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNpQQVARVADYVAFLYNGEL 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-221 |
1.19e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 95.15 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 24 DGVSFLVDKGEFIAIMGPSGSGKS-TLLQLLGFLD---RQTGGSYKFDGKSIEeysepeLARIRNEKIGFVFQ----AFN 95
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVA------PCALRGRKIATIMQnprsAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 96 LL--ARSSVYENVRLplfysnVPETAWDSKIKSAIDAVGIS--HRIVH-EPGELSGGEKQRVAIARSFVLDPEMILADEP 170
Cdd:PRK10418 94 PLhtMHTHARETCLA------LGKPADDATLTAALEAVGLEnaARVLKlYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 818736213 171 TGNLDSKNGEMIIKLLDELNRKTGRTIILITHEES-LAKYARRLIRMKDGKI 221
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGRI 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-221 |
1.38e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.92 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVY-----QSGESKTV------------ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYK 65
Cdd:COG4586 2 IEVENLSKTYrvyekEPGLKGALkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 66 FDGKSIEEySEPELARirneKIGFVF-------------QAFNLLARssVYEnvrlplfysnVPETAWDSKIKSAIDAVG 132
Cdd:COG4586 81 VLGYVPFK-RRKEFAR----RIGVVFgqrsqlwwdlpaiDSFRLLKA--IYR----------IPDAEYKKRLDELVELLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 133 ISHrIVHEP-GELSGGEKQRVAIARSFVLDPEMILADEPTGNLD--SKngEMIIKLLDELNRKTGRTIILITHE----ES 205
Cdd:COG4586 144 LGE-LLDTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvSK--EAIREFLKEYNRERGTTILLTSHDmddiEA 220
|
250
....*....|....*.
gi 818736213 206 LAKyarRLIRMKDGKI 221
Cdd:COG4586 221 LCD---RVIVIDHGRI 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-202 |
1.42e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.84 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFL-----DRQTGGSYKFDGKSIeeYS-E 76
Cdd:PRK14239 5 ILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI--YSpR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 77 PELARIRNEkIGFVFQAFNLLARSsVYENVRLPLFYSNVPETA-WDSKIKSAIDAVGISHRI---VHEPG-ELSGGEKQR 151
Cdd:PRK14239 79 TDTVDLRKE-IGMVFQQPNPFPMS-IYENVVYGLRLKGIKDKQvLDEAVEKSLKGASIWDEVkdrLHDSAlGLSGGQQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLdeLNRKTGRTIILITH 202
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTR 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
2.50e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLekVYQSGEskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELA 80
Cdd:PRK09536 1 MPMIDVSDL--SVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 RirneKIGFVFQ----AFNLLARSSVyENVRLPLFYSNVPETAWDSK-IKSAIDAVGISHRIVHEPGELSGGEKQRVAIA 155
Cdd:PRK09536 77 R----RVASVPQdtslSFEFDVRQVV-EMGRTPHRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 156 RSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESL-AKYARRLIRMKDGKI 221
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLaARYCDELVLLADGRV 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-223 |
4.17e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.42 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGES-KTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELAR 81
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRNEKIGFVFQafnlLARSSVYENVRL------PLFYSNVPETAwdSKIKS-AIDAVGISHRIVHE-PGELSGGEKQRVA 153
Cdd:PRK13643 81 PVRKKVGVVFQ----FPESQLFEETVLkdvafgPQNFGIPKEKA--EKIAAeKLEMVGLADEFWEKsPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 154 IARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNrKTGRTIILITH-EESLAKYARRLIRMKDGKIES 223
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHlMDDVADYADYVYLLEKGHIIS 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-202 |
4.76e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.56 E-value: 4.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTG-----GSYKFDGKSIEEySEPE 78
Cdd:PRK14258 8 IKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE-RRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 79 LARIRNEkIGFVFQAFNLLARSsVYENVRLPL-FYSNVPETAWDSKIKSAIDAVG----ISHRIVHEPGELSGGEKQRVA 153
Cdd:PRK14258 83 LNRLRRQ-VSMVHPKPNLFPMS-VYDNVAYGVkIVGWRPKLEIDDIVESALKDADlwdeIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 818736213 154 IARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH 202
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSH 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-226 |
5.41e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.23 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSG-ESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARI 82
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rnekIGFVFQ------AFNLlarsSVYENV--------RLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGE 148
Cdd:COG1101 82 ----IGRVFQdpmmgtAPSM----TIEENLalayrrgkRRGLRRGLTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 149 KQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITH--EESLaKYARRLIRMKDGKIESDIR 226
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmEQAL-DYGNRLIMMHEGRIILDVS 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-205 |
5.71e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 96.65 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDR---QTGGSYKFDGKSIEEysePELARIRnekiGFVFQaFNLLAR 99
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDA---KEMRAIS----AYVQQ-DDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 100 S-SVYEN------VRLPlfySNVPETAWDSKIKSAIDAVGIS---HRIVHEPGE---LSGGEKQRVAIARSFVLDPEMIL 166
Cdd:TIGR00955 113 TlTVREHlmfqahLRMP---RRVTKKEKRERVDEVLQALGLRkcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 818736213 167 ADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEES 205
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPS 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-202 |
9.26e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.48 E-value: 9.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYKFDGKSIeeysepelaR 81
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILyGLY-QPDSGEILIDGKPV---------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRNEK------IGFVFQAFNLLARSSVYENVRL---PLFYSNVPETAWDSKIKSAIDAVGIS---HRIVHepgELSGGEK 149
Cdd:COG3845 71 IRSPRdaialgIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDvdpDAKVE---DLSVGEQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 818736213 150 QRVAIARSFVLDPE-MILaDEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH 202
Cdd:COG3845 148 QRVEILKALYRGARiLIL-DEPTAVLTPQEADELFEILRRL-AAEGKSIIFITH 199
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-206 |
1.07e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirnekIGFV--FQAFNLLAR 99
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-----MGVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 100 SSVYEN--------VRLPLFYSNVPETAWDSKIKSAI-------DAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEM 164
Cdd:PRK11300 95 MTVIENllvaqhqqLKTGLFSGLLKTPAFRRAESEALdraatwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 818736213 165 ILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESL 206
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-221 |
1.24e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.86 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 19 KTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYsepELARIRNEKIGFVFQAFNLLA 98
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 99 RSSVYENVRLPLFYSNvpETAWDSKIKSAIDAVG-ISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSK 177
Cdd:PRK11614 94 RMTVEENLAMGGFFAE--RDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 818736213 178 NGEMIIKLLDELnRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:PRK11614 172 IIQQIFDTIEQL-REQGMTIFLVEQNANQAlKLADRGYVLENGHV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-221 |
3.22e-22 |
|
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: 90.03 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKsieeysePELARIR 83
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-------PLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NeKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03269 70 N-RIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQmELVEELCDRVLLLNKGRA 206
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-221 |
4.31e-22 |
|
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: 90.28 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 5 EVKNLEKVYqsGESktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirn 84
Cdd:TIGR03410 2 EVSNLNVYY--GQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 85 EKIGFVFQAFNLLARSSVYENVRLPLFYS-----NVPETAWD--SKIKSAIDAVGishrivhepGELSGGEKQRVAIARS 157
Cdd:TIGR03410 75 AGIAYVPQGREIFPRLTVEENLLTGLAALprrsrKIPDEIYElfPVLKEMLGRRG---------GDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 158 FVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAK-YARRLIRMKDGKI 221
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFAReLADRYYVMERGRV 210
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-221 |
8.13e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.23 E-value: 8.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKV--YQSG--ESKTV-ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIE--EY 74
Cdd:PRK15112 3 TLLEVRNLSKTfrYRTGwfRRQTVeAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 75 SepelarIRNEKIGFVFQ--AFNLLARSSVYENVRLPL-FYSNVPETAWDSKIKSAIDAVGI-SHRIVHEPGELSGGEKQ 150
Cdd:PRK15112 83 S------YRSQRIRMIFQdpSTSLNPRQRISQILDFPLrLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 151 RVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKY-ARRLIRMKDGKI 221
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEV 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-202 |
1.09e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLiEVKNLeKVYQSGEsktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELA 80
Cdd:PRK13539 1 MML-EGEDL-ACVRGGR---VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 RIRNEKigfvfqafNLLARS-SVYENVRlplFYSNVPETAwDSKIKSAIDAVGISHrIVHEP-GELSGGEKQRVAIARSF 158
Cdd:PRK13539 76 HYLGHR--------NAMKPAlTVAENLE---FWAAFLGGE-ELDIAAALEAVGLAP-LAHLPfGYLSAGQKRRVALARLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 818736213 159 VLDPEMILADEPTGNLDSKNGEMIIKLLDElNRKTGRTIILITH 202
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATH 185
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
1.66e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.68 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTV-ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGS---------YKFDGKSIE 72
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiqvgdiyigDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 73 EYSEPElaRIRNEK-----IGFVFQ--AFNLLaRSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVH-EPGEL 144
Cdd:PRK13631 101 TNPYSK--KIKNFKelrrrVSMVFQfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLErSPFGL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 145 SGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDElNRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-219 |
1.90e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.18 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLqllgfldRQTGGsykfdgksIEEYSEPELARIRNEKIGFVFQafnllaRSsv 102
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLL-------RAIAG--------LWPYGSGRIARPAGARVLFLPQ------RP-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 103 YenvrLP-------LFYSNVPETAWDSKIKSAIDAVGISHRI--VHEPG----ELSGGEKQRVAIARSFVLDPEMILADE 169
Cdd:COG4178 436 Y----LPlgtlreaLLYPATAEAFSDAELREALEAVGLGHLAerLDEEAdwdqVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 818736213 170 PTGNLDSKNGEMIIKLLDELNRKTgrTIILITHEESLAKYARRLIRMKDG 219
Cdd:COG4178 512 ATSALDEENEAALYQLLREELPGT--TVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-221 |
1.92e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 87.49 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 5 EVKNLekvyqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSepeLARIRN 84
Cdd:cd03215 6 EVRGL--------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS---PRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 85 EKIGFV---FQAFNLLARSSVYENVRLPLFysnvpetawdskiksaidavgishrivhepgeLSGGEKQRVAIARSFVLD 161
Cdd:cd03215 75 AGIAYVpedRKREGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 162 PEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-216 |
2.37e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 90.35 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRQ---TGGSYKFDGKSIEEYSE 76
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKDNwhvTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 77 PELARIRNEKIGFVFQAfnllARSSVYENVRL-PLFYSNVPETA--------WDSKIKSAID---AVGI-SHRIVHE--P 141
Cdd:COG4170 81 RERRKIIGREIAMIFQE----PSSCLDPSAKIgDQLIEAIPSWTfkgkwwqrFKWRKKRAIEllhRVGIkDHKDIMNsyP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 142 GELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRLIRM 216
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADTITVL 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-221 |
2.64e-21 |
|
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: 91.72 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQTGgSYKFDGKSIEEYSEPELARIrnekIGFVFQAFNLLArS 100
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLvGFFQARSG-EILLNGFSLKDIDRHTLRQF----INYLPQEPYIFS-G 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 101 SVYENvrlpLFYSNVPETAWDsKIKSAIDAV-----------GISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADE 169
Cdd:TIGR01193 563 SILEN----LLLGAKENVSQD-EIWAACEIAeikddienmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 818736213 170 PTGNLDSKNGEMIIKLLDELNRKtgrTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-202 |
5.26e-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: 87.45 E-value: 5.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQsgesKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKsieEYSEPELarir 83
Cdd:TIGR03740 1 LETKNLSKRFG----KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH---PWTRKDL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPetawDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:TIGR03740 70 -HKIGSLIESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITH 202
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSH 182
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-170 |
8.76e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.01 E-value: 8.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSgesKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLdRQTGGSYKFDGKSIEEYSEPEL 79
Cdd:COG1137 1 MMTLEAENLVKSYGK---RTV-VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIvGLV-KPDSGRIFLDGEDITHLPMHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARirnEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHrIVHEPG-ELSGGEKQRVAIARSF 158
Cdd:COG1137 76 AR---LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITH-LRKSKAySLSGGERRRVEIARAL 151
|
170
....*....|..
