|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-225 |
2.39e-116 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 332.01 E-value: 2.39e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGT-KQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQ 80
Cdd:COG1136 3 PLLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDIHSDIH 225
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-220 |
1.10e-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: 312.50 E-value: 1.10e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGT-KQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFR 82
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 KKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPS 162
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 163 IIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-226 |
1.45e-81 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 243.81 E-value: 1.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 8 HVSKIYGTKQKfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKeLG 87
Cdd:COG2884 6 NVSKRYPGGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR-IG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 88 FIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:COG2884 83 VVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 168 EPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSDIHQ 226
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLElVDRMPKRVLELEDGRLVRDEAR 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-223 |
7.18e-76 |
|
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: 229.63 E-value: 7.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGT-KQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQ 80
Cdd:COG4181 7 PIIELRGLTKTVGTgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKkdEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 161 PSIIFADEPTGALDSKSAQ---DLlhrLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDIHSD 223
Cdd:COG4181 165 PAILFADEPTGNLDAATGEqiiDL---LFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
1.22e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 224.97 E-value: 1.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKQK-FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkla 79
Cdd:COG1116 5 APALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 80 qfrkKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEknyQDVTEALGIYDLS---DKYPSEISGGQQQRTAAARA 156
Cdd:COG1116 80 ----PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERR---ERARELLELVGLAgfeDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 157 FVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKD--GDIHSDIH 225
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVFLADRVVVLSArpGRIVEEID 224
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-220 |
2.06e-73 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 223.06 E-value: 2.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQ-KFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF 81
Cdd:NF038007 1 MLNMQNAEKCYITKTiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-215 |
8.92e-71 |
|
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: 215.94 E-value: 8.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 8 HVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKELG 87
Cdd:TIGR03608 3 NISKKFGDKV---ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 88 FIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515743034 168 EPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAASFAQRVIML 215
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
2.65e-70 |
|
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: 214.69 E-value: 2.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNkklaqfRK 83
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------ER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-215 |
5.91e-70 |
|
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: 214.26 E-value: 5.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQ-KFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklaqfr 82
Cdd:cd03293 1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 kKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPS 162
Cdd:cd03293 73 -PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515743034 163 IIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASF-AQRVIML 215
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVL 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
6.20e-70 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 218.40 E-value: 6.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaq 80
Cdd:COG3839 1 MASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 fRKkeLGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:COG3839 75 -RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVeAMTLADRIAVMNDGRI 212
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-218 |
1.20e-69 |
|
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: 213.26 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFR 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG--VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 KKeLGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPS 162
Cdd:TIGR02673 79 RR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 163 IIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSlVDRVAHRVIILDDG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
1.35e-67 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 212.65 E-value: 1.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTkqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklAQ 80
Cdd:COG3842 3 MPALELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----PE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRkkELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEknyQDVTEAL---GIYDLSDKYPSEISGGQQQRTAAARAF 157
Cdd:COG3842 76 KR--NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIR---ARVAELLelvGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743034 158 VHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeALALADRIAVMNDGRI 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
1.34e-66 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 205.82 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQ-KFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnKKLAQF 81
Cdd:cd03257 1 LLEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS-RRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKELGFIFQD-YSVL-PTLTVKENIMLPLSVQKM--KKDEMEKNYQDVTEALGIY-DLSDKYPSEISGGQQQRTAAARA 156
Cdd:cd03257 80 RRKEIQMVFQDpMSSLnPRMTIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 157 FVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGvVAKIADRVAVMYAGKI 224
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-221 |
5.99e-65 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 201.43 E-value: 5.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGT-KQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF 81
Cdd:TIGR02211 1 LLKCENLGKRYQEgKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDIH 221
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-220 |
7.20e-65 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 202.21 E-value: 7.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQKfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF 81
Cdd:COG3638 1 PMLELRNLSKRYPGGTP--ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKkELGFIFQDYSVLPTLTVKENIM--------LPLSV-QKMKKDEMEKNYqDVTEALGIYDLSDKYPSEISGGQQQRTA 152
Cdd:COG3638 79 RR-RIGMIFQQFNLVPRLSVLTNVLagrlgrtsTWRSLlGLFPPEDRERAL-EALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 153 AARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDlARRYADRIIGLRDGRV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-220 |
9.53e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 204.93 E-value: 9.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTK-QKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKK 84
Cdd:COG1135 4 LENLSKTFPTKgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 85 eLGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNyqdVTEALGIYDLSDK---YPSEISGGQQQRTAAARAFVHQP 161
Cdd:COG1135 84 -IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKR---VAELLELVGLSDKadaYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAA-SFAQRVIMLKDGDI 220
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVrRICDRVAVLENGRI 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-220 |
3.33e-64 |
|
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: 208.22 E-value: 3.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQK--FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLA 79
Cdd:COG1123 259 PLLEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 80 QFRKKeLGFIFQD-YSVL-PTLTVKENIMLPLSVQK-MKKDEMEKnyqDVTEALGIYDLS----DKYPSEISGGQQQRTA 152
Cdd:COG1123 339 ELRRR-VQMVFQDpYSSLnPRMTVGDIIAEPLRLHGlLSRAERRE---RVAELLERVGLPpdlaDRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 153 AARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAvVRYIADRVAVMYDGRI 483
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-201 |
3.66e-64 |
|
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: 199.73 E-value: 3.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYG-TKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF 81
Cdd:cd03258 1 MIELKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKeLGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTH 201
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITH 199
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-220 |
2.55e-63 |
|
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: 198.18 E-value: 2.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtkQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRK 83
Cdd:cd03256 1 IEVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KeLGFIFQDYSVLPTLTVKENIMLPL-----SVQKMKKDEMEKNYQDVTEAL---GIYDLSDKYPSEISGGQQQRTAAAR 155
Cdd:cd03256 79 Q-IGMIFQQFNLIERLSVLENVLSGRlgrrsTWRSLFGLFPKEEKQRALAALervGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 156 AFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDlAREYADRIVGLKDGRI 223
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-220 |
1.78e-62 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 195.24 E-value: 1.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQ-KFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF 81
Cdd:TIGR02982 1 VISIRNLNHYYGHGSlRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKeLGFIFQDYSVLPTLTVKENIMLPLSVQ-KMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:TIGR02982 81 RRR-IGYIFQAHNLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-220 |
2.78e-62 |
|
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: 195.20 E-value: 2.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF 81
Cdd:COG1127 4 PMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKeLGFIFQDYSVLPTLTVKENIMLPLSVQ-KMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:COG1127 81 RRR-IGMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-237 |
1.43e-61 |
|
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: 193.22 E-value: 1.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTkqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaqfrk 83
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEknyQDVTEALGIYDLSD---KYPSEISGGQQQRTAAARAFVHQ 160
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIK---ERVAEALDLVQLEGyanRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAA-SFAQRVIMLKDGDIhsdihQQSKTKSKFYNE 237
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKI-----QQIGTPEEIYEE 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-218 |
1.41e-60 |
|
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: 188.94 E-value: 1.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLsNKKLAQFRK 83
Cdd:cd03229 1 LELKNVSKRYGQKT---VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KeLGFIFQDYSVLPTLTVKENIMLPLSvqkmkkdemeknyqdvtealgiydlsdkypseisGGQQQRTAAARAFVHQPSI 163
Cdd:cd03229 77 R-IGMVFQDFALFPHLTVLENIALGLS----------------------------------GGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-231 |
3.88e-60 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 193.33 E-value: 3.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTkqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaq 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGA---FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 frkKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:TIGR03265 76 ---RDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAA-SFAQRVIMLKDGDIHS-----DIHQQSKTK 231
Cdd:TIGR03265 153 PGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVIEQvgtpqEIYRHPATP 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-220 |
5.45e-60 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 189.43 E-value: 5.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqLSNKKLAQFR 82
Cdd:COG1126 1 MIEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 KKeLGFIFQDYSVLPTLTVKENIML-PLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:COG1126 77 RK-VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 162 SIIFADEPTGALD---SKSAQDLLHRL--EDMnkqfnsTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:COG1126 156 KVMLFDEPTSALDpelVGEVLDVMRDLakEGM------TMVVVTHEMGfAREVADRVVFMDGGRI 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-220 |
7.29e-60 |
|
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: 188.39 E-value: 7.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 9 VSKIYGtkQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKeLGF 88
Cdd:cd03292 6 VTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 89 IFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADE 168
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515743034 169 PTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKElVDTTRHRVIALERGKL 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-220 |
6.19e-59 |
|
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: 185.92 E-value: 6.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaqfrk 83
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAA-SFAQRVIMLKDGDI 220
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-220 |
2.77e-58 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 184.27 E-value: 2.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQlSNKKLAQFRK 83
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KeLGFIFQDYSVLPTLTVKENIML-PLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPS 162
Cdd:cd03262 77 K-VGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 163 IIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-223 |
3.72e-58 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 185.25 E-value: 3.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqfr 82
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 kKELGFIFQDYSVLPTLTVKENIML---PLsvQKMKKDEMEKNYQDVTEAL---GIYDLSDKYPSEISGGQQQRTAAARA 156
Cdd:COG1120 75 -RRIAYVPQEPPAPFGLTVRELVALgryPH--LGLFGRPSAEDREAVEEALertGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 157 FVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSD 223
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQ 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-220 |
7.45e-58 |
|
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: 184.24 E-value: 7.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTK-QKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQlsnKKLAQFR 82
Cdd:COG1124 2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR---RRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 KKeLGFIFQDY--SVLPTLTVKENIMLPLSVQKMKKDEmeknyQDVTEALGIYDLS----DKYPSEISGGQQQRTAAARA 156
Cdd:COG1124 79 RR-VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDRE-----ERIAELLEQVGLPpsflDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 157 FVHQPSIIFADEPTGALD-SKSAQdLLHRLEDMNKQFNSTIIMVTHDPSAASF-AQRVIMLKDGDI 220
Cdd:COG1124 153 LILEPELLLLDEPTSALDvSVQAE-ILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-223 |
3.98e-57 |
|
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: 181.76 E-value: 3.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtkQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqlsNKKLAQFRK 83
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KeLGFIFQDYS---VLPTltVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:COG1122 76 K-VGLVFQNPDdqlFAPT--VEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSD 223
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDlVAELADRVIVLDDGRIVAD 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-218 |
4.26e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 181.80 E-value: 4.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqlsnKKLAQFRK 83
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KeLGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:COG1131 74 R-IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEeAERLCDRVAIIDKG 207
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-240 |
1.49e-56 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 180.96 E-value: 1.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQKfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFR 82
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ--ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 KKeLGFIFQDYSVLPTLTVKENIM---------LPLSVQKMKKDEMEKNYQDVTEaLGIYDLSDKYPSEISGGQQQRTAA 153
Cdd:TIGR02315 79 RR-IGMIFQHYNLIERLTVLENVLhgrlgykptWRSLLGRFSEEDKERALSALER-VGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 154 ARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSDihqqsKTKS 232
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDlAKKYADRIVGLKAGEIVFD-----GAPS 231
|
....*...