gi 818736213 159 VLDPEMILADEP 170
Cdd:COG1137 152 ATNPKFILLDEP 163
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-202 |
2.76e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 86.37 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDR-----QTGGSYKFDGKSIEEySEP 77
Cdd:PRK14243 10 VLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA-PDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 78 ELARIRnEKIGFVFQAFNLLARSsVYENV----RLPLFYSNVPETA---------WDsKIKSAIDAVGIShrivhepgeL 144
Cdd:PRK14243 85 DPVEVR-RRIGMVFQKPNPFPKS-IYDNIaygaRINGYKGDMDELVerslrqaalWD-EVKDKLKQSGLS---------L 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 145 SGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTgrTIILITH 202
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTH 208
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-221 |
2.82e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.54 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLG-FLDRQTGgSYKFDGKSIEEYsepELARI 82
Cdd:PRK11176 342 IEFRNVTFTYPGKE--VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrFYDIDEG-EILLDGHDLRDY---TLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEkIGFVFQAFNLLaRSSVYENVRLPL--FYS-----NVPETAWD----SKIKSAIDAV----GIShrivhepgeLSGG 147
Cdd:PRK11176 416 RNQ-VALVSQNVHLF-NDTIANNIAYARteQYSreqieEAARMAYAmdfiNKMDNGLDTVigenGVL---------LSGG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 148 EKQRVAIARSFVLD-PEMILaDEPTGNLDSKNGEMIIKLLDELnrKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK11176 485 QRQRIAIARALLRDsPILIL-DEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-220 |
3.02e-20 |
|
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: 83.27 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGfldrqtggsykfdGKSIEEysEPELARIR 83
Cdd:cd03221 1 IELENLSKTY---GGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIA-------------GELEPD--EGIVTWGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQafnllarssvyenvrlplfysnvpetawdskiksaidavgishrivhepgeLSGGEKQRVAIARSFVLDPE 163
Cdd:cd03221 62 TVKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 164 MILADEPTGNLDSkngEMIIKLLDELNRKTGrTIILITHEES-LAKYARRLIRMKDGK 220
Cdd:cd03221 91 LLLLDEPTNHLDL---ESIEALEEALKEYPG-TVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-221 |
4.29e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.37 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIRNEkIGFVFQA--FNLLAR 99
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 100 SSVYENVRLPLFYSNV-PETAWDSKIKSAIDAVGI-SHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSK 177
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 818736213 178 NGEMIIKLLDELNRKTGRTIILITHEESLA-KYARRLIRMKDGKI 221
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVeRISHRVAVMYLGQI 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-219 |
4.64e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKsieEYSEPELAR 81
Cdd:PRK09700 4 PYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI---NYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 IRNEKIGFVFQAFNLLARSSVYENV---RLPLF-YSNVPETAWDS-KIKSAI--DAVGISHRIVHEPGELSGGEKQRVAI 154
Cdd:PRK09700 77 AAQLGIGIIYQELSVIDELTVLENLyigRHLTKkVCGVNIIDWREmRVRAAMmlLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 155 ARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHE-ESLAKYARRLIRMKDG 219
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-216 |
5.61e-20 |
|
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: 84.08 E-value: 5.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 21 VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEySEPELARirneKIGFVFQAFNLLARS 100
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIAR----GLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 101 SVYENVRlplFYSNVPEtawDSKIKSAIDAVGIS---HRIVHepgELSGGEKQRVAIARSFVLDPEMILADEPTGNLDsK 177
Cdd:cd03231 89 SVLENLR---FWHADHS---DEQVEEALARVGLNgfeDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALD-K 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 818736213 178 NGEMIIKLLDELNRKTGRTIILITHEE-SLAKYARRLIRM 216
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQDlGLSEAGARELDL 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-224 |
8.44e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 84.12 E-value: 8.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKT------------------VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYK 65
Cdd:cd03220 1 IELENVSKSYPTYKGGSsslkklgilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 66 FDGK--SIEEYS---EPELarirnekigfvfqafnllarsSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIvHE 140
Cdd:cd03220 81 VRGRvsSLLGLGggfNPEL---------------------TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-DL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 141 P-GELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH-EESLAKYARRLIRMKD 218
Cdd:cd03220 139 PvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHdPSSIKRLCDRALVLEK 217
|
....*.
gi 818736213 219 GKIESD 224
Cdd:cd03220 218 GKIRFD 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-220 |
1.16e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKS-TLLQLLGFLDrQTGGSYKFDGK----------SI 71
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLE-QAGGLVQCDKMllrrrsrqviEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 72 EEYSEPELARIRNEKIGFVFQ----AFN--LLARSSVYENVRLplfYSNVPETAWDSKIKSAIDAVGI--SHRIVHE-PG 142
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQepmtSLNpvFTVGEQIAESIRL---HQGASREEAMVEAKRMLDQVRIpeAQTILSRyPH 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 143 ELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEES-LAKYARRLIRMKDGK 220
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGE 246
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-202 |
1.71e-19 |
|
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: 86.61 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 6 VKNLEKVYQSgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEysepELARIRnE 85
Cdd:TIGR01257 931 VKNLVKIFEP--SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVR-Q 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 86 KIGFVFQAFNLLARSSVYENVrlpLFYSNVPETAWDS---KIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHI---LFYAQLKGRSWEEaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLdeLNRKTGRTIILITH 202
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTH 1118
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-222 |
1.85e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKVYqsgESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFdGKSIeeysepelar 81
Cdd:COG0488 314 KVLELEGLSKSY---GDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 irneKIGFVFQAFNLL-ARSSVYENVRlplfysnvpETAWDSKIKSAIDAVG---ISHRIVHEP-GELSGGEKQRVAIAR 156
Cdd:COG0488 379 ----KIGYFDQHQEELdPDKTVLDELR---------DGAPGGTEQEVRGYLGrflFSGDDAFKPvGVLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 157 SFVLDPEMILADEPTGNLDSkngEMIIKLLDELNRKTGrTIILITHEES-LAKYARRLIRMKDGKIE 222
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDI---ETLEALEEALDDFPG-TVLLVSHDRYfLDRVATRILEFEDGGVR 508
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-202 |
2.66e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.88 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeysePELARIR 83
Cdd:PRK13536 42 IDLAGVSKSYGD----KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-----PARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAFNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITH 202
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTH 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-221 |
2.67e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.62 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSGESKTV-ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQTGGSYKFDGKSIEEYSEP-EL 79
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIaGVLEPTSGEVNVRVGDEWVDMTKPgPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIRNEK-IGFVFQAFNLLARSSVYENVRLPLFYsNVPETAWDSKIKSAIDAVGISHRIVHE-----PGELSGGEKQRVA 153
Cdd:TIGR03269 359 GRGRAKRyIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 154 IARSFVLDPEMILADEPTGNLDS----KNGEMIIKLLDELNrktgRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEME----QTFIIVSHDmDFVLDVCDRAALMRDGKI 506
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-202 |
1.18e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.46 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDrQTGGSYKFDGKSIEeysepelARI 82
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILA-PDSGEVLWDGEPLD-------PED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNeKIGFVFQAFNLLARSSVYENV----RLplfySNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSF 158
Cdd:COG4152 70 RR-RIGYLPEERGLYPKMKVGEQLvylaRL----KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 818736213 159 VLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITH 202
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSH 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-220 |
2.22e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 19 KTVALDG----VSFLVDKGEFIAIMGPSGSGKSTLL-QLLGFLDRQtgGSYKFDGKSIEEYSEPELARIRnekiGFVFQA 93
Cdd:PRK03695 4 NDVAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLaRMAGLLPGS--GSIQFAGQPLEAWSAAELARHR----AYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 94 FNLLARSSVYENVRLPLfYSNVPETAWDSKIKSAIDAVGIS---HRIVhepGELSGGEKQRVAIARSF-----VLDPE-- 163
Cdd:PRK03695 78 QTPPFAMPVFQYLTLHQ-PDKTRTEAVASALNEVAEALGLDdklGRSV---NQLSGGEWQRVRLAAVVlqvwpDINPAgq 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 164 MILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHE--ESLaKYARRLIRMKDGK 220
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDlnHTL-RHADRVWLLKQGK 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-224 |
3.35e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKVYQSGESKT------------------VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGS 63
Cdd:COG1134 3 SMIEVENVSKSYRLYHEPSrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 64 YKFDGK--SIEEYS---EPELarirnekigfvfqafnllarsSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIv 138
Cdd:COG1134 83 VEVNGRvsALLELGagfHPEL---------------------TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFI- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 139 HEP-GELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH-EESLAKYARRLIRM 216
Cdd:COG1134 141 DQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHsMGAVRRLCDRAIWL 219
|
....*...
gi 818736213 217 KDGKIESD 224
Cdd:COG1134 220 EKGRLVMD 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-221 |
3.67e-18 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 79.46 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRqTGGSYKFDGKSIEEYSepeLARI 82
Cdd:cd03244 3 IEFKNVSLRYRPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLaLFRLVEL-SSGSILIDGVDISKIG---LHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAfNLLARSSVYENVRlplfysnvPETAW-DSKIKSAIDAVGISHRIVHEPGEL-----------SGGEKQ 150
Cdd:cd03244 77 R-SRISIIPQD-PVLFSGTIRSNLD--------PFGEYsDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 151 RVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDElnRKTGRTIILITHE-ESLAKYARRLIrMKDGKI 221
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRlDTIIDSDRILV-LDKGRV 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-221 |
3.75e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 20 TVALDGVSFLV-------------DKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirneK 86
Cdd:PRK10575 11 TFALRNVSFRVpgrtllhplsltfPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 87 IGFVFQAFNLLARSSVYENV---RLPLFYSNVPETAWD-SKIKSAIDAVGI---SHRIVHEpgeLSGGEKQRVAIARSFV 159
Cdd:PRK10575 87 VAYLPQQLPAAEGMTVRELVaigRYPWHGALGRFGAADrEKVEEAISLVGLkplAHRLVDS---LSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESL-AKYARRLIRMKDGKI 221
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGEM 226
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
23-221 |
3.85e-18 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 80.00 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLD-RQTGGSYKFDGKSIEEYSEPELARIRnekigfVFQAF------ 94
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKtIAGHPSyEVTSGTILFKGQDLLELEPDERARAG------LFLAFqypeei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 95 ----NLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGIS----HRIVHEpgELSGGEKQRVAIARSFVLDPEMIL 166
Cdd:TIGR01978 90 pgvsNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDeeflNRSVNE--GFSGGEKKRNEILQMALLEPKLAI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 167 ADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYAR--RLIRMKDGKI 221
Cdd:TIGR01978 168 LDEIDSGLDIDALKIVAEGINRL-REPDRSFLIITHYQRLLNYIKpdYVHVLLDGRI 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-221 |
5.63e-18 |
|
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: 78.99 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKtvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRQTgGSYKFDGKSIeeySEPELARI 82
Cdd:cd03369 7 IEVENLSVRYAPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILaLFRFLEAEE-GKIEIDGIDI---STIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNeKIGFVFQAFNLLArSSVYENVRLPLFYSnvpetawDSKIKSAIDavgishriVHEPGE-LSGGEKQRVAIARSFVLD 161
Cdd:cd03369 81 RS-SLTIIPQDPTLFS-GTIRSNLDPFDEYS-------DEEIYGALR--------VSEGGLnLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 162 PEMILADEPTGNLDSKNGEMIIKLLDELNrkTGRTIILITHE-ESLAKYARRLIrMKDGKI 221
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEF--TNSTILTIAHRlRTIIDYDKILV-MDAGEV 201
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-213 |
6.15e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 81.00 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLD----RQTGGSYKFDGKSIEEYSE 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 77 PELARIRNEKIGFVFQAFNLLARSSvyENVRLPLFySNVPetAWDSK----------IKSAID---AVGI-SHR-IVHE- 140
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPS--ERVGRQLM-QNIP--GWTYKgrwwqrfgwrKRRAIEllhRVGIkDHKdAMRSf 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 141 PGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHE-ESLAKYARRL 213
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADKI 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-211 |
6.89e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.14 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 19 KTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFL-DRQTGGSYKFD----GKSIEEYSEPELARIRnekIGFVFQA 93
Cdd:PRK14271 34 KTV-LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGYRYSGDvllgGRSIFNYRDVLEFRRR---VGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 94 FNLLARS---SVYENVRLplfYSNVPETAWDSKIKSAIDAVG----ISHRIVHEPGELSGGEKQRVAIARSFVLDPEMIL 166
Cdd:PRK14271 110 PNPFPMSimdNVLAGVRA---HKLVPRKEFRGVAQARLTEVGlwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 818736213 167 ADEPTGNLDSKNGEMIIKLLDELNRKTgrTIILITHeeSLAKYAR 211
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTH--NLAQAAR 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-221 |
1.17e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.14 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLekvyqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEeYSEPElARI 82
Cdd:COG1129 256 VLEVEGL--------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-IRSPR-DAI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNeKIGFV---FQAFNLLARSSVYENVRLPLF--YSN---VPETAWDSKIKSAIDAVGISHRIVHEP-GELSGGEKQRVA 153
Cdd:COG1129 326 RA-GIAYVpedRKGEGLVLDLSIRENITLASLdrLSRgglLDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 154 IARSFVLDPEMILADEPTGNLD--SKNGemIIKLLDELNRKtGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDvgAKAE--IYRLIRELAAE-GKAVIVISSElPELLGLSDRILVMREGRI 472
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-202 |
1.29e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRQTGgsykfdgkSIEEYSEPELARI 82
Cdd:PRK15056 7 IVVNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKaLMGFVRLASG--------KISILGQPTRQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKIGFVFQA------FNLLARSSVYENVRLPLFYSNVPeTAWDSKIKSA----IDAVGISHRIVhepGELSGGEKQRV 152
Cdd:PRK15056 76 QKNLVAYVPQSeevdwsFPVLVEDVVMMGRYGHMGWLRRA-KKRDRQIVTAalarVDMVEFRHRQI---GELSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 818736213 153 AIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH 202
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTH 200
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-221 |
1.75e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.83 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLekvyQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQ-TGGSYKFDGKSI-----EEY 74
Cdd:CHL00131 6 PILEIKNL----HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaGHPAYKiLEGDILFKGESIldlepEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 75 SE---------P-ELARIRNEKigFVFQAFNllARSSVYENVRL-PLFYSNVpetawdskIKSAIDAVGIS----HRIVH 139
Cdd:CHL00131 82 AHlgiflafqyPiEIPGVSNAD--FLRLAYN--SKRKFQGLPELdPLEFLEI--------INEKLKLVGMDpsflSRNVN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 140 EpgELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYarrlIR---- 215
Cdd:CHL00131 150 E--GFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQRLLDY----IKpdyv 222
|
....*...
gi 818736213 216 --MKDGKI 221
Cdd:CHL00131 223 hvMQNGKI 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-205 |
2.01e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.61 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 17 ESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGflDRQTGGSykFDGKSIEEYSEPELARIRneKIGFVFQAFNL 96
Cdd:PLN03211 79 QERTI-LNGVTGMASPGEILAVLGPSGSGKSTLLNALA--GRIQGNN--FTGTILANNRKPTKQILK--RTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 97 LARSSVYEN------VRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEP--GELSGGEKQRVAIARSFVLDPEMILAD 168
Cdd:PLN03211 152 YPHLTVRETlvfcslLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 818736213 169 EPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEES 205
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPS 267
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-218 |
2.17e-16 |
|
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: 73.73 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEkvYQSGESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLqllgfldRQTGGSYKFDGKSIEeysepelaRIR 83
Cdd:cd03223 1 IELENLS--LATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLF-------RALAGLWPWGSGRIG--------MPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAfNLLARSSVYENVRLPlfysnvpetaWDSkiksaidavgishrivhepgELSGGEKQRVAIARSFVLDPE 163
Cdd:cd03223 63 GEDLLFLPQR-PYLPLGTLREQLIYP----------WDD--------------------VLSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 164 MILADEPTGNLDsknGEMIIKLLDELNRKtGRTIILITHEESLAKYARRLIRMKD 218
Cdd:cd03223 112 FVFLDEATSALD---EESEDRLYQLLKEL-GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-202 |
2.36e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.26 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGksiEEYSEPELARIRNEKIGFVFQAFNLLARSS 101
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTAALAAGVAIIYQELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 102 VYENV---RLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKN 178
Cdd:PRK11288 96 VAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
|
170 180
....*....|....*....|....
gi 818736213 179 GEMIIKLLDELnRKTGRTIILITH 202
Cdd:PRK11288 176 IEQLFRVIREL-RAEGRVILYVSH 198
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-205 |
2.59e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.07 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQTGGSYkFDGKSIEEYSEPELari 82
Cdd:PRK10790 341 IDIDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLmGYYPLTEGEIR-LDGRPLSSLSHSVL--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNeKIGFVFQAFNLLArSSVYENVRLPLFYSNvpETAWDskiksAIDAV-----------GISHRIVHEPGELSGGEKQR 151
Cdd:PRK10790 414 RQ-GVAMVQQDPVVLA-DTFLANVTLGRDISE--EQVWQ-----ALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTgrTIILITHEES 205
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLS 536
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-223 |
4.19e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 37 AIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSE-----PELARIrnekiGFVFQAFNLLARSSVYENVRlplf 111
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiclpPEKRRI-----GYVFQDARLFPHYKVRGNLR---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 112 YSNVPETawDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNR 191
Cdd:PRK11144 99 YGMAKSM--VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176
|
170 180 190
....*....|....*....|....*....|....
gi 818736213 192 KTGRTIILITH--EESLaKYARRLIRMKDGKIES 223
Cdd:PRK11144 177 EINIPILYVSHslDEIL-RLADRVVVLEQGKVKA 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-221 |
9.37e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEkvyQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSePelARI 82
Cdd:COG3845 257 VLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS-P--RER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEKIGFV---FQAFNLLARSSVYENVRLPLFYSN-------VPETAWDSKIKSAIDAVGISHRIVHEP-GELSGGEKQR 151
Cdd:COG3845 331 RRLGVAYIpedRLGRGLVPDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 152 VAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDlDEILALSDRIAVMYEGRI 480
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-219 |
1.04e-15 |
|
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: 72.28 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 7 KNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGflDRQTGGSYK----FDGKSIEEysepELARI 82
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVITgeilINGRPLDK----NFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rnekIGFVFQAFNLLARSSVYEnvrlPLFYSnvpetAWDSkiksaidavgishrivhepgELSGGEKQRVAIARSFVLDP 162
Cdd:cd03232 81 ----TGYVEQQDVHSPNLTVRE----ALRFS-----ALLR--------------------GLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRkTGRTIILITHEES--LAKYARRLIRMKDG 219
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-204 |
2.03e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 24 DGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeysepelARIRNEkigfvFQAfNLL------ 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--------RRQRDE-----YHQ-DLLylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 98 ---ARSSVYENVRlplFYSNVPETAWDSKIKSAIDAVGISHRiVHEP-GELSGGEKQRVAIARSFVLDPEMILADEPTGN 173
Cdd:PRK13538 84 gikTELTALENLR---FYQRLHGPGDDEALWEALAQVGLAGF-EDVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190
....*....|....*....|....*....|..