gi 515743034 233 KFYNEIIQ 240
Cdd:TIGR02315 232 ELDDEVLR 239
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-218 |
1.49e-56 |
|
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: 179.59 E-value: 1.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKQKfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqfrkKE 85
Cdd:cd03225 2 LKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 LGFIFQDysvlP-----TLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:cd03225 77 VGLVFQN----PddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-220 |
1.61e-56 |
|
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: 180.39 E-value: 1.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKe 85
Cdd:cd03261 3 LRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 LGFIFQDYSVLPTLTVKENIMLPLSVQ-KMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSII 164
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 165 FADEPTGALDSKSA---QDLLHRLedmNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:cd03261 159 LYDEPTAGLDPIASgviDDLIRSL---KKELGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-223 |
4.30e-55 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 186.85 E-value: 4.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGT-KQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQ 80
Cdd:PRK10535 3 ALLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAASFAQRVIMLKDGDIHSD 223
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-236 |
4.75e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 179.96 E-value: 4.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTkqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqlSNKKLaqfRK 83
Cdd:COG1118 3 IEVRNISKRFGS---FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--TNLPP---RE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEknyQDVTEALGIYDLS---DKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:COG1118 75 RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIR---ARVEELLELVQLEglaDRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 161 PSIIFADEPTGALDSKSAQDL---LHRLEDmnkQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIhsdihQQSKTKSKFYN 236
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELrrwLRRLHD---ELGGTTVFVTHDQEeALELADRVVVMNQGRI-----EQVGTPDEVYD 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-218 |
5.36e-55 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 176.54 E-value: 5.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQ-KFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQ 80
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDG 218
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-223 |
9.70e-55 |
|
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: 173.78 E-value: 9.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRkke 85
Cdd:cd03214 2 VENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 lgfifqdySVLPtltvkenimlplsvQKMkkdemeknyqdvtEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIF 165
Cdd:cd03214 76 --------AYVP--------------QAL-------------ELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 166 ADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSD 223
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQ 179
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-251 |
1.05e-54 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 179.12 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYgtkQKFKaLHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaqfr 82
Cdd:NF040840 1 MIRIENLSKDW---KEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 kKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPS 162
Cdd:NF040840 72 -RGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 163 IIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDIHS--DIHQQ-SKTKSKFYNEI 238
Cdd:NF040840 151 LLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNfEEALSLADRVGIMLNGRLSQvgDVREVfRRPKNEFVARF 230
|
250
....*....|...
gi 515743034 239 IQLQSALGGVAND 251
Cdd:NF040840 231 VGFENIIEGVAEK 243
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-220 |
1.80e-54 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 175.37 E-value: 1.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklaqFRKKE 85
Cdd:TIGR00968 3 IANISKRFG---SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------ARDRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 LGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIF 165
Cdd:TIGR00968 74 IGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 166 ADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:TIGR00968 154 LDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEeAMEVADRIVVMSNGKI 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-220 |
2.58e-54 |
|
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: 175.91 E-value: 2.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTK--QKFK-------------------ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGT 62
Cdd:cd03294 1 IKIKGLYKIFGKNpqKAFKllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 63 VEISGNEINQLSNKKLAQFRKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSE 142
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 143 ISGGQQQRTAAARAFVHQPSIIFADEPTGALD---SKSAQDLLHRLEDMNKQfnsTIIMVTHDPSAA-SFAQRVIMLKDG 218
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDpliRREMQDELLRLQAELQK---TIVFITHDLDEAlRLGDRIAIMKDG 237
|
..
gi 515743034 219 DI 220
Cdd:cd03294 238 RL 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-218 |
2.59e-54 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 174.58 E-value: 2.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MP---ILNVNHVSKIYGT-KQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNK 76
Cdd:PRK10584 1 MPaenIVEVHHLKKSVGQgEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 77 KLAQFRKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARA 156
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 157 FVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDG 218
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-214 |
1.32e-53 |
|
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: 175.63 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQK-FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVIS---SIDSISGGTVEISGNEINQLSNKKL 78
Cdd:COG0444 1 LLEVRNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILgllPPPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 79 AQFRKKELGFIFQD-YSVL-PTLTVKENIMLPLSV-QKMKKDEMEKNyqdVTEALGIYDLS------DKYPSEISGGQQQ 149
Cdd:COG0444 81 RKIRGREIQMIFQDpMTSLnPVMTVGDQIAEPLRIhGGLSKAEARER---AIELLERVGLPdperrlDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 150 RTAAARAFVHQPSIIFADEPTGALD-SKSAQ--DLLHRLedmNKQFNSTIIMVTHD-PSAASFAQRV-IM 214
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDvTIQAQilNLLKDL---QRELGLAILFITHDlGVVAEIADRVaVM 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-220 |
1.24e-52 |
|
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: 170.60 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILnVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklaq 80
Cdd:cd03296 1 MSIE-VRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMK----KDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARA 156
Cdd:cd03296 71 VQERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 157 FVHQPSIIFADEPTGALDSKSAQDL---LHRLEDmnkQFNSTIIMVTHDPSAA-SFAQRVIMLKDGDI 220
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELrrwLRRLHD---ELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-220 |
2.90e-52 |
|
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: 177.02 E-value: 2.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGtKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISG---GTVEISGNEINQLSnkkl 78
Cdd:COG1123 3 PLLEVRDLSVRYP-GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELS---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 79 AQFRKKELGFIFQDY-SVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAF 157
Cdd:COG1123 78 EALRGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743034 158 VHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGvVAEIADRVVVMDDGRI 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-220 |
6.98e-51 |
|
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: 165.97 E-value: 6.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtkqKFKaLHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaqfrk 83
Cdd:cd03299 1 LKVENLSKDWK---EFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEeAWALADKVAIMLNGKL 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-224 |
6.71e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 163.39 E-value: 6.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTkQKFKAlhdiNFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaqfRK 83
Cdd:COG3840 2 LRLDDLTYRYGD-FPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----RP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 keLGFIFQDYSVLPTLTVKENIMLPLSvQKMKKDEMEKnyQDVTEAL---GIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:COG3840 73 --VSMLFQENNLFPHLTVAQNIGLGLR-PGLKLTAEQR--AQVEQALervGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSDI 224
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADG 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-201 |
1.45e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 165.74 E-value: 1.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 7 NHVSKIYGTKQK-FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKe 85
Cdd:PRK11153 5 KNISKVFPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 LGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNyqdVTEAL---GIYDLSDKYPSEISGGQQQRTAAARAFVHQPS 162
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKAR---VTELLelvGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 515743034 163 IIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTH 201
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-220 |
1.86e-49 |
|
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: 162.47 E-value: 1.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 8 HVSKIYGtkQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfRKKeLG 87
Cdd:cd03295 5 NVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---RRK-IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 88 FIFQDYSVLPTLTVKENIMLplsVQKMKKDEMEKNYQDVTEALGIYDL-----SDKYPSEISGGQQQRTAAARAFVHQPS 162
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIAL---VPKLLKWPKEKIRERADELLALVGLdpaefADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 163 IIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEI 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-220 |
3.18e-49 |
|
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: 159.49 E-value: 3.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaqfrK 83
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV-----K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLplsvqkmkkdemeknyqdvtealgiydlsdkypseiSGGQQQRTAAARAFVHQPSI 163
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEeAERLCDRVAILNNGRI 173
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-223 |
4.88e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 161.41 E-value: 4.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQlSNKKLAQFR 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 KkELGFIFQDYSVLPTLTVKENIML-PLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:PRK09493 77 Q-EAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDpsaASFAQRV----IMLKDGDIHSD 223
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHE---IGFAEKVasrlIFIDKGRIAED 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-218 |
1.73e-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: 157.54 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQKfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkLAQFRK 83
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KeLGFIFQDySVLPTLTVKENImlplsvqkmkkdemeknyqdvtealgiydlsdkypseISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03228 77 N-IAYVPQD-PFLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDG 218
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-223 |
3.24e-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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 158.00 E-value: 3.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIY--GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF 81
Cdd:TIGR04521 1 IKLKNVSYIYqpGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKeLGFIFQdY--SVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGI-YDLSDKYPSEISGGQQQRTAAARAFV 158
Cdd:TIGR04521 81 RKK-VGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 159 HQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSD 223
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEdVAEYADRVIVMHKGKIVLD 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-220 |
3.94e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 155.36 E-value: 3.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkLAQFRKKeLGFIFQDySVLPTLTV 101
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQ-VAYVPQE-PALWGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMLPLSVQKMKKDEMEknYQDVTEALGI-YDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQD 180
Cdd:COG4619 91 RDNLPFPFQLRERKFDRER--ALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515743034 181 LLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:COG4619 169 VEELLREYLAEEGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
4.06e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.40 E-value: 4.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQlsnkklaq 80
Cdd:COG1121 4 MPAIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 fRKKELGFIFQDYSVLPT--LTVKENIMLPLSVQK-----MKKDEMEKnyqdVTEAL---GIYDLSDKYPSEISGGQQQR 150
Cdd:COG1121 73 -ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRRglfrrPSRADREA----VDEALervGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 151 TAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAAS-FAQRVIMLKDGDIHS 222
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVReYFDRVLLLNRGLVAH 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-223 |
2.14e-46 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 158.57 E-value: 2.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklAQ 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP----AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 frKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNyqdVTEALGIY---DLSDKYPSEISGGQQQRTAAARAF 157
Cdd:PRK09452 85 --NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPR---VMEALRMVqleEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 158 VHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAA-SFAQRVIMLKDGDIHSD 223
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQD 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-220 |
1.38e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 152.48 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPIlNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEIN---QLSNKK 77
Cdd:PRK11124 1 MSI-QLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 78 LAQFRKKeLGFIFQDYSVLPTLTVKEN-IMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARA 156
Cdd:PRK11124 77 IRELRRN-VGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 157 FVHQPSIIFADEPTGALDSK-SAQ--DLLHRLEdmnkQFNSTIIMVTHDPSAA-SFAQRVIMLKDGDI 220
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEiTAQivSIIRELA----ETGITQVIVTHEVEVArKTASRVVYMENGHI 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-218 |
1.62e-45 |
|
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: 151.68 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 23 HDINFSVD-KGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKELGFIFQDYSVLPTLTV 101
Cdd:cd03297 13 FTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIM--LPLSVQKMKKDEMEKnyqdVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQ 179
Cdd:cd03297 93 RENLAfgLKRKRNREDRISVDE----LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515743034 180 DLLHRLEDMNKQFNSTIIMVTHDPSAA-SFAQRVIMLKDG 218
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAeYLADRIVVMEDG 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-231 |
2.10e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 152.09 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEIN---QLSNKKLAQFR 82
Cdd:COG4161 5 LKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 KKeLGFIFQDYSVLPTLTVKEN-IMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:COG4161 82 QK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 162 SIIFADEPTGALDSK-SAQ--DLLHRLedmnKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI----HSDIHQQSKTK 231
Cdd:COG4161 161 QVLLFDEPTAALDPEiTAQvvEIIREL----SQTGITQVIVTHEVEfARKVASQVVYMEKGRIieqgDASHFTQPQTE 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-220 |
3.61e-45 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 154.86 E-value: 3.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPIlNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNkklaq 80
Cdd:PRK10851 1 MSI-EIANIKKSFG---RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 fRKKELGFIFQDYSVLPTLTVKENIMLPLSV-QKMKKDEMEKNYQDVTEALGIYDLS---DKYPSEISGGQQQRTAAARA 156
Cdd:PRK10851 72 -RDRKVGFVFQHYALFRHMTVFDNIAFGLTVlPRRERPNAAAIKAKVTQLLEMVQLAhlaDRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 157 FVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQGNI 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-218 |
1.00e-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: 147.78 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfrKKE 85
Cdd:cd00267 2 IENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 LGFIFQdysvlptltvkenimlplsvqkmkkdemeknyqdvtealgiydlsdkypseISGGQQQRTAAARAFVHQPSIIF 165
Cdd:cd00267 75 IGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515743034 166 ADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPElAELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-170 |
1.13e-44 |
|
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: 147.41 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklAQFRKKELGFIFQDYSVLPTLTV 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 102 KENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSD----KYPSEISGGQQQRTAAARAFVHQPSIIFADEPT 170
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-220 |
1.20e-44 |
|
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: 149.64 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVIS-SIDSISG----GTVEISGNEINQLSNKKL 78
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrLNDLIPGapdeGEVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 79 AqfRKKELGFIFQDYSVLPtLTVKENIMLPLSVQKMKKDEMEKnyQDVTEALGIYDLSDK-----YPSEISGGQQQRTAA 153
Cdd:cd03260 78 E--LRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELD--ERVEEALRKAALWDEvkdrlHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 154 ARAFVHQPSIIFADEPTGALDSKSAQ---DLLHRLEDmnkqfNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAkieELIAELKK-----EYTIVIVTHNMQqAARVADRTAFLLNGRL 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-227 |
1.53e-44 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 149.25 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 8 HVSKIY-GTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqFRKKEL 86
Cdd:PRK10908 6 HVSKAYlGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVP-FLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 87 GFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFA 166
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 167 DEPTGALDSKSAQDLLHRLEDMNKqFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSDIHQQ 227
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGlISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-215 |
1.79e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 150.40 E-value: 1.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIY-GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkla 79
Cdd:COG4525 1 MSMLTVRHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 80 qfrkKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVH 159
Cdd:COG4525 76 ----ADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 160 QPSIIFADEPTGALDS---KSAQDLLHRLEdmnKQFNSTIIMVTHDPSAASF-AQRVIML 215
Cdd:COG4525 152 DPRFLLMDEPFGALDAltrEQMQELLLDVW---QRTGKGVFLITHSVEEALFlATRLVVM 208
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-220 |
2.31e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 151.40 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 8 HVSKIYGTKQKfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfRKKeLG 87
Cdd:COG1125 6 NVTKRYPDGTV--AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---RRR-IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 88 FIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKnyqDVTEALGIYDLS-----DKYPSEISGGQQQRTAAARAFVHQPS 162
Cdd:COG1125 80 YVIQQIGLFPHMTVAENIATVPRLLGWDKERIRA---RVDELLELVGLDpeeyrDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 163 IIFADEPTGALD---SKSAQDLLHRLEdmnKQFNSTIIMVTHDPSAA-SFAQRVIMLKDGDI 220
Cdd:COG1125 157 ILLMDEPFGALDpitREQLQDELLRLQ---RELGKTIVFVTHDIDEAlKLGDRIAVMREGRI 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-218 |
5.75e-44 |
|
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: 148.47 E-value: 5.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGneinqLSNKKLAQFRK 83
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG-----EDVRKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQeVEALCDRVVILHKG 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-216 |
1.67e-43 |
|
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: 146.14 E-value: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGneinqlsnKKLAQFRKKe 85
Cdd:cd03235 2 VEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERKR- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 LGFIFQDYSVLPT--LTVKENIMLPL-----SVQKMKKDEMEKnyqdVTEAL---GIYDLSDKYPSEISGGQQQRTAAAR 155
Cdd:cd03235 70 IGYVPQRRSIDRDfpISVRDVVLMGLyghkgLFRRLSKADKAK----VDEALervGLSELADRQIGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 156 AFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAAS-FAQRVIMLK 216
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLeYFDRVLLLN 206
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-218 |
1.77e-43 |
|
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: 146.84 E-value: 1.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqfrkkelgfIFQDYSVLPTLTV 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMLPLS--VQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQ 179
Cdd:TIGR01184 72 RENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515743034 180 DLLHRLEDMNKQFNSTIIMVTHDPSAASF-AQRVIMLKDG 218
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNG 191
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-220 |
6.74e-43 |
|
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: 152.99 E-value: 6.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkLAQFRKKeLGFIFQDySVLPTLT 100
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD---PASWRRQ-IAWVPQN-PYLFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIMlpLSVQKMKKDEMeknyQDVTEALGIYDLSDKYP-----------SEISGGQQQRTAAARAFVHQPSIIFADEP 169
Cdd:COG4988 427 IRENLR--LGRPDASDEEL----EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515743034 170 TGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-242 |
7.15e-43 |
|
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: 154.22 E-value: 7.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQKfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkLAQFRK 83
Cdd:COG2274 474 IELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KeLGFIFQDysvlPTL---TVKENIMLplsvqkmkkDEMEKNYQDVTEAL---GIYD----LSDKYPSEI-------SGG 146
Cdd:COG2274 550 Q-IGVVLQD----VFLfsgTIRENITL---------GDPDATDEEIIEAArlaGLHDfieaLPMGYDTVVgeggsnlSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 147 QQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDIHSD-IH 225
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDgTH 693
|
250
....*....|....*..
gi 515743034 226 QQSKTKSKFYNEIIQLQ 242
Cdd:COG2274 694 EELLARKGLYAELVQQQ 710
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-215 |
2.24e-42 |
|
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: 144.12 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQfrk 83
Cdd:cd03219 1 LEVRGLTKRFG---GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 keLGFI--FQDYSVLPTLTVKENIMLPLSVQK----------MKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRT 151
Cdd:cd03219 75 --LGIGrtFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 152 AAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNkQFNSTIIMVTHD-PSAASFAQRVIML 215
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDmDVVMSLADRVTVL 216
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-223 |
2.30e-42 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 146.87 E-value: 2.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 37 IMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaqfrkKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKK 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL------RHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 117 DEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTI 196
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*...
gi 515743034 197 IMVTHDPSAA-SFAQRVIMLKDGDIHSD 223
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKIAQI 182
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-236 |
9.02e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.97 E-value: 9.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 17 QKFKA---LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqlSNKKLAQFR------KKELG 87
Cdd:PRK11264 11 KKFHGqtvLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID--TARSLSQQKglirqlRQHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 88 FIFQDYSVLPTLTVKENIML-PLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFA 166
Cdd:PRK11264 89 FVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 167 DEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDGdihsDIHQQSKTKSKFYN 236
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSfARDVADRAIFMDQG----RIVEQGPAKALFAD 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-215 |
5.31e-41 |
|
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: 141.33 E-value: 5.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQ 80
Cdd:COG0411 2 DPLLEVRGLTKRFG---GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 frkkeLGFI--FQDYSVLPTLTVKENIMLPLSVQ------------KMKKDEMEKNYQDVTEAL---GIYDLSDKYPSEI 143
Cdd:COG0411 79 -----LGIArtFQNPRLFPELTVLENVLVAAHARlgrgllaallrlPRARREEREARERAEELLervGLADRADEPAGNL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 144 SGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSA-ASFAQRVIML 215
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLvMGLADRIVVL 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-220 |
6.66e-41 |
|
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: 139.95 E-value: 6.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQKfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInqLSNKKLAQfrk 83
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASF-AQRVIMLKDGDI 220
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-220 |
1.07e-40 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 143.06 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaq 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 frkKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:PRK11650 76 ---RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743034 161 PSIIFADEPTGALDSK-SAQdllHRLE--DMNKQFNSTIIMVTHDP-SAASFAQRVIMLKDGDI 220
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKlRVQ---MRLEiqRLHRRLKTTSLYVTHDQvEAMTLADRVVVMNGGVA 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-222 |
5.74e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 139.38 E-value: 5.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQKFkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEinqLSNKKLAQF 81
Cdd:PRK13635 4 EIIRVEHISFRYPDAATY-ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKeLGFIFQ--DYSVLPTlTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVH 159
Cdd:PRK13635 80 RRQ-VGMVFQnpDNQFVGA-TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 160 QPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDIHS 222
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-225 |
1.49e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 137.50 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVeISGNeinqlsnKKLAQFRK 83
Cdd:PRK11247 13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT-------APLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 kELGFIFQDYSVLPTLTVKENIMLPLsvqkmkKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:PRK11247 82 -DTRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 164 IFADEPTGALDSKS---AQDLLHRLEdmnKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSDIH 225
Cdd:PRK11247 155 LLLDEPLGALDALTrieMQDLIESLW---QQHGFTVLLVTHDVSeAVAMADRVLLIEEGKIGLDLT 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-223 |
2.59e-39 |
|
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: 136.75 E-value: 2.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISS-IDSISGGTVEISGNEINQLSnkkLA 79
Cdd:COG1119 1 DPLLELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGED---VW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 80 QFRKKeLGFI---FQDYsVLPTLTVKE--------NIMLPLSVQkmkkDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQ 148
Cdd:COG1119 75 ELRKR-IGLVspaLQLR-FPRDETVLDvvlsgffdSIGLYREPT----DEQRERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 149 QRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSA--ASFaQRVIMLKDGDIHSD 223
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEipPGI-THVLLLKDGRVVAA 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-220 |
2.76e-39 |
|
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: 135.58 E-value: 2.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTkqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqlsnKKLAQFRKKe 85
Cdd:cd03265 3 VENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 LGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIF 165
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 166 ADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRI 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-202 |
4.81e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 137.94 E-value: 4.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQKF--------KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQL 73
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 74 SNKKLAQFRKKeLGFIFQD-YSVL-PTLTVKENIMLPLSVQKM--KKDEMEKnyqdVTEALGIYDLS----DKYPSEISG 145
Cdd:COG4608 86 SGRELRPLRRR-MQMVFQDpYASLnPRMTVGDIIAEPLRIHGLasKAERRER----VAELLELVGLRpehaDRYPHEFSG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 146 GQQQRTAAARAFVHQPSIIFADEPTGALD-SKSAQdLLHRLEDMNKQFNSTIIMVTHD 202
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDvSIQAQ-VLNLLEDLQDELGLTYLFISHD 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-244 |
8.70e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 141.84 E-value: 8.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKQKfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkLAQFRKKe 85
Cdd:COG1132 342 FENVSFSYPGDRP--VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQ- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 LGFIFQDySVLPTLTVKENIMLPlsvqKMKKDEmeknyQDVTEAL---GIYD----LSDKYPSEI-------SGGQQQRT 151
Cdd:COG1132 416 IGVVPQD-TFLFSGTIRENIRYG----RPDATD-----EEVEEAAkaaQAHEfieaLPDGYDTVVgergvnlSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 152 AAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDIhsdI----HQQ 227
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRI---VeqgtHEE 560
|
250
....*....|....*..
gi 515743034 228 SKTKSKFYNEIIQLQSA 244
Cdd:COG1132 561 LLARGGLYARLYRLQFG 577
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-220 |
9.61e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 137.93 E-value: 9.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 8 HVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklaqFRKKELG 87
Cdd:PRK11432 11 NITKRFG---SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS------IQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 88 FIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEknyQDVTEALGIYDLS---DKYPSEISGGQQQRTAAARAFVHQPSII 164
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERK---QRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 165 FADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAAsFA--QRVIMLKDGDI 220
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEA-FAvsDTVIVMNKGKI 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-220 |
1.44e-38 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 137.85 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 9 VSKIYGTKQKFKalhDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaqfrkKELGF 88
Cdd:PRK11000 9 VTKAYGDVVISK---DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE------RGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 89 IFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADE 168
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 169 PTGALDskSAQDLLHRLE--DMNKQFNSTIIMVTHDP-SAASFAQRVIMLKDGDI 220
Cdd:PRK11000 160 PLSNLD--AALRVQMRIEisRLHKRLGRTMIYVTHDQvEAMTLADKIVVLDAGRV 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-220 |
1.44e-38 |
|
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: 140.59 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIY--------GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTL----LNVISSidsisGGTVEISGNE 69
Cdd:COG4172 274 PLLEARDLKVWFpikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 70 INQLSNKKLAQFRKkELGFIFQD-YSVL-PTLTVKENIMLPLSVQKMKKDEMEKNyQDVTEALGIYDLS----DKYPSEI 143
Cdd:COG4172 349 LDGLSRRALRPLRR-RMQVVFQDpFGSLsPRMTVGQIIAEGLRVHGPGLSAAERR-ARVAEALEEVGLDpaarHRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 144 SGGQQQRTAAARAFVHQPSIIFADEPTGALD-SKSAQ--DLLHRLedmNKQFNSTIIMVTHDPSA-ASFAQRVIMLKDGD 219
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDvSVQAQilDLLRDL---QREHGLAYLFISHDLAVvRALAHRVMVMKDGK 503
|
.