gi 818736213 174 LDSKNGEMIIKLLDE-LNRktGRTIILITHEE 204
Cdd:PRK13538 160 IDKQGVARLEALLAQhAEQ--GGMVILTTHQD 189
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-214 |
2.68e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSgesKTVALDgVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELA 80
Cdd:PRK10895 1 MATLTAKNLAKAYKG---RRVVED-VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 RirnEKIGFVFQAFNLLARSSVYENVRLPL-FYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFV 159
Cdd:PRK10895 77 R---RGIGYLPQEASIFRRLSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 160 LDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH--EESLAKYARRLI 214
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHnvRETLAVCERAYI 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-221 |
6.28e-15 |
|
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: 73.44 E-value: 6.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTvaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRQTGgsyKFDGKSIEEYSePELARI 82
Cdd:TIGR00957 637 ITVHNATFTWARDLPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEG---HVHMKGSVAYV-PQQAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEkigfvfqafnllarsSVYENVRL-----PLFYSNVPETAW---DSKIKSAIDAVGISHRIVHepgeLSGGEKQRVAI 154
Cdd:TIGR00957 711 QND---------------SLRENILFgkalnEKYYQQVLEACAllpDLEILPSGDRTEIGEKGVN----LSGGQKQRVSL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 155 ARSFVLDPEMILADEPTGNLDSKNGEMII-KLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-220 |
6.35e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.22 E-value: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 19 KTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGflDRQTGGSYKFD-----GKSIEEysepELARIrnekIGFVFQA 93
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGdrlvnGRPLDS----SFQRS----IGYVQQQ 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 94 FNLLARSSVYENVRLPLFY---SNVPETAWDSKIKSAIDAVGI---SHRIVHEPGE-LSGGEKQRVAIARSFVLDPEMIL 166
Cdd:TIGR00956 845 DLHLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMesyADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLL 924
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 167 -ADEPTGNLDSKNGEMIIKLLDELNrKTGRTIILITHEES---LAKYARRLIRMKDGK 220
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSailFEEFDRLLLLQKGGQ 981
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-202 |
1.50e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeEYSEPelaRIRNEK-IGFVFQAFNLLARS 100
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGP---KSSQEAgIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 101 SVYENVrlplFYSNVPETAWDS----KIKSAIDA----VGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTG 172
Cdd:PRK10762 95 TIAENI----FLGREFVNRFGRidwkKMYAEADKllarLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190
....*....|....*....|....*....|
gi 818736213 173 NLDSKNGEMIIKLLDELnRKTGRTIILITH 202
Cdd:PRK10762 171 ALTDTETESLFRVIREL-KSQGRGIVYISH 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-214 |
2.04e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.98 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTVALDgVSFLVDKGEFIAIMGPSGSGKSTLLQLLG------------FLDRQTGGSYKFDG--- 68
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivFKNEHTNDMTNEQDyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 69 --------KSIEEYSEPE----------------------------LARIRNeKIGFVFQAfNLLARSSVYENVRLPlfy 112
Cdd:PTZ00265 1245 deeqnvgmKNVNEFSLTKeggsgedstvfknsgkilldgvdicdynLKDLRN-LFSIVSQE-PMLFNMSIYENIKFG--- 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 113 snvPETAWDSKIKSAIDAVGISHRIVHEPGE-----------LSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEM 181
Cdd:PTZ00265 1320 ---KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1396
|
250 260 270
....*....|....*....|....*....|...
gi 818736213 182 IIKLLDELNRKTGRTIILITHEESLAKYARRLI 214
Cdd:PTZ00265 1397 IEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-203 |
4.83e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 9 LEKVYQSGESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQL-LGFLDRQTGgsykfdgkSIEEysEPELarirneKI 87
Cdd:PRK09544 7 LENVSVSFGQRRV-LSDVSLELKPGKILTLLGPNGAGKSTLVRVvLGLVAPDEG--------VIKR--NGKL------RI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 88 GFVFQAFNLlarssvyeNVRLPL----FYSNVPETAwDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPE 163
Cdd:PRK09544 70 GYVPQKLYL--------DTTLPLtvnrFLRLRPGTK-KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 818736213 164 MILADEPTGNLDSkNGEM-IIKLLDELNRKTGRTIILITHE 203
Cdd:PRK09544 141 LLVLDEPTQGVDV-NGQVaLYDLIDQLRRELDCAVLMVSHD 180
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-209 |
1.04e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 19 KTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirnekigfvfqafNLLA 98
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLID-------------AIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 99 RSSVYENVRLplfysnvpetawdskiksaIDAVGISHRI--VHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDS 176
Cdd:COG2401 109 KGDFKDAVEL-------------------LNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190
....*....|....*....|....*....|...
gi 818736213 177 KNGEMIIKLLDELNRKTGRTIILITHEESLAKY 209
Cdd:COG2401 170 QTAKRVARNLQKLARRAGITLVVATHHYDVIDD 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-202 |
1.45e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 21 VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDrQTGGSYKFDGKSIEeysepelAR---IRnEKIGFVFQAFNL 96
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLtGLLP-ASEGEAWLFGQPVD-------AGdiaTR-RRVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 97 LARSSVYENVRL--PLFysNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNL 174
Cdd:NF033858 351 YGELTVRQNLELhaRLF--HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
170 180
....*....|....*....|....*...
gi 818736213 175 DSKNGEMIIKLLDELNRKTGRTIILITH 202
Cdd:NF033858 429 DPVARDMFWRLLIELSREDGVTIFISTH 456
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-220 |
2.48e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELArirNEKIGFVFQAFNLLARSS 101
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAL---ENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 102 VYENV---RLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKN 178
Cdd:PRK10982 90 VMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 818736213 179 GEMIIKLLDELnRKTGRTIILITHE-ESLAKYARRLIRMKDGK 220
Cdd:PRK10982 170 VNHLFTIIRKL-KERGCGIVYISHKmEEIFQLCDEITILRDGQ 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-204 |
3.00e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.13 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEysepELARI 82
Cdd:PRK13540 1 MLDVIELDFDYHD----QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNLLARSSVYENVRLPLFYSNVpetawDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDP 162
Cdd:PRK13540 73 Q-KQLCFVGHRSGINPYLTLRENCLYDIHFSPG-----AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDElNRKTGRTIILITHEE 204
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSHQD 187
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-217 |
5.14e-13 |
|
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: 65.32 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 37 AIMGPSGSGKSTLLQLLGF-LDRQTGGSYKFDGKSieeysePELARIrNEKIGFVFQAFNLLA--------RSSVYENVr 107
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYaLTGELPPNSKGGAHD------PKLIRE-GEVRAQVKLAFENANgkkytitrSLAILENV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 108 lplFYSNVPETAWdskiksaidavgishRIVHEPGELSGGEKQ------RVAIARSFVLDPEMILADEPTGNLDSKNGEM 181
Cdd:cd03240 98 ---IFCHQGESNW---------------PLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 818736213 182 -IIKLLDELNRKTGRTIILITHEESLAKYARRLIRMK 217
Cdd:cd03240 160 sLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-206 |
6.66e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.18 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEeYSEPELARIRnEKIGFVFQ-AFNLLARSS 101
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALR-QQVATVFQdPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 102 VYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHrIVHEPGE-LSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGE 180
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQH-FRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180
....*....|....*....|....*.
gi 818736213 181 MIIKLLDELNRKtGRTIILITHEESL 206
Cdd:PRK13638 174 QMIAIIRRIVAQ-GNHVIISSHDIDL 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
6-214 |
7.66e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.51 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 6 VKNLEKVYQSGESkTVALDGVSFlvDKGEFIAIMGPSGSGKSTLLQLLGfldrqtgGSYKFDGKSIEeysepelarIRNE 85
Cdd:cd03237 1 YTYPTMKKTLGEF-TLEVEGGSI--SESEVIGILGPNGIGKTTFIKMLA-------GVLKPDEGDIE---------IELD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 86 KIGFVFQAFNLLARSSVYEnvrlpLFYSNVPETAWDSKIKSAI-DAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEM 164
Cdd:cd03237 62 TVSYKPQYIKADYEGTVRD-----LLSSITKDFYTHPYFKTEIaKPLQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 818736213 165 ILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKY-ARRLI 214
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYlADRLI 187
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-221 |
8.25e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.04 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLgflDRQtggsYKFDGKSIEEYSEPeLARIRNE----KIGFVFQAfNLL 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLI---QRH----FDVSEGDIRFHDIP-LTKLQLDswrsRLAVVSQT-PFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 98 ARSSVYENVRLplfysNVPEtAWDSKIKSAIDAVGISHRIVHEP-------GE----LSGGEKQRVAIARSFVLDPEMIL 166
Cdd:PRK10789 401 FSDTVANNIAL-----GRPD-ATQQEIEHVARLASVHDDILRLPqgydtevGErgvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 167 ADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-221 |
2.02e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSePELAri 82
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 rnEKIG--FVFQAFNLLARSSVYENVRLPLFYSNVPEtawdSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVL 160
Cdd:PRK15439 84 --HQLGiyLVPQEPLLFPNLSVKENILFGLPKRQASM----QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
36-203 |
2.21e-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: 65.73 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 36 IAIMGPSGSGKSTLLQLLGFLDRQtggsykFDGksiEEYSEPelarirNEKIGFVFQAFNLLARSSVYENV--------- 106
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKD------FNG---EARPQP------GIKVGYLPQEPQLDPTKTVRENVeegvaeikd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 107 ---RLPLFYSNVPE----------------------TAW--DSKIKSAIDAVGIShrivhePGE-----LSGGEKQRVAI 154
Cdd:TIGR03719 99 aldRFNEISAKYAEpdadfdklaaeqaelqeiidaaDAWdlDSQLEIAMDALRCP------PWDadvtkLSGGERRRVAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 818736213 155 ARSFVLDPEMILADEPTGNLDSkngEMIIKLLDELNRKTGrTIILITHE 203
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPG-TVVAVTHD 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-222 |
3.84e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 21 VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRQTGGSYKfdGKSIEeYSePELARIRNekigfvfqafnllar 99
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEISEGRVWA--ERSIA-YV-PQQAWIMN--------------- 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 100 SSVYENVrlpLFYSnvPETAwdSKIKSAI-------DAVGISHRIVHEPGE----LSGGEKQRVAIARSFVLDPEMILAD 168
Cdd:PTZ00243 735 ATVRGNI---LFFD--EEDA--ARLADAVrvsqleaDLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 818736213 169 EPTGNLDSKNGEMIIKLLdELNRKTGRTIILITHEESLAKYARRLIRMKDGKIE 222
Cdd:PTZ00243 808 DPLSALDAHVGERVVEEC-FLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-210 |
4.25e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 1 MKLIEVKNLEKVYQSGESKTVALDgVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKF-DGKSIEEYSepeL 79
Cdd:PTZ00265 380 IKKIQFKNVRFHYDTRKDVEIYKD-LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDIN---L 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIRNeKIGFVFQAfNLLARSSVYENVRLPLF----------YSNvpETAWDSK-------------------------- 123
Cdd:PTZ00265 456 KWWRS-KIGVVSQD-PLLFSNSIKNNIKYSLYslkdlealsnYYN--EDGNDSQenknkrnscrakcagdlndmsnttds 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 124 ------------IKSAiDAVGISHRI-VHE----------------PGELSGGEKQRVAIARSFVLDPEMILADEPTGNL 174
Cdd:PTZ00265 532 neliemrknyqtIKDS-EVVDVSKKVlIHDfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
250 260 270
....*....|....*....|....*....|....*.