gi 515743034 220 I 220
Cdd:COG4172 504 V 504
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
9-234 |
2.15e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 134.76 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 9 VSKIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSI---DSISGGTVEISGNEInQLSNKKLAQFRKK- 84
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTV-QREGRLARDIRKSr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 85 -ELGFIFQDYSVLPTLTVKENIML------PL---SVQKMKKDEMEKNYQDVTEaLGIYDLSDKYPSEISGGQQQRTAAA 154
Cdd:PRK09984 86 aNTGYIFQQFNLVNRLSVLENVLIgalgstPFwrtCFSWFTREQKQRALQALTR-VGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 155 RAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSDIHQQSKTKSK 233
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
|
.
gi 515743034 234 F 234
Cdd:PRK09984 245 F 245
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-212 |
4.46e-38 |
|
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: 132.22 E-value: 4.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklAQF 81
Cdd:COG4133 1 MMLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR----EDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKkELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEknYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:COG4133 74 RR-RLAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAASFAQRV 212
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELAAARVL 200
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-218 |
1.08e-37 |
|
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: 130.75 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIygTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISS--IDSISGGTVEISGneinqlSNKKLAQF 81
Cdd:cd03213 9 LTVTVKSSP--SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLING------RPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RkKELGFIFQDYSVLPTLTVKENIMLPLsvqKMKKdemeknyqdvtealgiydlsdkypseISGGQQQRTAAARAFVHQP 161
Cdd:cd03213 81 R-KIIGYVPQDDILHPTLTVRETLMFAA---KLRG--------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAASFAQ--RVIMLKDG 218
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFELfdKLLLLSQG 188
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-241 |
1.31e-37 |
|
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: 138.36 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYgTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF 81
Cdd:COG4987 332 PSLELEDVSFRY-PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 rkkeLGFIFQDYSVLPTlTVKENIML--P-LSvqkmkKDEMEknyqDVTEALGIYDLSDKYP-----------SEISGGQ 147
Cdd:COG4987 411 ----IAVVPQRPHLFDT-TLRENLRLarPdAT-----DEELW----AALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 148 QQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDIH-SDIHQ 226
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIVeQGTHE 554
|
250
....*....|....*
gi 515743034 227 QSKTKSKFYNEIIQL 241
Cdd:COG4987 555 ELLAQNGRYRQLYQR 569
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-218 |
1.52e-37 |
|
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: 134.84 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 24 DINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEIsGNEINQLSNKKlaQFRKKE---LGFIFQDYSVLPTLT 100
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL-GGEVLQDSARG--IFLPPHrrrIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIMLplSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQD 180
Cdd:COG4148 94 VRGNLLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 515743034 181 LLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-220 |
2.42e-37 |
|
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: 129.26 E-value: 2.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLsnkKLAQFRKKeLGFIFQDYSVLPTlTV 101
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELGDH-VGYLPQDDELFSG-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMlplsvqkmkkdemeknyqdvtealgiydlsdkypseiSGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDL 181
Cdd:cd03246 93 AENIL-------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 515743034 182 LHRLEDMNKQfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:cd03246 136 NQAIAALKAA-GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-223 |
3.00e-37 |
|
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: 130.57 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQK-FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGneINQLSNKKLAQF 81
Cdd:cd03266 1 MITADALTKRFRDVKKtVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RkkeLGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:cd03266 79 R---LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMnKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSD 223
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYE 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-218 |
3.80e-37 |
|
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: 133.70 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 24 DINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKELGFIFQDYSVLPTLTVKE 103
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 104 NimLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLH 183
Cdd:TIGR02142 95 N--LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 515743034 184 RLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQeVLRLADRVVVLEDG 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-220 |
1.52e-36 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 128.44 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 26 NFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEIsgneiNQLSNKKLAQFRKKeLGFIFQDYSVLPTLTVKENI 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV-----NDQSHTGLAPYQRP-VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 106 MLPLSVQ-KMKKDEMEKnYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHR 184
Cdd:TIGR01277 92 GLGLHPGlKLNAEQQEK-VVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 515743034 185 LEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-223 |
1.92e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 128.55 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 26 NFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNeinqlsNKKLAQFRKKELGFIFQDYSVLPTLTVKENI 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ------DHTTTPPSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 106 MLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRL 185
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 515743034 186 EDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDIHSD 223
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSlEDAARIAPRSLVVADGRIAWD 211
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-220 |
2.20e-36 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 129.15 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKK---- 77
Cdd:COG4598 7 PALEVRDLHKSFGDLE---VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 78 ------LAQFRKKeLGFIFQDYSVLPTLTVKENIML-PLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQR 150
Cdd:COG4598 84 padrrqLQRIRTR-LGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 151 TAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGfARDVSSHVVFLHQGRI 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-220 |
2.65e-36 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 127.61 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 24 DINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQlsnkklAQFRKKELGFIFQDYSVLPTLTVKE 103
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA------APPADRPVSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 104 NIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLH 183
Cdd:cd03298 90 NVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 515743034 184 RLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-220 |
5.81e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 129.01 E-value: 5.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPIlNVNHVSKIYGTKQKF--KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQlSNKKL 78
Cdd:PRK13637 1 MSI-KIENLTHIYMEGTPFekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 79 AQFRKKeLGFIFQ--DYSVLPTlTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGI--YDLSDKYPSEISGGQQQRTAAA 154
Cdd:PRK13637 79 SDIRKK-VGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 155 RAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKC 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
6.71e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.57 E-value: 6.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQKFkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkLAQF 81
Cdd:PRK13632 6 VMIKVENVSFSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKeLGFIFQDysvlPT-----LTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARA 156
Cdd:PRK13632 82 RKK-IGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743034 157 FVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-223 |
1.05e-35 |
|
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: 126.55 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 17 QKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklAQFRKKELGFIFQDysvl 96
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD----PADLRRNIGYVPQD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 97 PTL---TVKENIML--PLSvqkmkKDE--MEknyqdVTEALGIYDLSDKYP-----------SEISGGQQQRTAAARAFV 158
Cdd:cd03245 87 VTLfygTLRDNITLgaPLA-----DDEriLR-----AAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 159 HQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfnSTIIMVTHDPSAASFAQRVIMLKDGDIHSD 223
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-218 |
1.07e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 127.51 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklaqfr 82
Cdd:PRK11248 1 MLQISHLYADYGGK---PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 kKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPS 162
Cdd:PRK11248 70 -AERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 163 IIFADEPTGALDS---KSAQDLLHRL-EDMNKQfnstIIMVTHDPSAASF-AQRVIMLKDG 218
Cdd:PRK11248 149 LLLLDEPFGALDAftrEQMQTLLLKLwQETGKQ----VLLITHDIEEAVFmATELVLLSPG 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-221 |
2.19e-35 |
|
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: 125.06 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 8 HVSKI-YGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNeinQLSNKKlaqfRKKEL 86
Cdd:cd03226 1 RIENIsFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKE----RRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 87 GFIFQD-YSVLPTLTVKENIMLPLsvqkMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIF 165
Cdd:cd03226 74 GYVMQDvDYQLFTDSVREELLLGL----KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 166 ADEPTGALDSKSAQ---DLLHRLEDMNKqfnsTIIMVTHDPS-AASFAQRVIMLKDGDIH 221
Cdd:cd03226 150 FDEPTSGLDYKNMErvgELIRELAAQGK----AVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-215 |
3.83e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 124.52 E-value: 3.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVI----SSIDSISgGTVEISGNEINQLsnkklaQFRKKELGFIFQDYSVLP 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlSPAFSAS-GEVLLNGRRLTAL------PAEQRRIGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 98 TLTVKENIM--LPLSVQKMKKDEMeknYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDS 175
Cdd:COG4136 90 HLSVGENLAfaLPPTIGRAQRRAR---VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515743034 176 KSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIML 215
Cdd:COG4136 167 ALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-231 |
5.35e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.97 E-value: 5.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIY--GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQ 80
Cdd:COG1101 1 MLELKNLSKTFnpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FrkkeLGFIFQDYSV--LPTLTVKENIMLPLSVQKMK------KDEMEKNYQDVTEALGIyDLSDKYPSEI---SGGQQQ 149
Cdd:COG1101 81 Y----IGRVFQDPMMgtAPSMTIEENLALAYRRGKRRglrrglTKKRRELFRELLATLGL-GLENRLDTKVgllSGGQRQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 150 RTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAA-SFAQRVIMLKDGDIHSDIHQQS 228
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAlDYGNRLIMMHEGRIILDVSGEE 235
|
...
gi 515743034 229 KTK 231
Cdd:COG1101 236 KKK 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-218 |
1.31e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.64 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNkklaq 80
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQH---AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 fRKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:PRK11607 89 -YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDG 218
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRG 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-220 |
1.43e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.38 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSI-DSISG----GTVEISGNEINQlSNK 76
Cdd:COG1117 10 PKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPGarveGEILLDGEDIYD-PDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 77 KLAQFRKKeLGFIFQDYSVLPTlTVKENIMLPLSVQKMK-KDEMEknyQDVTEAL---GIYD-----LsDKYPSEISGGQ 147
Cdd:COG1117 86 DVVELRRR-VGMVFQKPNPFPK-SIYDNVAYGLRLHGIKsKSELD---EIVEESLrkaALWDevkdrL-KKSALGLSGGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 148 QQRTAAARAFVHQPSIIFADEPTGALDSKSAQ---DLLHRL-EDMnkqfnsTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAkieELILELkKDY------TIVIVTHNMQqAARVSDYTAFFYLGEL 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-220 |
2.41e-34 |
|
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: 122.93 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqfrK 83
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMK--KDEMEKnyqdvtealgIYDL-------SDKYPSEISGGQQQRTAAA 154
Cdd:cd03224 75 AGIGYVPEGRRIFPELTVEENLLLGAYARRRAkrKARLER----------VYELfprlkerRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 155 RAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNaRFALEIADRAYVLERGRV 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-220 |
4.54e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 123.65 E-value: 4.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInQLSNKKLAQFRKKeLGFIFQ---DYSVLP 97
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT-VGIVFQnpdDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 98 TltVKENIML-PLSVqKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSK 176
Cdd:PRK13639 95 T--VEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515743034 177 SAQDLLHRLEDMNKQfNSTIIMVTHDPSAAS-FAQRVIMLKDGDI 220
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPvYADKVYVMSDGKI 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-181 |
5.96e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 122.27 E-value: 5.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQfrk 83
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170
....*....|....*...
gi 515743034 164 IFADEPTGALDSKSAQDL 181
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDI 172
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-220 |
1.16e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 122.49 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIY------GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLS 74
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 75 NKKLAQFRkKELGFIFQDY--SVLPTLTVKENIMLPLS-VQKMKKDEMEKNYQDVTEALGIYD-LSDKYPSEISGGQQQR 150
Cdd:PRK10419 81 RAQRKAFR-RDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 151 TAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAAS-FAQRVIMLKDGDI 220
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVErFCQRVMVMDNGQI 230
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-220 |
1.18e-33 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 122.02 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSI-DSISG----GTVEISGNEINQlSNKK 77
Cdd:TIGR00972 1 AIEIENLNLFYG---EKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMnDLVPGvrieGKVLFDGQDIYD-KKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 78 LAQFRKKeLGFIFQDYSVLPtLTVKENIMLPLSVQKMK-KDEMEKNYQDVTEALGIYD-LSDK---YPSEISGGQQQRTA 152
Cdd:TIGR00972 77 VVELRRR-VGMVFQKPNPFP-MSIYDNIAYGPRLHGIKdKKELDEIVEESLKKAALWDeVKDRlhdSALGLSGGQQQRLC 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 153 AARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFnsTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:TIGR00972 155 IARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNmQQAARISDRTAFFYDGEL 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-223 |
1.21e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 123.27 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIY--GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQ--- 80
Cdd:PRK13651 5 VKNIVKIFnkKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEkvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 ---------FRK--------KELGFIFQ--DYSVLPTlTVKENIML-PLSVqKMKKDEMEKNYQDVTEALGIyDLS--DK 138
Cdd:PRK13651 85 eklviqktrFKKikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFgPVSM-GVSKEEAKKRAAKYIELVGL-DESylQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 139 YPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKD 217
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDlDNVLEWTKRTIFFKD 240
|
....*.