gi 818736213 175 DSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYA 210
Cdd:PTZ00265 611 DNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYA 646
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-217 |
6.20e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.65 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqSGESkTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeysepeLARI 82
Cdd:TIGR01257 1937 ILRLNELTKVY-SGTS-SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-------LTNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RN--EKIGFV--FQAFN--LLARSSVYENVRLplfySNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIAR 156
Cdd:TIGR01257 2008 SDvhQNMGYCpqFDAIDdlLTGREHLYLYARL----RGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAI 2083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 157 SFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITH--EESLAKYARRLIRMK 217
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHsmEECEALCTRLAIMVK 2145
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-219 |
1.16e-11 |
|
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: 61.96 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 13 YQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLL-QLLGFLDRQTGGSYKFDGKSIEEYSEPELARIRNEkIGFVF 91
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS-VAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 92 QAFNLLaRSSVYENVRLPLFYSNvpetawdSKIKSAIDAVGISHRIVHEP-------GE----LSGGEKQRVAIARSFVL 160
Cdd:cd03290 86 QKPWLL-NATVEENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPfgdqteiGErginLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 161 DPEMILADEPTGNLDSKNG-----EMIIKLLdelnRKTGRTIILITHEESLAKYARRLIRMKDG 219
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSdhlmqEGILKFL----QDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-202 |
2.50e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLgfldrqtGGSY---KFDGKSIEEYSEPEL 79
Cdd:PRK13549 5 LLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-------SGVYphgTYEGEIIFEGEELQA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIRN-EKIGFV--FQAFNLLARSSVYENvrlpLFYSNVPETA----WDS----------KIKSAIDavgishriVHEP- 141
Cdd:PRK13549 74 SNIRDtERAGIAiiHQELALVKELSVLEN----IFLGNEITPGgimdYDAmylraqkllaQLKLDIN--------PATPv 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 142 GELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITH 202
Cdd:PRK13549 142 GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISH 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-203 |
6.44e-11 |
|
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: 61.38 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSgeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLdrQTGGSYkfDGKSIEEYSEPELARI 82
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV--YPHGTW--DGEIYWSGSPLKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNEK---IGFVFQAFNLLARSSVYENVRL-PLFYSNVPETAWDSKIKSA--------IDAVGISHRIvhepGELSGGEKQ 150
Cdd:TIGR02633 73 RDTEragIVIIHQELTLVPELSVAENIFLgNEITLPGGRMAYNAMYLRAknllrelqLDADNVTRPV----GDYGGGQQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818736213 151 RVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHE 203
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHK 200
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-224 |
7.81e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 21 VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL------GFLDR--QTGGSYKFDGKSIEEYSEPELARIR-----NEKI 87
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgGGAPRgaRVTGDVTLNGEPLAAIDAPRLARLRavlpqAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 88 GFVFQA--FNLLARssvYENVRLPLFYSNVP-ETAWdskikSAIDAVGISHRIVHEPGELSGGEKQRVAIARSF------ 158
Cdd:PRK13547 95 AFAFSAreIVLLGR---YPHARRAGALTHRDgEIAW-----QALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 159 ---VLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESL-AKYARRLIRMKDGKIESD 224
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaARHADRIAMLADGAIVAH 236
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-202 |
7.95e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 7 KNLEKVYqsGESKTVaLDGV--SFLvdKGEFIAIMGPSGSGKSTLLQLLGFLDRQtggsykFDGKSI--EEYS------E 76
Cdd:PRK11819 10 NRVSKVV--PPKKQI-LKDIslSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEARpaPGIKvgylpqE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 77 PEL---ARIRNEKIGFVFQAFNLLAR-SSVYENVRLPLFYSNvpET---------------AW--DSKIKSAIDAVGISh 135
Cdd:PRK11819 79 PQLdpeKTVRENVEEGVAEVKAALDRfNEIYAAYAEPDADFD--ALaaeqgelqeiidaadAWdlDSQLEIAMDALRCP- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 136 rivhePGE-----LSGGEKQRVAIARSFVLDPEMILADEPTGNLDSkngEMIIKLLDELNRKTGrTIILITH 202
Cdd:PRK11819 156 -----PWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLEQFLHDYPG-TVVAVTH 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-221 |
1.33e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLekvyqSGEsktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRqTGGSYKFDGKSIEEYSEPE-LAR 81
Cdd:PRK10762 258 LKVDNL-----SGP----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSPQDgLAN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 irnekiGFVF-----QAFNLLARSSVYENVRLPL--FYSNVPetawdSKIKSAIDAVGISHRI----VHEP------GEL 144
Cdd:PRK10762 328 ------GIVYisedrKRDGLVLGMSVKENMSLTAlrYFSRAG-----GSLKHADEQQAVSDFIrlfnIKTPsmeqaiGLL 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 145 SGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHE--ESLAkYARRLIRMKDGKI 221
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEmpEVLG-MSDRILVMHEGRI 473
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-219 |
3.86e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 16 GESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGflDRQTGGSYKFDGKsIEEYSEPE--LARI-----RNE--- 85
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA--GRKTGGYIEGDIR-ISGFPKKQetFARIsgyceQNDihs 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 86 -----KIGFVFQAFNLLARS-SVYENVRlplFYSNVPETAWDSKIKSAIdaVGIshrivhePG--ELSGGEKQRVAIARS 157
Cdd:PLN03140 966 pqvtvRESLIYSAFLRLPKEvSKEEKMM---FVDEVMELVELDNLKDAI--VGL-------PGvtGLSTEQRKRLTIAVE 1033
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 158 FVLDPEMILADEPTGNLDSKNGEMIIKLLDElNRKTGRTIILITHEESLAKYAR--RLIRMKDG 219
Cdd:PLN03140 1034 LVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIDIFEAfdELLLMKRG 1096
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-223 |
3.88e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 5 EVKNLEKvYQSGESKTValdgvSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPE-----L 79
Cdd:PRK09700 267 EVRNVTS-RDRKKVRDI-----SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARI---RNEKiGFvFQAFNLLARSSVYENVRLP-------LFYSNVPE-TAWDSKIKSAIDAVGISHRIvhepGELSGGE 148
Cdd:PRK09700 341 AYItesRRDN-GF-FPNFSIAQNMAISRSLKDGgykgamgLFHEVDEQrTAENQRELLALKCHSVNQNI----TELSGGN 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 149 KQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNrKTGRTIILITHE-ESLAKYARRLIRMKDGKIES 223
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSElPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-221 |
4.44e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEKVYQSgesktvALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPE---- 78
Cdd:PRK10982 250 ILEVRNLTSLRQP------SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainh 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 79 -LARIRNEKIGFVFQAFNLLARSSVYENVRLplfYSNVPETAWDSKIKS----AIDAVGI---SHRIvhEPGELSGGEKQ 150
Cdd:PRK10982 324 gFALVTEERRSTGIYAYLDIGFNSLISNIRN---YKNKVGLLDNSRMKSdtqwVIDSMRVktpGHRT--QIGSLSGGNQQ 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 151 RVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEmPELLGITDRILVMSNGLV 469
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-221 |
7.05e-10 |
|
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: 57.56 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQsgESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDrqTGGSYKFDGKSieeYSEPELARI 82
Cdd:cd03289 3 MTVKDLTAKYT--EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVS---WNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNLLARSsvyenvrlplFYSNV-PETAW-DSKIKSAIDAVGISHRIVHEPGEL-----------SGGEK 149
Cdd:cd03289 76 R-KAFGVIPQKVFIFSGT----------FRKNLdPYGKWsDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 150 QRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDElnRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-224 |
1.16e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 8 NLEKVYQSGESKTV--ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRQTGGSYKFDGKSieEYSePELARIRN 84
Cdd:PLN03232 616 SIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSV--AYV-PQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 85 ekigfvfqafnllarSSVYENVrlpLFYSNV-PETAWdskikSAIDAVGISH-------RIVHEPGE----LSGGEKQRV 152
Cdd:PLN03232 693 ---------------ATVRENI---LFGSDFeSERYW-----RAIDVTALQHdldllpgRDLTEIGErgvnISGGQKQRV 749
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 153 AIARSFVLDPEMILADEPTGNLDSKNGEMIIK--LLDELNrktGRTIILITHEESLAKYARRLIRMKDGKIESD 224
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK---GKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-202 |
1.27e-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: 57.61 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTvaLDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDrqTGGSYKFDGKSIEEYSepeLARI 82
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSaLLRLLS--TEGEIQIDGVSWNSVT---LQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RnEKIGFVFQAFNLLARSsvyenvrlplFYSNV-PETAW-DSKIKSAIDAVGISHRIVHEPGEL-----------SGGEK 149
Cdd:TIGR01271 1291 R-KAFGVIPQKVFIFSGT----------FRKNLdPYEQWsDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHK 1359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818736213 150 QRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTgrTIILITH 202
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC--TVILSEH 1410
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-209 |
1.56e-09 |
|
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: 56.22 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 33 GEFIAIMGPSGSGKSTLLQLLGflDRQTGGSYKFDGKS-----IEEYSEPEL----ARIRNEKIGFVF--QAFNLLARSs 101
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILA--GKLKPNLGKFDDPPdwdeiLDEFRGSELqnyfTKLLEGDVKVIVkpQYVDLIPKA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 102 VYENVRLPLfySNVPETawdSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEM 181
Cdd:cd03236 103 VKGKVGELL--KKKDER---GKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180
....*....|....*....|....*...