gi 515743034 218 GDIHSD 223
Cdd:PRK13651 241 GKIIKD 246
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
22-221 |
1.99e-33 |
|
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: 126.69 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqfrkKELGFIFQDYSVLPTlTV 101
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMlplsvqkmkkdEMEKNYQD--VTEAL---GIYDL----SDKYPSEI-------SGGQQQRTAAARAFVHQPSIIF 165
Cdd:TIGR01842 409 AENIA-----------RFGENADPekIIEAAklaGVHELilrlPDGYDTVIgpggatlSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 166 ADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAASFAQRVIMLKDGDIH 221
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVDKILVLQDGRIA 532
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-220 |
2.27e-33 |
|
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: 120.79 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfRKKeLGFIFQDYSVLPTlT 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSM-IGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIMlpLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEI-------SGGQQQRTAAARAFVHQPSIIFADEPTGAL 173
Cdd:cd03254 93 IMENIR--LGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLgenggnlSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515743034 174 DSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:cd03254 171 DTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-202 |
4.60e-33 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 122.53 E-value: 4.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKQ-KFKALHDINFSVDKGEFVAIMGPSGSGKT----TLLNVISSiDSISGGTVEISGNEINQLSN 75
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 76 KKLAQFRKKELGFIFQD--YSVLPTLTVKENIMLPLSVQK-MKKDEMEKNYQDVTEALGIYDLSDK---YPSEISGGQQQ 149
Cdd:PRK09473 89 KELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515743034 150 RTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD 202
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-218 |
8.21e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.36 E-value: 8.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTkqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInQLSNKKLAQ 80
Cdd:COG1129 2 EPLLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 frkkELG--FIFQDYSVLPTLTVKENIML---PLSVQKMKKDEMEKNYQDVTEALGIyDLS-DKYPSEISGGQQQRTAAA 154
Cdd:COG1129 78 ----AAGiaIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 155 RAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKDG 218
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRlDEVFEIADRVTVLRDG 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-222 |
1.18e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.22 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEinqLSNKKLAQFR 82
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 KKeLGFIFQDysvlPT-----LTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAF 157
Cdd:PRK13650 81 HK-IGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 158 VHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDIHS 222
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVES 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-220 |
1.27e-32 |
|
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: 118.87 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 7 NHVSkiYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLsnkKLAQFRKKeL 86
Cdd:cd03253 4 ENVT--FAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRA-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 87 GFIFQDySVLPTLTVKENImlplsvQKMKKDEMEKNYQDVTEALGIYD----LSDKYPSE-------ISGGQQQRTAAAR 155
Cdd:cd03253 78 GVVPQD-TVLFNDTIGYNI------RYGRPDATDEEVIEAAKAAQIHDkimrFPDGYDTIvgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 156 AFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-220 |
1.56e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 118.55 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAq 80
Cdd:COG0410 1 MPMLEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 frKKELGFIFQDYSVLPTLTVKENIMLPLSVQKmKKDEMEKNYQDVtealgiYDLsdkYP----------SEISGGQQQR 150
Cdd:COG0410 77 --RLGIGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERV------YEL---FPrlkerrrqraGTLSGGEQQM 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 151 TAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAA-SFAQRVIMLKDGDI 220
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFAlEIADRAYVLERGRI 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-218 |
1.56e-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: 124.48 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFrkkeLGFIFQDYSVLPTlTV 101
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH----IGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENImlplsvQKMKKDEMEKnyqdVTEAL---GIYD----LSDKYPSEI-------SGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:COG4618 423 AENI------ARFGDADPEK----VVAAAklaGVHEmilrLPDGYDTRIgeggarlSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515743034 168 EPTGALDSKSAQDLLHRLEDMnKQFNSTIIMVTHDPSAASFAQRVIMLKDG 218
Cdd:COG4618 493 EPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-215 |
1.80e-32 |
|
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: 123.94 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklAQFRKKELGFIFQdysvLPTL 99
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSWRDQIAWVPQ----HPFL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 100 ---TVKENIMLPLSVQK--MKKDEMEKNY-QDVTEAL--GIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTG 171
Cdd:TIGR02857 408 fagTIAENIRLARPDASdaEIREALERAGlDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515743034 172 ALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIML 215
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-223 |
1.93e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.11 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RkkelgfifqdySVLP---TL----TVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAA 154
Cdd:PRK13548 78 R-----------AVLPqhsSLsfpfTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 155 RAFV------HQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSD 223
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVAD 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-220 |
2.19e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 123.64 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVS-KIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKT----TLLNVISSIDSISGGTVEISGNEINQLSN 75
Cdd:COG4172 4 MPLLSVEDLSvAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 76 KKLAQFRKKELGFIFQD--YSVLPTLTVKENIMLPLSV-QKMKKDEMEknyQDVTEAL---GIYDLS---DKYPSEISGG 146
Cdd:COG4172 84 RELRRIRGNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAAR---ARALELLervGIPDPErrlDAYPHQLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 147 QQQRTAAARAFVHQPSIIFADEPTGALD-SKSAQ--DLLHRLedmNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDvTVQAQilDLLKDL---QRELGMALLLITHDlGVVRRFADRVAVMRQGEI 235
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-223 |
4.41e-32 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 117.39 E-value: 4.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQfrk 83
Cdd:TIGR03864 2 LEVAGLSFRYGAR---RALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALAR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 keLGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:TIGR03864 76 --LGVVFQQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDIHSD 223
Cdd:TIGR03864 154 LLLDEPTVGLDPASRAAITAHVRALARDQGLSVLWATHLVDEIEASDRLVVLHRGRVLAD 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-220 |
4.51e-32 |
|
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: 116.99 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVIS---SIDSISGGTVEISGNEINQlsnkklAQFrKKELGFIFQDYSVL 96
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKP------DQF-QKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 97 PTLTVKENI--MLPLSVQKMKKDEMEKNYQDVT--EALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGA 172
Cdd:cd03234 94 PGLTVRETLtyTAILRLPRKSSDAIRKKRVEDVllRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515743034 173 LDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAASFA--QRVIMLKDGDI 220
Cdd:cd03234 174 LDSFTALNLVSTLSQLARR-NRIVILTIHQPRSDLFRlfDRILLLSSGEI 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-218 |
7.34e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.91 E-value: 7.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfrKKELGFIFQDysvlP-- 97
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV----RSKVGLVFQD----Pdd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 98 ---TLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALD 174
Cdd:PRK13647 91 qvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515743034 175 SKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:PRK13647 171 PRGQETLMEILDRLHNQ-GKTVIVATHDVDlAAEWADQVIVLKEG 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-218 |
1.17e-31 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 115.99 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIY-----GTKQkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEI--SGNEIN--Q 72
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKR-LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDlaQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 73 LSNKKLAQFRKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYD-LSDKYPSEISGGQQQRT 151
Cdd:COG4778 82 ASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPPATFSGGEQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 152 AAARAFVHQPSIIFADEPTGALDSKSAQ---DLLHRLedmnKQFNSTIIMVTHDPSA-ASFAQRVIMLKDG 218
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAvvvELIEEA----KARGTAIIGIFHDEEVrEAVADRVVDVTPF 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-223 |
1.36e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.99 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQKFKAlhdINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEIN---------QLS 74
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKG---VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 75 NKKLAQFRKKELGFIFQDYSVLPTLTVKENIM-LPLSVQKMKKDEMEKNYQDVTEALGIYDLS-DKYPSEISGGQQQRTA 152
Cdd:PRK10619 83 DKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 153 AARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSD 223
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGfARHVSSHVIFLHQGKIEEE 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-223 |
4.90e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.21 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRk 83
Cdd:COG4559 2 LEAENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 kelgfifqdySVLP-------TLTVKENIMLPLSVQKMKKDEmekNYQDVTEAL---GIYDLSDKYPSEISGGQQQRTAA 153
Cdd:COG4559 78 ----------AVLPqhsslafPFTVEEVVALGRAPHGSSAAQ---DRQIVREALalvGLAHLAGRSYQTLSGGEQQRVQL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 154 ARAFV-------HQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSD 223
Cdd:COG4559 145 ARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNlAAQYADRILLLHQGRLVAQ 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-220 |
7.77e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.50 E-value: 7.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 8 HVSKIYGTKQKF--KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEI-NQLSNKKLAQFRKK 84
Cdd:PRK13634 7 KVEHRYQYKTPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 85 eLGFIFQ-DYSVLPTLTVKENIML-PLSVqKMKKDEMEKNYQDVTEALGI-YDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:PRK13634 87 -VGIVFQfPEHQLFEETVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKGTV 224
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-220 |
9.09e-31 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 114.54 E-value: 9.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQKFKalhDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEI---SGN--EINQLSNK 76
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCR---DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAelELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 77 KLAQFRKKELGFIFQDysvlPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIY--------DLSDKYPSEISGGQQ 148
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQN----PRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWleeveidpTRIDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 149 QRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAAS-FAQRVIMLKDGDI 220
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRV 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-223 |
9.39e-31 |
|
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: 113.97 E-value: 9.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKQK-----------FK-------ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISG 67
Cdd:cd03267 3 VSNLSKSYRVYSKepgligslkslFKrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 68 NEINQLSNKKLAQFrkkelGFIF-QDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGG 146
Cdd:cd03267 83 LVPWKRRKKFLRRI-----GVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 147 QQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDIHSD 223
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-221 |
1.23e-30 |
|
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: 113.06 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKqkfKALHDINFSVDKGEFvAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKklaqFRK 83
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KeLGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03264 73 R-IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPS-AASFAQRVIMLKDGDIH 221
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-220 |
4.46e-30 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 112.32 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGtKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLsnkKLAQFRK 83
Cdd:cd03251 1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KeLGFIFQDySVLPTLTVKENIMLPlsvqkmKKDEMEKNYQDVTEALGIYDLSDKYP-----------SEISGGQQQRTA 152
Cdd:cd03251 77 Q-IGLVSQD-VFLFNDTVAENIAYG------RPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 153 AARAFVHQPSIIFADEPTGALDSKS---AQDLLHRLedmnkQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESerlVQAALERL-----MKNRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-218 |
5.21e-30 |
|
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: 111.22 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGneinqlsnKKLAQFRK 83
Cdd:cd03269 1 LEVENVTKRFGRVT---ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------KPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 164 IFADEPTGALDSKSaQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDG 218
Cdd:cd03269 150 LILDEPFSGLDPVN-VELLKDVIRELARAGKTVILSTHQmELVEELCDRVLLLNKG 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-223 |
7.67e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 111.71 E-value: 7.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIY-------------------GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTV 63
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 64 EISGnEINQLsnkkLaqfrkkELGFIFQdysvlPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTE--ALGIY-DLSDK-Y 139
Cdd:COG1134 84 EVNG-RVSAL----L------ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEfaELGDFiDQPVKtY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 140 PSeisgGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSA-ASFAQRVIMLKDG 218
Cdd:COG1134 148 SS----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAvRRLCDRAIWLEKG 222
|
....*
gi 515743034 219 DIHSD 223
Cdd:COG1134 223 RLVMD 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-223 |
8.89e-30 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 117.27 E-value: 8.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 17 QKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFrkkeLGFIFQDySVL 96
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRN----IGYVPQD-PRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 97 PTLTVKENIMLplSVQKMKKDEMeknyQDVTEALGIYDLSDKYPS-----------EISGGQQQRTAAARAFVHQPSIIF 165
Cdd:TIGR03375 551 FYGTLRDNIAL--GAPYADDEEI----LRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 166 ADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDIHSD 223
Cdd:TIGR03375 625 LDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLDLVDRIIVMDNGRIVAD 680
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-215 |
9.30e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.02 E-value: 9.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNeinqlsnkklaqfrkKELGFIFQDYSV---LP 97
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------------ARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 98 tLTVKENIML----PLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGAL 173
Cdd:NF040873 72 -LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515743034 174 DSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAASFAQRVIML 215
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-220 |
9.75e-30 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 116.69 E-value: 9.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVI---SSIDSISGGTVEISGNEINqlsnkklAQFRKKELGFIFQDYSVLPT 98
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPID-------AKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 99 LTVKENIM------LPLSVQKMKKDEMeknYQDVTEALGIYDLSD------KYPSEISGGQQQRTAAARAFVHQPSIIFA 166
Cdd:TIGR00955 114 LTVREHLMfqahlrMPRRVTKKEKRER---VDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 167 DEPTGALDSKSAQDLLHRLEDMnKQFNSTIIMVTHDPSAASFAQ--RVIMLKDGDI 220
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQPSSELFELfdKIILMAEGRV 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-220 |
1.08e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 112.00 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 13 YGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqfrkKELGFIFQD 92
Cdd:PRK10253 17 YG---KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 93 YSVLPTLTVKENIM------LPLSVQKMKKDEMEKNyqDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFA 166
Cdd:PRK10253 90 ATTPGDITVQELVArgryphQPLFTRWRKEDEEAVT--KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 167 DEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKI 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-223 |
1.41e-29 |
|
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: 110.70 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 13 YGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLsnkklaqfrkkELGFIFQd 92
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----------GLGGGFN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 93 ysvlPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGA 172
Cdd:cd03220 97 ----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515743034 173 LDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSA-ASFAQRVIMLKDGDIHSD 223
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSiKRLCDRALVLEKGKIRFD 223
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-220 |
1.86e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 110.54 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTT----LLNVISSIDSISGGTVEISGNEINQLSnkklaqFRKKELGFIFQD--YS 94
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNprTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 95 VLPTLTVK----ENIMLPLSVQKMKKDEM-----EKNYQDVTEALgiydlsDKYPSEISGGQQQRTAAARAFVHQPSIIF 165
Cdd:TIGR02770 75 FNPLFTMGnhaiETLRSLGKLSKQARALIlealeAVGLPDPEEVL------KKYPFQLSGGMLQRVMIALALLLEPPFLI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 166 ADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSA-ASFAQRVIMLKDGDI 220
Cdd:TIGR02770 149 ADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVvARIADEVAVMDDGRI 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-220 |
1.97e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.72 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNkkLAQFRKKElGFIFQ--DYSVLPT 98
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LWDIRNKA-GMVFQnpDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 99 LtVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSA 178
Cdd:PRK13633 102 I-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515743034 179 QDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-220 |
2.24e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 112.53 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYG-TKQKFKALHDINFSVDKGEFVAIMGPSGSGKT-TLLNVISSID---SISGGTVEISGNEINQLSN 75
Cdd:PRK11022 1 MALLNVDKLSVHFGdESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 76 KKLAQFRKKELGFIFQD--YSVLPTLTVKENIMLPLSV-QKMKKDEMEKNYQDVTEALGIYDLS---DKYPSEISGGQQQ 149
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 150 RTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQV 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-220 |
3.63e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 110.40 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGN-----EINQLSN 75
Cdd:PRK11701 4 QPLLSVRGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 76 KKLAQFRKKELGFIFQD--YSVLPTLTVKENIMLPLsvqkmkkdeM---EKNYQDVTEALGIY------DLS--DKYPSE 142
Cdd:PRK11701 81 AERRRLLRTEWGFVHQHprDGLRMQVSAGGNIGERL---------MavgARHYGDIRATAGDWlerveiDAAriDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 143 ISGGQQQRTAAARAFVHQPSIIFADEPTGALDSkSAQ----DLLHRLEdmnKQFNSTIIMVTHDPSAAS-FAQRVIMLKD 217
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVQarllDLLRGLV---RELGLAVVIVTHDLAVARlLAHRLLVMKQ 227
|
...
gi 515743034 218 GDI 220
Cdd:PRK11701 228 GRV 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-220 |
7.03e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 110.27 E-value: 7.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQKfKALHDINFSVDKGEFVAIMGPSGSGKTT---LLNVISSIDSISGGTVEISGNEINQlsnKKLA 79
Cdd:PRK13640 5 IVEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTA---KTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 80 QFRKKeLGFIFQDY-SVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFV 158
Cdd:PRK13640 81 DIREK-VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 159 HQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-220 |
1.00e-28 |
|
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: 108.38 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqfrK 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSH---ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNyqdvtealgIYDLsdkYP----------SEISGGQQQRTAA 153
Cdd:TIGR03410 75 AGIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDE---------IYEL---FPvlkemlgrrgGDLSGGQQQQLAI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 154 ARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:TIGR03410 143 ARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDfARELADRYYVMERGRV 210
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-242 |
1.01e-28 |
|
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: 108.73 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfrKKELGFIFQDySVLPTLT 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIMLPLSVQKMKKDEMEKNYQDVTEAlgIYDLSDKYP-------SEISGGQQQRTAAARAFVHQPSIIFADEPTGAL 173
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKLAGAHDF--ISELPEGYDtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 174 DSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDIHSD-IHQQSKTKSKFYNEIIQLQ 242
Cdd:cd03252 170 DYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQgSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-220 |
1.10e-28 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 107.69 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKklaqfrK 83
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTLTVKENIMLpLSVQKMKKDemeKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRL-LARLLGIRK---KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 164 IFADEPTGALDS---KSAQDLLHRLedmnKQFNSTIIMVTHDPSA-ASFAQRVIMLKDGDI 220
Cdd:cd03268 148 LILDEPTNGLDPdgiKELRELILSL----RDQGITVLISSHLLSEiQKVADRIGIINKGKL 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-242 |
1.52e-28 |
|
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: 108.40 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 7 NHVSKIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfRKKeL 86
Cdd:cd03249 4 KNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL---RSQ-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 87 GFIFQDysvlPTL---TVKENIMLPlsvqkmKKDEMEKNYQDVTEALGIYDLSDKYP-----------SEISGGQQQRTA 152
Cdd:cd03249 80 GLVSQE----PVLfdgTIAENIRYG------KPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 153 AARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI-HSDIHQQSKTK 231
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQNGQVvEQGTHDELMAQ 227
|
250
....*....|.
gi 515743034 232 SKFYNEIIQLQ 242
Cdd:cd03249 228 KGVYAKLVKAQ 238
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-220 |
1.97e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.28 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKELGFIFQDYSVLPTLT 100
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQD 180
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515743034 181 LLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEV 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-220 |
2.23e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.21 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 5 NVNHVSKIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGN------EINQLSNKKL 78
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 79 aqfrKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMK-KDEMEKNYQDVTEALG----IYDLSDKYPSEISGGQQQRTAA 153
Cdd:PRK14246 89 ----RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 154 ARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFnsTIIMVTHDP-SAASFAQRVIMLKDGDI 220
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPqQVARVADYVAFLYNGEL 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
9-218 |
2.53e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.76 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 9 VSKIY--GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEIN-QLSNKKLAQFRKKe 85
Cdd:PRK13641 8 VDYIYspGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLRKK- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 LGFIFQ-DYSVLPTLTVKENIML-PLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:PRK13641 87 VSLVFQfPEAQLFENTVLKDVEFgPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKDG 218
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVLVLEHG 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-236 |
4.45e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.55 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSIS-----GGTVEISGNEINQlSNK 76
Cdd:PRK14239 4 PILQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYS-PRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 77 KLAQFRKkELGFIFQDYSVLPtLTVKENIMLPLSVQKMK-KDEMEKNYQDVTEALGIYD-LSDK-YPSEI--SGGQQQRT 151
Cdd:PRK14239 80 DTVDLRK-EIGMVFQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIWDeVKDRlHDSALglSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 152 AAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFnsTIIMVTHDPSAAS-FAQRVIMLKDGdihsDIHQQSKT 230
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASrISDRTGFFLDG----DLIEYNDT 231
|
....*.
gi 515743034 231 KSKFYN 236
Cdd:PRK14239 232 KQMFMN 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-189 |
4.78e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.04 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQ 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 frkKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:COG1137 78 ---LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190
....*....|....*....|....*....|..
gi 515743034 161 PSIIFADEPTGALDSKSA---QDLLHRLEDMN 189
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVadiQKIIRHLKERG 186
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
5.36e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.53 E-value: 5.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQKFkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqf 81
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 rKKELGFIFQD-YSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:PRK13648 82 -RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDIH 221
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVY 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-219 |
6.19e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.44 E-value: 6.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEinqlsnkklaqfrkkELGFIFQD-YsvLPTLT 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA---------------RVLFLPQRpY--LPLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIMLPLSVQKMKKDEMEknyqDVTEALGIYDLSDKY------PSEISGGQQQRTAAARAFVHQPSIIFADEPTGALD 174
Cdd:COG4178 442 LREALLYPATAEAFSDAELR----EALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515743034 175 SKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGD 219
Cdd:COG4178 518 EENEAALYQLLREELP--GTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-202 |
1.05e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 108.26 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVS---KIYGTKQKF-------KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEIN 71
Cdd:PRK15079 7 VLLEVADLKvhfDIKDGKQWFwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 72 QLSNKKLAQFRKkELGFIFQD--YSVLPTLTVKENIMLPLSV--QKMKKDEMEKNYQDVTEALGIY-DLSDKYPSEISGG 146
Cdd:PRK15079 87 GMKDDEWRAVRS-DIQMIFQDplASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLpNLINRYPHEFSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 147 QQQRTAAARAFVHQPSIIFADEPTGALD-SKSAQdLLHRLEDMNKQFNSTIIMVTHD 202
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDvSIQAQ-VVNLLQQLQREMGLSLIFIAHD 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-220 |
1.28e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.72 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNeinQLSNKKLAQFR 82
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 KKeLGFIFQDY-SVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:PRK13642 81 RK-IGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-220 |
1.42e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.79 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIY--GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEI-NQLSNKKLAQ 80
Cdd:PRK13646 3 IRFDNVSYTYqkGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKeLGFIFQ-DYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGI-YDLSDKYPSEISGGQQQRTAAARAFV 158
Cdd:PRK13646 83 VRKR-IGMVFQfPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 159 HQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNeVARYADEVIVMKEGSI 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-213 |
3.28e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 105.62 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 24 DINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKeLGFIFQDYSVLPTLTVKE 103
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 104 NIMLPL------------SVQKMKkdemeknyqdvTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTG 171
Cdd:PRK11831 104 NVAYPLrehtqlpapllhSTVMMK-----------LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515743034 172 ALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFA--------QRVI 213
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDvPEVLSIAdhayivadKKIV 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-218 |
3.88e-27 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 103.70 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQK--FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNeinqlsnkklaqf 81