gi 818736213 182 IIKLLDELNrKTGRTIILITHEESLAKY 209
Cdd:cd03236 178 AARLIRELA-EDDNYVLVVEHDLAVLDY 204
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-202 |
1.66e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.11 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLgfldrqTG----GSYkfDGKSIEEYSEPELARIRN-EKIGFVF--QAF 94
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVL------SGvyphGSY--EGEILFDGEVCRFKDIRDsEALGIVIihQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 95 NLLARSSVYENvrlpLFYSNvpETA------WDSKIKSAID---AVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMI 165
Cdd:NF040905 88 ALIPYLSIAEN----IFLGN--ERAkrgvidWNETNRRAREllaKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 818736213 166 LADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITH 202
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-221 |
1.70e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 26 VSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSepelARIRNEKiGFVF-----QAFNLLARS 100
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS----TAQRLAR-GLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 101 SVYENV------RLPLFYSNVPETAWDSKIKSAIdavGISHRIVHEP-GELSGGEKQRVAIARSFVLDPEMILADEPTGN 173
Cdd:PRK15439 357 PLAWNVcalthnRRGFWIKPARENAVLERYRRAL---NIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 818736213 174 LDSKNGEMIIKLLDELNrKTGRTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK15439 434 VDVSARNDIYQLIRSIA-AQNVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-225 |
1.70e-09 |
|
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: 57.14 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRQTGGSYKFDGKSIEEYSEPELARirnEKIGFV---FQAFNLLA 98
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAIR---AGIAMVpedRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 99 RSSVYENVRLPL-----FYSNVPETAWDSKIKSAIDAVGISHRIVHEP-GELSGGEKQRVAIARSFVLDPEMILADEPTG 172
Cdd:TIGR02633 353 ILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 173 NLDSKNGEMIIKLLDELNRKtGRTIILITHE--ESLAkYARRLIRMKDGKIESDI 225
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSElaEVLG-LSDRVLVIGEGKLKGDF 485
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-221 |
1.85e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKVYQSGeskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEySEPELAR 81
Cdd:PRK10522 321 QTLELRNVTFAYQDN---GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 irnEKIGFVFQAFNLLARSSVYENvrlplfysnvpETAWDSKIKSAIDAVGISHRIVHEPGE-----LSGGEKQRVAIAR 156
Cdd:PRK10522 397 ---KLFSAVFTDFHLFDQLLGPEG-----------KPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 157 SFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-221 |
1.94e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.35 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 7 KNLEKVYQSGESKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDR--QTGGSYKFDGKSIEEYSEPelarir 83
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGnvSVEGDIHYNGIPYKEFAEK------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 nekigfvFQafnllaRSSVY---ENVRLPLFysNVPETawdskIKSAIDAVGisHRIVHEpgeLSGGEKQRVAIARSFVL 160
Cdd:cd03233 81 -------YP------GEIIYvseEDVHFPTL--TVRET-----LDFALRCKG--NEFVRG---ISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 161 DPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKYAR--RLIRMKDGKI 221
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLfdKVLVLYEGRQ 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-224 |
2.17e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRQTGGSYKFDGKsieeysepelarirnekIGFVFQA---FNlla 98
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-----------------VAYVPQVswiFN--- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 99 rSSVYENVrlpLFYSnvPETAwdSKIKSAIDAVGISHRIVHEPG-----------ELSGGEKQRVAIARSFVLDPEMILA 167
Cdd:PLN03130 693 -ATVRDNI---LFGS--PFDP--ERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818736213 168 DEPTGNLDSKNGEMIIK--LLDELNRKTGrtiILITHEESLAKYARRLIRMKDGKIESD 224
Cdd:PLN03130 765 DDPLSALDAHVGRQVFDkcIKDELRGKTR---VLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-221 |
4.79e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGesktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKfdgksieeYSEpelarir 83
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--------WSE------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFvfqafnlLARSSVYEnvrlplFYSNVPETAWDSKIKSAID---AV-GISHR-------IVHEPGELSGGEKQRV 152
Cdd:PRK15064 381 NANIGY-------YAQDHAYD------FENDLTLFDWMSQWRQEGDdeqAVrGTLGRllfsqddIKKSVKVLSGGEKGRM 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 153 AIARSFVLDPEMILADEPTGNLDSkngEMIIKLLDELNRKTGrTIILITHE-ESLAKYARRLIRMKDGKI 221
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDM---ESIESLNMALEKYEG-TLIFVSHDrEFVSSLATRIIEITPDGV 513
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-211 |
6.21e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.41 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 3 LIEVKNLEkvyQSGESKTVaLDGVSFLVDKGEFIAIMGPSGSGKSTL-LQLLGFLDRQ-TGGSYKFDGKSIEEYSEPELA 80
Cdd:PRK09580 1 MLSIKDLH---VSVEDKAI-LRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREDYEvTGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 81 rirNEKIGFVFQA-----------FNLLARSSVYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEpgELSGGEK 149
Cdd:PRK09580 77 ---GEGIFMAFQYpveipgvsnqfFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNV--GFSGGEK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 150 QRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYAR 211
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIK 212
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-216 |
8.23e-09 |
|
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: 53.80 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTL-------------LQLLG-FLDRQTGGSYKFDGKSIEEYSePELA----RIRN 84
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSaYARQFLGQMDKPDVDSIEGLS-PAIAidqkTTSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 85 EkigfvfqafnllARSSV------YENVRLplFYSNVPETAwdsKIKSAIDaVGISH-RIVHEPGELSGGEKQRVAIARS 157
Cdd:cd03270 90 N------------PRSTVgtvteiYDYLRL--LFARVGIRE---RLGFLVD-VGLGYlTLSRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 158 ---------FVLdpemilaDEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYARRLIRM 216
Cdd:cd03270 152 igsgltgvlYVL-------DEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-216 |
8.33e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.10 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLlgfldrqtggsykfdgksieeysepelarirnekiGFVFQAFNLLARSs 101
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-----------------------------------GLYASGKARLISF- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 102 vyenvrLPLFYSNvpETAWDSKIKSAIDaVGISH-RIVHEPGELSGGEKQRVAIARSFVLDPE--MILADEPTGNLDSKN 178
Cdd:cd03238 54 ------LPKFSRN--KLIFIDQLQFLID-VGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 818736213 179 GEMIIKLLDELnRKTGRTIILITHEESLAKYARRLIRM 216
Cdd:cd03238 125 INQLLEVIKGL-IDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-171 |
1.08e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 19 KTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQTGGSYKFDGkSIEEysepelARIRNE---KIGFVFQAF 94
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIaGARKIQQGRVEVLGG-DMAD------ARHRRAvcpRIAYMPQGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 95 --NLLARSSVYENV----RlpLFYSNVPETAWdsKIKSAIDAVGIsHRIVHEP-GELSGGEKQRVAIARSFVLDPEMILA 167
Cdd:NF033858 86 gkNLYPTLSVFENLdffgR--LFGQDAAERRR--RIDELLRATGL-APFADRPaGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
....
gi 818736213 168 DEPT 171
Cdd:NF033858 161 DEPT 164
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-217 |
1.44e-08 |
|
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: 52.36 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 31 DKGEFIAIMGPSGSGKSTLLQLLGFLdrqTGGSYKFDGKSIEEYSEPELARIRNEKIGFVFQafnllarssvyenvrlpl 110
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDAIGLA---LGGAQSATRRRSGVKAGCIVAAVSAELIFTRLQ------------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 111 fysnvpetawdskiksaidavgishrivhepgeLSGGEKQRVAIA-----RSFVLDPEMILaDEPTGNLDSKNG----EM 181
Cdd:cd03227 78 ---------------------------------LSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGqalaEA 123
|
170 180 190
....*....|....*....|....*....|....*.
gi 818736213 182 IIKLLDElnrktGRTIILITHEESLAKYARRLIRMK 217
Cdd:cd03227 124 ILEHLVK-----GAQVIVITHLPELAELADKLIHIK 154
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-221 |
1.50e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 26 VSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEeYSEPELArIRNekiGFVF-----QAFNLLARS 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSPRDA-IRA---GIMLcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 101 SVYENV-----RLPLFYSNVPETAWDSKI-KSAIDAVGISHRIVHEP-GELSGGEKQRVAIARSFVLDPEMILADEPTGN 173
Cdd:PRK11288 347 SVADNInisarRHHLRAGCLINNRWEAENaDRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 818736213 174 LDSKNGEMIIKLLDELnRKTGRTIILITHE--ESLAkYARRLIRMKDGKI 221
Cdd:PRK11288 427 IDVGAKHEIYNVIYEL-AAQGVAVLFVSSDlpEVLG-VADRIVVMREGRI 474
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-221 |
1.83e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQL------------LGFLDRQTGgsykfDGKSIEEysepelarIRnEKIGFV 90
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndLTLFGRRRG-----SGETIWD--------IK-KHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 91 FQAFNLLAR-SSVYENVRLPLF------YSNVPEtAWDSKIKSAIDAVGISHRIVHEP-GELSGGEKQRVAIARSFVLDP 162
Cdd:PRK10938 342 SSSLHLDYRvSTSVRNVILSGFfdsigiYQAVSD-RQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHP 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 163 EMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIIL------------ITHeeslakyarRLIRMKDGKI 221
Cdd:PRK10938 421 TLLILDEPLQGLDPLNRQLVRRFVDVLISE-GETQLLfvshhaedapacITH---------RLEFVPDGDI 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-219 |
1.91e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 20 TVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQL-LGFLdrqtggsykfdgksieeysEPELARIRNE-KIGFVFQaFNLL 97
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMiMGEL-------------------EPSEGKIKHSgRISFSPQ-TSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 98 ARSSVYENVRLPLFYSnvpetawDSKIKSAIDAVGISHRIVHEP-------GE----LSGGEKQRVAIARSFVLDPEMIL 166
Cdd:TIGR01271 499 MPGTIKDNIIFGLSYD-------EYRYTSVIKACQLEEDIALFPekdktvlGEggitLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 818736213 167 ADEPTGNLDSKNGEMII-----KLLdelnrkTGRTIILITHEESLAKYARRLIRMKDG 219
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFesclcKLM------SNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-175 |
2.19e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKVYqsgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFdGKSIeeysepelar 81
Cdd:TIGR03719 321 KVIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV---------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 irneKIGFVFQAF-NLLARSSVYENVR-----LPLFYSNVPETAWDSKIK-SAIDavgiSHRIVhepGELSGGEKQRVAI 154
Cdd:TIGR03719 386 ----KLAYVDQSRdALDPNKTVWEEISggldiIKLGKREIPSRAYVGRFNfKGSD----QQKKV---GQLSGGERNRVHL 454
|
170 180
....*....|....*....|.
gi 818736213 155 ARSFVLDPEMILADEPTGNLD 175
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-223 |
2.20e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLG---FLDrqtggsykfDGKSIEEySEPELARI-----RNEKiGFVF--- 91
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---------DGRIIYE-QDLIVARLqqdppRNVE-GTVYdfv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 92 ---------------QAFNLLARSSVYENV-RLplfySNVPET-----AW--DSKIKSAIDAVGIShriVHEP-GELSGG 147
Cdd:PRK11147 88 aegieeqaeylkryhDISHLVETDPSEKNLnEL----AKLQEQldhhnLWqlENRINEVLAQLGLD---PDAAlSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 148 EKQRVAIARSFVLDPEMILADEPTGNLDSKNgemiIKLLDELNRKTGRTIILITHEES-LAKYARRLIRMKDGKIES 223
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDRSfIRNMATRIVDLDRGKLVS 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-202 |
2.30e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 28 FLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIeeySEPELARIrnekIGFVFQAFNLLARSSVYENVR 107
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGDRSRF----MAYLGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 108 lplFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLD 187
Cdd:PRK13543 105 ---FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIS 181
|
170
....*....|....*
gi 818736213 188 ELNRKTGRTiILITH 202
Cdd:PRK13543 182 AHLRGGGAA-LVTTH 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-202 |
2.35e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.63 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 32 KGEFIAIMGPSGSGKSTLLQLL--------GFLDRQTGGSYK-------FDGkSIEEYsepeLARIRNEKIGfvfqafnl 96
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILagvlkpdeGEVDEDLKISYKpqyispdYDG-TVEEF----LRSANTDDFG-------- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 97 larSSVYENV---RL---PLFYSNVPEtawdskiksaidavgishrivhepgeLSGGEKQRVAIARSFVLDPEMILADEP 170
Cdd:COG1245 432 ---SSYYKTEiikPLgleKLLDKNVKD--------------------------LSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190
....*....|....*....|....*....|..