Cdd:cd03250 1 ISVEDASFTWDSGEQetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 rkkeLGFIFQdYSVLPTLTVKENIM--LPLSvqkmkkdemEKNYQDVTEA------LGIYDLSDKypSEI-------SGG 146
Cdd:cd03250 68 ----IAYVSQ-EPWIQNGTIRENILfgKPFD---------EERYEKVIKAcalepdLEILPDGDL--TEIgekginlSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 147 QQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDG 218
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-215 |
1.37e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKklaQF 81
Cdd:PRK10247 6 PLLQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RkKELGFIFQDysvlPTL---TVKENIMLPLSVQKMKKDemEKNYQDVTEALGIYD-LSDKYPSEISGGQQQRTAAARAF 157
Cdd:PRK10247 80 R-QQVSYCAQT----PTLfgdTVYDNLIFPWQIRNQQPD--PAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 158 VHQPSIIFADEPTGALDSKSAQ---DLLHRLedmNKQFNSTIIMVTHDPSAASFAQRVIML 215
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHnvnEIIHRY---VREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-220 |
2.83e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.68 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSI-----DSISGGTVEISGNEINQLSnkkLAQFRKKeLGFIFQDYS 94
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD---VIELRRR-VQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 95 VLPTLTVKENIMLPLSVQKMKKDEMEKnYQDVTEALG-------IYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:PRK14247 93 PIPNLSIFENVALGLKLNRLVKSKKEL-QERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515743034 168 EPTGALDSKSAQDLLHRLEDMNKQFnsTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQqAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-220 |
3.67e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.78 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQ--KFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEI----------SGNEI 70
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 71 NQLSNKKLAQFRK--KELGFIFQ--DYSVLPTlTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGI-YDLSDKYPSEISG 145
Cdd:PRK13631 101 TNPYSKKIKNFKElrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 146 GQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-218 |
5.02e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.62 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIY--GTKqkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqLSNKKLAQ 80
Cdd:PRK13636 5 ILKVEELNYNYsdGTH----ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKeLGFIFQDY-SVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVH 159
Cdd:PRK13636 80 LRES-VGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 160 QPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDG 218
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEG 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
5.95e-26 |
|
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: 105.65 E-value: 5.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQK--FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEIS-GNE-INQLSNKK 77
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 78 LAQFR-KKELGFIFQDYSVLPTLTVKEN------IMLPLSVQKMKKDEMEKNYQ-DVTEALGIYDlsdKYPSEISGGQQQ 149
Cdd:TIGR03269 358 DGRGRaKRYIGILHQEYDLYPHRTVLDNlteaigLELPDELARMKAVITLKMVGfDEEKAEEILD---KYPDELSEGERH 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 150 RTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDfVLDVCDRAALMRDGKI 506
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
6.34e-26 |
|
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: 99.81 E-value: 6.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIygtkqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNkklAQF 81
Cdd:cd03215 3 PVLEVRGLSVK-------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP---RDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKELGFIFQD---YSVLPTLTVKENIMLplsvqkmkkdemeknyqdvtealgiydlsdkyPSEISGGQQQRTAAARAFV 158
Cdd:cd03215 73 IRAGIAYVPEDrkrEGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 159 HQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-220 |
8.18e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 99.31 E-value: 8.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQKfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKklaqfRK 83
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSVLPTlTVKENIMLPLSvqkmkkdemeknyqdvtealgiydlsdkypseisGGQQQRTAAARAFVHQPSI 163
Cdd:cd03247 75 SLISVLNQRPYLFDT-TLRNNLGRRFS----------------------------------GGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
8.36e-26 |
|
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: 99.04 E-value: 8.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTkqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlAQFRK 83
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 keLGFIFQdysvlptltvkenimlplsvqkmkkdemeknyqdvtealgiydlsdkypseISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03216 77 --IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDeVFEIADRVTVLRDG 158
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-220 |
1.10e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.79 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQKFK--------ALHDINFSVDKGEFVAIMGPSGSGKTT----LLNVISSidsisGGTVEISGNE 69
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 70 INQLSNKKLAQFRKKeLGFIFQD-YSVL-PTLTVKENIMLPLSVQK--MKKDEMEKNYQDVTEALGI-YDLSDKYPSEIS 144
Cdd:PRK15134 349 LHNLNRRQLLPVRHR-IQVVFQDpNSSLnPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMEEVGLdPETRHRYPAEFS 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 145 GGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAA-SFAQRVIMLKDGDI 220
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVrALCHQVIVLRQGEV 504
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-218 |
1.99e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqfr 82
Cdd:PRK11231 2 TLRTENLTVGYGTK---RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 kKELGFIFQDYSVLPTLTVKENI------MLPLSVQKMKKDEmeknyQDVTEAL---GIYDLSDKYPSEISGGQQQRTAA 153
Cdd:PRK11231 76 -RRLALLPQHHLTPEGITVRELVaygrspWLSLWGRLSAEDN-----ARVNQAMeqtRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 154 ARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAAS-FAQRVIMLKDG 218
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASrYCDHLVVLANG 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-202 |
2.02e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.99 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKQKFKalhDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEinqlsnkklaqfrkkE 85
Cdd:COG0488 1 LENLSKSFGGRPLLD---DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL---------------R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 LGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNY----------------QDVTEALGIYDLS------------- 136
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVLDGDAELRALEAELEELEaklaepdedlerlaelQEEFEALGGWEAEaraeeilsglgfp 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 137 ----DKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSaqdlLHRLEDMNKQFNSTIIMVTHD 202
Cdd:COG0488 143 eedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYPGTVLVVSHD 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
2.86e-25 |
|
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: 103.59 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQKfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqf 81
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 rkKELGFIFQDYSVLPTlTVKENIMLPlsvqkmKKDEMEKNYQDVTEALGIYDLSDKYP-----------SEISGGQQQR 150
Cdd:TIGR02868 409 --RRVSVCAQDAHLFDT-TVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515743034 151 TAAARAFVHQPSIIFADEPTGALDSKSAQDLlhrLEDMNKQFNS-TIIMVTHDP 203
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADEL---LEDLLAALSGrTVVLITHHL 530
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-201 |
4.17e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.18 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTkqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInQLSNKKLAq 80
Cdd:COG3845 3 PPALELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 fRKKELGFIFQDYSVLPTLTVKENIML---PLSVQKMKKDEMEKNYQDVTEALGIY-DLsDKYPSEISGGQQQRTAAARA 156
Cdd:COG3845 78 -IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDvDP-DAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515743034 157 FVHQPSI-IFaDEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTH 201
Cdd:COG3845 156 LYRGARIlIL-DEPTAVLTPQEADELFEILRRLAAE-GKSIIFITH 199
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-220 |
5.56e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.00 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 25 INFSVDKGEFVAIMGPSGSGKTTLLNVissidsISG-----GTVEISGNEINQLSnkkLAQFRKKeLGFIFQDySVLPTL 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNA------LLGflpyqGSLKINGIELRELD---PESWRKH-LSWVGQN-PQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 100 TVKENIMLPlsvqkmKKDEMEKNYQDVTEALGIYDLSDKYP-----------SEISGGQQQRTAAARAFVHQPSIIFADE 168
Cdd:PRK11174 438 TLRDNVLLG------NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515743034 169 PTGALDSKSAQDLLHRLED-MNKQfnsTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAaSRRQ---TTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-220 |
8.82e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 100.72 E-value: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 36 AIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKELGFIFQDYSVLPTLTVKENIMLplsvqKMK 115
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRY-----GMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 116 KdEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNST 195
Cdd:PRK11144 103 K-SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
170 180 190
....*....|....*....|....*....|.
gi 515743034 196 IIMVTHdpsaaS------FAQRVIMLKDGDI 220
Cdd:PRK11144 182 ILYVSH-----SldeilrLADRVVVLEQGKV 207
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-220 |
1.18e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIY--GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEI-NQLSNKKLAQ 80
Cdd:PRK13649 3 INLQNVSYTYqaGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKeLGFIFQ-DYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIY-DLSDKYPSEISGGQQQRTAAARAFV 158
Cdd:PRK13649 83 IRKK-VGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743034 159 HQPSIIFADEPTGALDSKSAQDLLHRLEDMNkQFNSTIIMVTH--DpSAASFAQRVIMLKDGDI 220
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHlmD-DVANYADFVYVLEKGKL 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-227 |
1.67e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.65 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKELGFIFQ-DYSVLPT 98
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 99 LTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIY-DLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKS 177
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 178 AQDLLHRLEDMNkQFNSTIIMVTH-DPSAASFAQRVIMLKDGDI-----HSDIHQQ 227
Cdd:PRK13643 180 RIEMMQLFESIH-QSGQTVVLVTHlMDDVADYADYVYLLEKGHIiscgtPSDVFQE 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-207 |
1.86e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.99 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 13 YGTKQKFKalhDINFSVDKGEFVAIMGPSGSGKTTLLNVISSI-----DSISGGTVEISGNEInqLSNKKLAQFRKKELG 87
Cdd:PRK14267 14 YGSNHVIK---GVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDVDPIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 88 FIFQDYSVLPTLTVKENIMLPLSVQKM--KKDEMEKNYQDVTEALGIYD-----LSDkYPSEISGGQQQRTAAARAFVHQ 160
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDevkdrLND-YPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDMNKQFnsTIIMVTHDPSAAS 207
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAA 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-220 |
2.04e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.54 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKQ--KFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISS-IDSISGGTveISGNEINQLSNKKLAQFR 82
Cdd:PRK13645 9 LDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGlIISETGQT--IVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 --KKELGFIFQ--DYSVLPTLTVKENIMLPLSVQKMKkdemEKNYQDVTEALGIYDLSDKY----PSEISGGQQQRTAAA 154
Cdd:PRK13645 87 rlRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENK----QEAYKKVPELLKLVQLPEDYvkrsPFELSGGQKRRVALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 155 RAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-217 |
3.71e-24 |
|
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: 94.91 E-value: 3.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEinqlsnkklaqfrkkELGFIFQD-YsvLPTLT 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------DLLFLPQRpY--LPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIMLPLSvqkmkkdemeknyqdvtealgiydlsdkypSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDsksaQD 180
Cdd:cd03223 80 LREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EE 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 515743034 181 LLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKD 217
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-220 |
1.14e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.54 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 16 KQKFKALHDINFSVDKGEFVAIMGPSGSGKTT----LLNVISSidsiSGGTVEISGNEINQLSNKKLAQFRKkELGFIFQ 91
Cdd:PRK10261 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVES----QGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 92 D-YSVL-PTLTVKENIMLPLSVQKM-KKDEMEKNYQDVTEALGIY-DLSDKYPSEISGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:PRK10261 409 DpYASLdPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515743034 168 EPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAAS-FAQRVIMLKDGDI 220
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVErISHRVAVMYLGQI 542
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-204 |
2.48e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 96.19 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKQKF-------KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQL 73
Cdd:PRK11308 3 QPLLQAIDLKKHYPVKRGLfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 74 SNKKLAQFRKKeLGFIFQD-YSVL-PTLTVKENIMLPLSVQ-KMKKDEMEKNYQDVTEALGIY-DLSDKYPSEISGGQQQ 149
Cdd:PRK11308 83 DPEAQKLLRQK-IQIVFQNpYGSLnPRKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 150 RTAAARAFVHQPSIIFADEPTGALD-SKSAQdLLHRLEDMNKQFNSTIIMVTHDPS 204
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDvSVQAQ-VLNLMMDLQQELGLSYVFISHDLS 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-220 |
2.78e-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: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQKF------------------KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVE 64
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 65 ISGNEINQLSNKklaqFRKKeLGFIF-QDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEI 143
Cdd:COG4586 81 VLGYVPFKRRKE----FARR-IGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 144 SGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdIEALCDRVIVIDHGRI 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-218 |
3.59e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.18 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQlsnKKLAQFr 82
Cdd:COG4152 1 MLELKGLTKRFGDKT---AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRI- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 kkelGFifqdysvLP-------TLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAAR 155
Cdd:COG4152 74 ----GY-------LPeerglypKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743034 156 AFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKDG 218
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQmELVEELCDRIVIINKG 205
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-235 |