gi 818736213 171 TGNLDSKNGEMIIKLLDELNRKTGRTIILITH 202
Cdd:COG1245 483 SAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH 514
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
4-220 |
3.29e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGEsktVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSykfdgksieeysepeLARIR 83
Cdd:TIGR00954 452 IKFENIPLVTPNGD---VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR---------------LTKPA 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 84 NEKIGFVFQAfNLLARSSVYENVRLPLFYSNVPETAW-DSKIKSAIDAVGISHRIVHEPG---------ELSGGEKQRVA 153
Cdd:TIGR00954 514 KGKLFYVPQR-PYMTLGTLRDQIIYPDSSEDMKRRGLsDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIA 592
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 154 IARSFVLDPEMILADEPTGNLDSKNGEMIIKLLdelnRKTGRTIILITHEESLAKYARRLIRMkDGK 220
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKYHEYLLYM-DGR 654
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-219 |
4.18e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLlqLLGFLD--RQTGGSYKFDGKSIEEYSEPELARirnekigfvfqAFNLLARS 100
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTL--LLTFMRmvEVCGGEIRVNGREIGAYGLRELRR-----------QFSMIPQD 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 101 SVYEN--VRLPL--FYSNVPETAWdskikSAIDAVGISHRIVHEPGEL-----------SGGEKQRVAIARSFV-LDPEM 164
Cdd:PTZ00243 1393 PVLFDgtVRQNVdpFLEASSAEVW-----AALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLkKGSGF 1467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818736213 165 ILADEPTGNLDSKngemiiklLDELNRKTGR------TIILITHE-ESLAKYaRRLIRMKDG 219
Cdd:PTZ00243 1468 ILMDEATANIDPA--------LDRQIQATVMsafsayTVITIAHRlHTVAQY-DKIIVMDHG 1520
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-202 |
4.34e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 32 KGEFIAIMGPSGSGKSTLLQLLG------FLDRQTGGSY-----KFDGKSIEEYsepeLARIRNEKIGFVF--QAFNLLA 98
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSgelkpnLGDYDEEPSWdevlkRFRGTELQDY----FKKLANGEIKVAHkpQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 99 RSsVYENVRLPLfySNVPETAwdsKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKN 178
Cdd:COG1245 174 KV-FKGTVRELL--EKVDERG---KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180
....*....|....*....|....
gi 818736213 179 GEMIIKLLDELNRKtGRTIILITH 202
Cdd:COG1245 248 RLNVARLIRELAEE-GKYVLVVEH 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-206 |
7.43e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 26 VSFLVDKGEFIAIMGPSGSGKSTLLQLL-GFLDRQTGGSYKFDGKSIEEYSEPELArirnekiGFVFQAFNLLARSSVYe 104
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKSTILKLIsGELQPSSGTVFRSAKVRMAVFSQHHVD-------GLDLSSNPLLYMMRCF- 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 105 nvrlplfySNVPEtawdSKIKSAIDAVGISHRIVHEPG-ELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMII 183
Cdd:PLN03073 600 --------PGVPE----QKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALI 667
|
170 180
....*....|....*....|...
gi 818736213 184 KLLdeLNRKTGrtIILITHEESL 206
Cdd:PLN03073 668 QGL--VLFQGG--VLMVSHDEHL 686
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-222 |
7.59e-08 |
|
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: 50.06 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 32 KGEFIAIMGPSGSGKSTLLQLL-GFLDRQTGGSYKFDGksieeysepelarirnekigfvfqafnllarssvyenvrlpl 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 111 fysnvpetawdSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKL----- 185
Cdd:smart00382 39 -----------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190
....*....|....*....|....*....|....*..
gi 818736213 186 LDELNRKTGRTIILITHEESLAKyARRLIRMKDGKIE 222
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLG-PALLRRRFDRRIV 143
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-219 |
1.13e-07 |
|
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: 51.01 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQL-LGFLdrqtggsykfdgksieeysEPELARIRNE-KIGFVFQaFNLLARS 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLiLGEL-------------------EPSEGKIKHSgRISFSSQ-FSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 101 SVYENVRLPLFYSnvpetawDSKIKSAIDAVGISHRIVHEP-------GE----LSGGEKQRVAIARSFVLDPEMILADE 169
Cdd:cd03291 113 TIKENIIFGVSYD-------EYRYKSVVKACQLEEDITKFPekdntvlGEggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 170 PTGNLDSKNGEMII-----KLLdelnrkTGRTIILITHEESLAKYARRLIRMKDG 219
Cdd:cd03291 186 PFGYLDVFTEKEIFescvcKLM------ANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-202 |
1.62e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 32 KGEFIAIMGPSGSGKSTLLQLLGfldrqtgGSYKFDGKSIEEysepelarirNEKIGFVFQafnllaRSSVYENVRLPLF 111
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLA-------GVLKPDEGEVDP----------ELKISYKPQ------YIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 112 YSNVPETAWDSKIKSAI-DAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELN 190
Cdd:PRK13409 421 LRSITDDLGSSYYKSEIiKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIA 500
|
170
....*....|..
gi 818736213 191 RKTGRTIILITH 202
Cdd:PRK13409 501 EEREATALVVDH 512
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-202 |
2.30e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 32 KGEFIAIMGPSGSGKSTLLQLL-GFL-----DRQTGGSY-----KFDGKSIEEYsepeLARIRNEKIGFVF--QAFNLLA 98
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILsGELipnlgDYEEEPSWdevlkRFRGTELQNY----FKKLYNGEIKVVHkpQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 99 RSsVYENVRLPLfySNVPETawdSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKN 178
Cdd:PRK13409 174 KV-FKGKVRELL--KKVDER---GKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180
....*....|....*....|....
gi 818736213 179 GEMIIKLLDELNRktGRTIILITH 202
Cdd:PRK13409 248 RLNVARLIRELAE--GKYVLVVEH 269
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-203 |
1.36e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 21 VALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARIRNEKIGFVF---QAFNLL 97
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIdgdREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 98 ARSSVYENVR-----LPLFYSNVPET-AW--DSKIKSAIDAVGISHRIVHEP-GELSGGEKQRVAIARSFVLDPEMILAD 168
Cdd:PRK10636 95 EAQLHDANERndghaIATIHGKLDAIdAWtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190
....*....|....*....|....*....|....*
gi 818736213 169 EPTGNLDSkngEMIIKLLDELNRKTGrTIILITHE 203
Cdd:PRK10636 175 EPTNHLDL---DAVIWLEKWLKSYQG-TLILISHD 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-224 |
1.87e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 24 DGVSFLVDKGEFIAIMGPSGSGKSTLLQ-LLGFLDRQTGGSYKFDGKSIEeYSEPELArIRNeKIGFVFQ---AFNLLAR 99
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVK-IRNPQQA-IAQ-GIAMVPEdrkRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 100 SSVYENVRLPL-----FYSNVPETAWDSKIKSAIDAVGISHRIVHEP-GELSGGEKQRVAIARSFVLDPEMILADEPTGN 173
Cdd:PRK13549 356 MGVGKNITLAAldrftGGSRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 818736213 174 LDSKNGEMIIKLLDELnRKTGRTIILITHE--ESLAKYARRLIrMKDGKIESD 224
Cdd:PRK13549 436 IDVGAKYEIYKLINQL-VQQGVAIIVISSElpEVLGLSDRVLV-MHEGKLKGD 486
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-214 |
2.30e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 2.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818736213 144 LSGGEKQRVAIARSfvLDPEMI----LADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYARRLI 214
Cdd:PRK00635 477 LSGGEQERTALAKH--LGAELIgityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMISLADRII 548
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-206 |
2.55e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 9 LEKVYQSGESKTVA-LDGVSFLVDKGEFIAIMGPSGSGKSTLL-----QLLGFLdRQTGGSYKFDGKSIEEYSE---PEL 79
Cdd:TIGR00956 62 FRKLKKFRDTKTFDiLKPMDGLIKPGELTVVLGRPGSGCSTLLktiasNTDGFH-IGVEGVITYDGITPEEIKKhyrGDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIRNEKIGF----VFQAFNLLARSSVYENvRlplfYSNVPETAWDSKIKSAIDAV-GISHRIVHEPGE-----LSGGEK 149
Cdd:TIGR00956 141 VYNAETDVHFphltVGETLDFAARCKTPQN-R----PDGVSREEYAKHIADVYMATyGLSHTRNTKVGNdfvrgVSGGER 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 818736213 150 QRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLdelnrktgRTIILITHEESL 206
Cdd:TIGR00956 216 KRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL--------KTSANILDTTPL 264
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-202 |
2.59e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELARirnekigfvfqAFNLLARSSV 102
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR-----------VLSIIPQSPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 103 Y--ENVRLPL--FYSNVPETAWD----SKIKSAID--AVGISHRiVHEPGE-LSGGEKQRVAIARSFVLDPEMILADEPT 171
Cdd:PLN03232 1321 LfsGTVRFNIdpFSEHNDADLWEalerAHIKDVIDrnPFGLDAE-VSEGGEnFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190
....*....|....*....|....*....|.
gi 818736213 172 GNLDSKNGEMIIKLLDELNRKTgrTIILITH 202
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKSC--TMLVIAH 1428
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-208 |
3.42e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 22 ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSieeysepelarirnekiGFVFQAFNLLARSS 101
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------------ALIAISSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 102 VYENVRLPLFYSNVPETAWDSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPtgnLDSKNGEM 181
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA---LSVGDQTF 178
|
170 180
....*....|....*....|....*....
gi 818736213 182 IIKLLDELN--RKTGRTIILITHEESLAK 208
Cdd:PRK13545 179 TKKCLDKMNefKEQGKTIFFISHSLSQVK 207
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-213 |
3.68e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 38 IMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSEPELarirnekiGFVFQAFNLLARSSVYENVRlplFYSNVPE 117
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC--------TYIGHNLGLKLEMTVFENLK---FWSEIYN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 118 TAwdSKIKSAIDAVGISHRIVHEPGELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLdELNRKTGRTI 197
Cdd:PRK13541 100 SA--ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI-VMKANSGGIV 176
|
170
....*....|....*.
gi 818736213 198 ILITHEESLAKYARRL 213
Cdd:PRK13541 177 LLSSHLESSIKSAQIL 192
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
136-209 |
1.18e-05 |
|
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: 44.49 E-value: 1.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 136 RIVHEPG--ELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESLAKY 209
Cdd:cd03222 62 TPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDY 137
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-224 |
1.60e-05 |
|
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: 45.17 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSGESKTV-ALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEysePELARI 82
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---DNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 83 RNeKIGFVFQAFNLLARssVYenvrlplfysNVPETAWDSKIKSAIDAVGISHRIVHEPG-----ELSGGEKQRVAiars 157
Cdd:COG4615 405 RQ-LFSAVFSDFHLFDR--LL----------GLDGEADPARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLA---- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 158 fvldpeMILA---DEPtgnldskngemiIKLLDE--------------------LnRKTGRTIILITHEEslaKY---AR 211
Cdd:COG4615 468 ------LLVAlleDRP------------ILVFDEwaadqdpefrrvfytellpeL-KARGKTVIAISHDD---RYfdlAD 525
|
250
....*....|...
gi 818736213 212 RLIRMKDGKIESD 224
Cdd:COG4615 526 RVLKMDYGKLVEL 538
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-175 |
2.45e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 2 KLIEVKNLEKVYqsGEskTVALDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFdGKSIeeysepelar 81
Cdd:PRK11819 323 KVIEAENLSKSF--GD--RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV---------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 82 irneKIGFVFQAF-NLLARSSVYENVrlplfySN-----------VPETAWDSKI--------KSAidavgishrivhep 141
Cdd:PRK11819 388 ----KLAYVDQSRdALDPNKTVWEEI------SGgldiikvgnreIPSRAYVGRFnfkggdqqKKV-------------- 443
|
170 180 190
....*....|....*....|....*....|....
gi 818736213 142 GELSGGEKQRVAIARSFVLDPEMILADEPTGNLD 175
Cdd:PRK11819 444 GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
121-206 |
2.85e-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: 44.65 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 121 DSKIKSAIDAVGISHRIVHEPGEL--------SGGEKQ------RVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLL 186
Cdd:TIGR00606 1169 DENVSASDKRRNYNYRVVMLKGDTaldmrgrcSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHAL 1248
|
90 100
....*....|....*....|....
gi 818736213 187 DEL--NRKTGRT--IILITHEESL 206
Cdd:TIGR00606 1249 VEIikSRSQQRNfqLLVITHDEDF 1272
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
36-202 |
3.05e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 36 IAIMGPSGSGKSTLLQLLGF-LDRQTGGSYKFDGKSIEEYSEP---------------------ELARIRNEKIGFVFQA 93
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLINVGSEEasvelefehggkryrierrqgEFAEFLEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 94 FNLLARSSVYENVRLPLfysNVPETAWDSKIKSAIDAVGISHRIVHE------PGELSGGEKQRVAIAR--SFVLDpemi 165
Cdd:COG0419 106 LKRLLGLEIYEELKERL---KELEEALESALEELAELQKLKQEILAQlsgldpIETLSGGERLRLALADllSLILD---- 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 818736213 166 ladepTGNLDSKNGEMIIKLLDELNrktgrtiiLITH 202
Cdd:COG0419 179 -----FGSLDEERLERLLDALEELA--------IITH 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-203 |
6.71e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 5 EVKNLEkvYQSGESKTValDGVSFLVDKGEFIAIMGPSGSGKSTLLQL-LGFLDRQTGGSY---KFDGKSIEEYSE---P 77
Cdd:PRK11147 321 EMENVN--YQIDGKQLV--KDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQADSGRIHcgtKLEVAYFDQHRAeldP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 78 ElarirnekigfvfqafnllarSSVYENVRlplfysnvpetawDSKiksaiDAVGISHRIVHEPG--------------- 142
Cdd:PRK11147 397 E---------------------KTVMDNLA-------------EGK-----QEVMVNGRPRHVLGylqdflfhpkramtp 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 143 --ELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELnrkTGrTIILITHE 203
Cdd:PRK11147 438 vkALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY---QG-TVLLVSHD 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
140-217 |
1.07e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 140 EPGELSGGEKQ------RVAIARSFVLD-------PEMILaDEPTGNLDSKNGEMIIKLLDELNRKTGRTIILITHEESL 206
Cdd:PRK02224 778 EPEQLSGGERAlfnlslRCAIYRLLAEGiegdaplPPLIL-DEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDEL 856
|
90
....*....|.
gi 818736213 207 AKYARRLIRMK 217
Cdd:PRK02224 857 VGAADDLVRVE 867
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-221 |
2.37e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.05 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 4 IEVKNLEKVYQSgeSKTVALDGVSFLVDKGEFIAIMGPSGSGKSTL-LQLLGFLDrqtggsyKFDGKSI---EEYSEPEL 79
Cdd:cd03288 20 IKIHDLCVRYEN--NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVD-------IFDGKIVidgIDISKLPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 80 ARIRNeKIGFVFQAFNLLARSsvyenVRLPLfysnVPE------TAWD----SKIKSAIDAV-GISHRIVHEPGE-LSGG 147
Cdd:cd03288 91 HTLRS-RLSIILQDPILFSGS-----IRFNL----DPEckctddRLWEaleiAQLKNMVKSLpGGLDAVVTEGGEnFSVG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818736213 148 EKQRVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLdeLNRKTGRTIILITHEESLAKYARRLIRMKDGKI 221
Cdd:cd03288 161 QRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
111-216 |
4.54e-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: 40.77 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 111 FYSNVPETAwdSKIKSAIDaVGISHRIVHEPG-ELSGGEKQRVAIARSF---VLDPEMILADEPTGNLdskNGEMIIKLL 186
Cdd:TIGR00630 799 FFEAVPSIS--RKLQTLCD-VGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGL---HFDDIKKLL 872
|
90 100 110
....*....|....*....|....*....|..
gi 818736213 187 DELNR--KTGRTIILITHEESLAKYARRLIRM 216
Cdd:TIGR00630 873 EVLQRlvDKGNTVVVIEHNLDVIKTADYIIDL 904
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
32-69 |
5.49e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 5.49e-04
10 20 30
....*....|....*....|....*....|....*....
gi 818736213 32 KGEFIAIMGPSGSGKSTLL-QLLGFLDRQTGGSYKFDGK 69
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLnALLPELVLATGEISEKLGR 122
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
145-175 |
5.62e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 5.62e-04
10 20 30
....*....|....*....|....*....|.
gi 818736213 145 SGGEKQRVAIARSFVLDPEMILADEPTGNLD 175
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
32-53 |
6.08e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 39.41 E-value: 6.08e-04
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
143-202 |
6.57e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 6.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 143 ELSGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNgemIIKLLDELN-RKTgrTIILITH 202
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT---IRWLEDVLNeRNS--TMIIISH 210
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
137-211 |
7.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 137 IVHEPGELSGGEK-Q-----RVAIARSFVLDPEMILADEPTGNLDSKNGEMIIKLLDELNRktGRTIILITHEESLAKYA 210
Cdd:COG4717 552 RTRPVEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAK--GRQVIYFTCHEELVELF 629
|
.
gi 818736213 211 R 211
Cdd:COG4717 630 Q 630
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-219 |
8.63e-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: 40.00 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 142 GELSGGEKQRVAIARSF--VLDPEMILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYARRLIRMKDG 219
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRAADYVIDIGPG 565
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
24-50 |
1.15e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.04 E-value: 1.15e-03
10 20
....*....|....*....|....*..
gi 818736213 24 DGVSFLVDKGEFIAIMGPSGSGKSTLL 50
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
24-69 |
1.59e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 1.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 818736213 24 DGVSFL---VDKGEFIAIMGPSGSGKSTLL-QLLGFLDRQTGGSYKFDGK 69
Cdd:PRK01889 183 EGLDVLaawLSGGKTVALLGSSGVGKSTLVnALLGEEVQKTGAVREDDSK 232
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-227 |
1.65e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 144 LSGGEKQRVAIARSFVLDPE---MILADEPTGNLDSKNGEMIIKLLDELnRKTGRTIILITHEESLAKYARRLIRMKDGK 220
Cdd:PRK00635 1700 LSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTL-VSLGHSVIYIDHDPALLKQADYLIEMGPGS 1778
|
....*..
gi 818736213 221 IESDIRI 227
Cdd:PRK00635 1779 GKTGGKI 1785
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
136-214 |
1.98e-03 |
|
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: 37.83 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 136 RIVHEPGE-------LSGGEKQRVAIARSFVL-----DPEMILaDEPTGNLDSKNGEMIIKLLDELNRKTgrTIILITHE 203
Cdd:cd03278 99 EIIEAPGKkvqrlslLSGGEKALTALALLFAIfrvrpSPFCVL-DEVDAALDDANVERFARLLKEFSKET--QFIVITHR 175
|
90
....*....|.
gi 818736213 204 ESLAKYARRLI 214
Cdd:cd03278 176 KGTMEAADRLY 186
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
111-216 |
2.33e-03 |
|
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: 37.98 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 111 FYSNVPETAwdSKIKSAIDaVGISHRIVHEPG-ELSGGEKQRVAIARSF---VLDPEMILADEPTGNLDSkngEMIIKLL 186
Cdd:cd03271 139 FFENIPKIA--RKLQTLCD-VGLGYIKLGQPAtTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHF---HDVKKLL 212
|
90 100 110
....*....|....*....|....*....|..
gi 818736213 187 DELNRKT--GRTIILITHEESLAKYARRLIRM 216
Cdd:cd03271 213 EVLQRLVdkGNTVVVIEHNLDVIKCADWIIDL 244
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-214 |
2.36e-03 |
|
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: 38.77 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 23 LDGVSFLVDKGEFIAIMGPSGSGKSTLLQLLGFLDRQTGGSYKFDGKSIEEYSepeLARIRNeKIGFVFQAFNLLARSsv 102
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRF-KITIIPQDPVLFSGS-- 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 103 yenVRLPL--FYSNVPETAWD----SKIKSAIDAV--GISHRIVhEPGE-LSGGEKQRVAIARSFVLDPEMILADEPTGN 173
Cdd:TIGR00957 1376 ---LRMNLdpFSQYSDEEVWWalelAHLKTFVSALpdKLDHECA-EGGEnLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 818736213 174 LDSKNgemiikllDELNRKTGR------TIILITHE-ESLAKYARRLI 214
Cdd:TIGR00957 1452 VDLET--------DNLIQSTIRtqfedcTVLTIAHRlNTIMDYTRVIV 1491
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
35-104 |
3.69e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 3.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818736213 35 FIAIMGPSGSGKSTLLQLLGFL---DRQTGGSYKFDGKSIEEYSEPELARIRNEKIGFVFQAFNLLARSSVYE 104
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLadfDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYR 73
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
32-69 |
5.53e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.37 E-value: 5.53e-03
10 20 30
....*....|....*....|....*....|....*....
gi 818736213 32 KGEFIAIMGPSGSGKSTLL-QLLGFLDRQTGGSYKFDGK 69
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLnALLPELDLRTGEISEKLGR 143
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
145-227 |
8.22e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 36.64 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736213 145 SGGEKQRVAIARSFVLDPEMILADEPTGNLDSKNGEmiiKLLDELNR--KTGRTIILIT-HEESLAKYARRLIRMKDGKI 221
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN---EVWDEVRSmvRDGATVLLTTqYMEEAEQLAHELTVIDRGRV 222
|
....*.
gi 818736213 222 ESDIRI 227
Cdd:NF000106 223 IADGKV 228
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
33-72 |
8.49e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 36.97 E-value: 8.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 818736213 33 GEFIAIMGPSGSGKSTLLQ--LLGFLDRQTGGSYKFDG--KSIE 72
Cdd:PRK00349 635 GKFTCVTGVSGSGKSTLINetLYKALARKLNGAKKVPGkhKEIE 678
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-216 |
8.57e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.12 E-value: 8.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818736213 144 LSGGEKQRVAIARSF---VLDPEMILADEPTGNLDSKNGEMIIKLLDELNRKtGRTIILITHEESLAKYARRLIRM 216
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVKVADYVLEL 884
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
144-202 |
8.80e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 36.97 E-value: 8.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818736213 144 LSGGEKQRVAIA-----RS-----FVLdpemilaDEPTGNLDSkngEMIIKLLDELNR--KTGRTIILITH 202
Cdd:PRK00349 831 LSGGEAQRVKLAkelskRStgktlYIL-------DEPTTGLHF---EDIRKLLEVLHRlvDKGNTVVVIEH 891
|
|
| |