3.68e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 8 HVSKIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfrKKELG 87
Cdd:TIGR00958 483 DVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 88 FIFQDySVLPTLTVKENIMLPLsvQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEI-------SGGQQQRTAAARAFVHQ 160
Cdd:TIGR00958 559 LVGQE-PVLFSGSVRENIAYGL--TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVgekgsqlSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 161 PSIIFADEPTGALDSKSAQdllhRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI-HSDIHQQSKTKSKFY 235
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVvEMGTHKQLMEDQGCY 707
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-202 |
2.61e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.98 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQf 81
Cdd:PRK11300 4 PLLSVSGLMMRFG---GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 rkkeLGFI--FQDYSVLPTLTVKENIMLP-------------LSVQKMKKDEMEKNYQDVT--EALGIYDLSDKYPSEIS 144
Cdd:PRK11300 80 ----MGVVrtFQHVRLFREMTVIENLLVAqhqqlktglfsglLKTPAFRRAESEALDRAATwlERVGLLEHANRQAGNLA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 145 GGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD 202
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
2.68e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.52 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQ 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDT---TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 frkkELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEM-EKNYQDVTEAL---GIYDLSDKYPSEISGGQQQRTAAARA 156
Cdd:PRK09536 78 ----RVASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWtETDRAAVERAMertGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 157 FVHQPSIIFADEPTGALDSKSA---QDLLHRLEDMNKqfnsTIIMVTHDPS-AASFAQRVIMLKDGDIH 221
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQvrtLELVRRLVDDGK----TAVAAIHDLDlAARYCDELVLLADGRVR 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-218 |
4.37e-22 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 90.40 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 15 TKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISsidSISGGTVEISGN-EINQLSNKKLAQFRKKELGFIFQDY 93
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA---NRTEGNVSVEGDiHYNGIPYKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 94 SVLPTLTVKENIMLPLSVQkmkkdemeknyqdvtealgiydlSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGAL 173
Cdd:cd03233 93 VHFPTLTVRETLDFALRCK-----------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515743034 174 DSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQ--RVIMLKDG 218
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLfdKVLVLYEG 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-219 |
7.84e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.15 E-value: 7.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 16 KQKFKALHDINFSVDKGEFVAIMGPSGSGKT-TLLNVISSIDSiSGGTVEISGN----------EINQLSNKKLAQFRKK 84
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 85 ELGFIFQD--YSVLPTLTVKENIMLPLSV-QKMKKDEMEKNYQDVTEALGIYD---LSDKYPSEISGGQQQRTAAARAFV 158
Cdd:PRK10261 105 DMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 159 HQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGD 219
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGE 246
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-220 |
8.01e-22 |
|
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: 90.22 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 9 VSKIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfrKKELGF 88
Cdd:cd03248 17 VTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 89 IFQDySVLPTLTVKENIMLPL---SVQKMKKDEMEKNYQDVTE--ALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03248 93 VGQE-PVLFARSLQDNIAYGLqscSFECVKEAAQKAHAHSFISelASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 164 IFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
1.28e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.63 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKQKfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQ 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FrkkeLGFIFQ--DYSVLPTlTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFV 158
Cdd:PRK13652 79 F----VGLVFQnpDDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 159 HQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRI 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-221 |
1.92e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQKFKalhDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISgneinqlsnKKLaqf 81
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLD---DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------ETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 rkkELGFIFQDYSVL-PTLTVKENImlplsvqkmkKDEMEKNY-QDVTEALGIYDLS----DKYPSEISGGQQQRTAAAR 155
Cdd:COG0488 379 ---KIGYFDQHQEELdPDKTVLDEL----------RDGAPGGTeQEVRGYLGRFLFSgddaFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 156 AFVHQPSIIFADEPTGALDSKSaqdlLHRLEDMNKQFNSTIIMVTHDPSA-ASFAQRVIMLKDGDIH 221
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDRYFlDRVATRILEFEDGGVR 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-220 |
3.96e-21 |
|
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: 91.79 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 19 FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDS---ISG------------GTVEIS----------GNEINQ- 72
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyepTSGriiyhvalcekcGYVERPskvgepcpvcGGTLEPe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 73 ------LSNKKLAQFRKKeLGFIFQ-DYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISG 145
Cdd:TIGR03269 93 evdfwnLSDKLRRRIRKR-IAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 146 GQQQRTAAARAFVHQPSIIFADEPTGALDSKSAqDLLHR-LEDMNKQFNSTIIMVTHDPSA-ASFAQRVIMLKDGDI 220
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA-KLVHNaLEEAVKASGISMVLTSHWPEViEDLSDKAIWLENGEI 247
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-220 |
5.56e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.56 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 7 NHVSKIYGTKQKfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfrKKEL 86
Cdd:PRK13657 338 DDVSFSYDNSRQ--GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 87 GFIFQDySVLPTLTVKENIMLPlsvqkmKKDEMEKNYQDVTEALGIYDLSDKYP-----------SEISGGQQQRTAAAR 155
Cdd:PRK13657 412 AVVFQD-AGLFNRSIEDNIRVG------RPDATDEEMRAAAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 156 AFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-218 |
1.33e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 90.32 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 32 GEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNeinqlsNKKLAQFRKKELGFIFQDYSVLPTLTVKENIM----- 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILAN------NRKPTKQILKRTGFVTQDDILYPHLTVRETLVfcsll 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 107 -LPLSvqkMKKDEMEKNYQDVTEALGIYD-----LSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQD 180
Cdd:PLN03211 168 rLPKS---LTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515743034 181 LLHRLEDMnKQFNSTIIMVTHDPSAASFA--QRVIMLKDG 218
Cdd:PLN03211 245 LVLTLGSL-AQKGKTIVTSMHQPSSRVYQmfDSVLVLSEG 283
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-181 |
2.31e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.49 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkLAQ 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKELGFIFQDYSVLPTLTVKENIMLPLSVQK-MKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVH 159
Cdd:PRK10895 75 RARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180
....*....|....*....|..
gi 515743034 160 QPSIIFADEPTGALDSKSAQDL 181
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDI 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-202 |
2.81e-20 |
|
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: 89.22 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQKFkaLHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSisggtvEISGNEINQLSNKklaqfr 82
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------DFNGEARPQPGIK------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 kkeLGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNY--------------------QDVTEALGIYDLS------ 136
Cdd:TIGR03719 70 ---VGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISakyaepdadfdklaaeqaelQEIIDAADAWDLDsqleia 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 137 ---------DKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLedmnKQFNSTIIMVTHD 202
Cdd:TIGR03719 147 mdalrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-218 |
5.59e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIY-GTKQKFKALHDINFSVDKGEFVAIMGPSGSGKT-TLLNVISSIDS----ISGGTVEISGNEINQLS 74
Cdd:PRK15134 3 QPLLAIENLSVAFrQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 75 NKKLAQFRKKELGFIFQD--YSVLPTLTVKENIMLPLSVQK-MKKDEMEKNYQDVTEALGIYD----LSDkYPSEISGGQ 147
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRgMRREAARGEILNCLDRVGIRQaakrLTD-YPHQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 148 QQRTAAARAFVHQPSIIFADEPTGALD-SKSAQdLLHRLEDMNKQFNSTIIMVTHDPSAA-SFAQRVIMLKDG 218
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDvSVQAQ-ILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNG 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-211 |
7.85e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 84.33 E-value: 7.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 25 INFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQlsnkkLAQFRKKELGFIFQDYSVLPTLTVKEN 104
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-----QRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 105 imlpLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDsKSAQDLLHR 184
Cdd:TIGR01189 94 ----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-KAGVALLAG 168
|
170 180
....*....|....*....|....*..
gi 515743034 185 LEDMNKQFNSTIIMVTHDPSAASFAQR 211
Cdd:TIGR01189 169 LLRAHLARGGIVLLTTHQDLGLVEARE 195
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-220 |
9.76e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.93 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNkklAQ 80
Cdd:PRK11614 3 KVMLSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT---AK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKELGFIFQDYSVLPTLTVKENIMLP--LSVQKMKKDEMEKNYQDVTEalgIYDLSDKYPSEISGGQQQRTAAARAFV 158
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEENLAMGgfFAERDQFQERIKWVYELFPR---LHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 159 HQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAA-SFAQRVIMLKDGDI 220
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQAlKLADRGYVLENGHV 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-207 |
1.58e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.83 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSI-DSISG----GTVEISGNEINQlSNKK 77
Cdd:PRK14243 10 VLRTENLNVYYG---SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLnDLIPGfrveGKVTFHGKNLYA-PDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 78 LAQFRKKeLGFIFQDYSVLPTlTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYP---SEISGGQQQRTAAA 154
Cdd:PRK14243 86 PVEVRRR-IGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDELVERSLRQAALWDEVKDKLKqsgLSLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 155 RAFVHQPSIIFADEPTGALDSKSA---QDLLHRLEdmnKQFnsTIIMVTHDPSAAS 207
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTlriEELMHELK---EQY--TIIIVTHNMQQAA 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-202 |
1.82e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 81.73 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQKFKalhDINFSVDKGEFVAIMGPSGSGKTTLLNVissidsISGGTVEISGnEINQLSNKKLAQFrk 83
Cdd:cd03221 1 IELENLSKTYGGKLLLK---DISLTINPGDRIGLVGRNGAGKSTLLKL------IAGELEPDEG-IVTWGSTVKIGYF-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 kelgfifqdysvlptltvkenimlplsvqkmkkdemeknyqdvtealgiydlsdkypSEISGGQQQRTAAARAFVHQPSI 163
Cdd:cd03221 69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*....
gi 515743034 164 IFADEPTGALDSKSAQdllhRLEDMNKQFNSTIIMVTHD 202
Cdd:cd03221 92 LLLDEPTNHLDLESIE----ALEEALKEYPGTVILVSHD 126
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-218 |
2.06e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF 81
Cdd:PRK09700 4 PYISMAGIGKSFGPVH---ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 rkkELGFIFQDYSVLPTLTVKENIM---LP----LSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAA 154
Cdd:PRK09700 81 ---GIGIIYQELSVIDELTVLENLYigrHLtkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 155 RAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKDG 218
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-220 |
2.09e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkKLAQFRKKeLGFIFQD-YSVLPTL 99
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKL-VGIVFQNpETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 100 TVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQ 179
Cdd:PRK13644 94 TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515743034 180 DLLHRLEDMNKQfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK13644 174 AVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-218 |
2.85e-19 |
|
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: 82.68 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 16 KQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISS--IDSISGGTVEISGNEINQlsnkklaQFRkKELGFIFQDY 93
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDK-------NFQ-RSTGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 94 SVLPTLTVKENIMlplsvqkmkkdemeknYQDVTEALGIYdlsdkypseisggQQQRTAAARAFVHQPSIIFADEPTGAL 173
Cdd:cd03232 89 VHSPNLTVREALR----------------FSALLRGLSVE-------------QRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515743034 174 DSKSAQDLLHRLedmNKQFNS--TIIMVTHDPSAASFAQ--RVIMLKDG 218
Cdd:cd03232 140 DSQAAYNIVRFL---KKLADSgqAILCTIHQPSASIFEKfdRLLLLKRG 185
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-251 |
4.06e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.99 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 36 AIMGPSGSGKTTLLNVISSI-DSISG----GTVEISGNEInqLSNKKLAQFRKKeLGFIFQDYSVLPtLTVKENIMLPLS 110
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMnDKVSGyrysGDVLLGGRSI--FNYRDVLEFRRR-VGMLFQRPNPFP-MSIMDNVLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 111 VQKMKKdemEKNYQDVTEA----LGIYD-----LSDKyPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDL 181
Cdd:PRK14271 127 AHKLVP---RKEFRGVAQArlteVGLWDavkdrLSDS-PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 182 LHRLEDMNKQFnsTIIMVTHD-PSAASFAQRVIMLKDGDIHSDIHQQSKTKSKFYNEIIQLQSALGGVAND 251
Cdd:PRK14271 203 EEFIRSLADRL--TVIIVTHNlAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGDVKD 271
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-201 |
9.79e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 9.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLsnkklAQF 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-----ARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTH 201
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTH 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-218 |
1.25e-18 |
|
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: 84.49 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTkqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSI--DSISGGTVEISGNEinqLSNKKLAQ 80
Cdd:TIGR02633 1 LLEMKGIVKTFGG---VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSP---LKASNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 FRKKELGFIFQDYSVLPTLTVKENIML----PLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYP-SEISGGQQQRTAAAR 155
Cdd:TIGR02633 75 TERAGIVIIHQELTLVPELSVAENIFLgneiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743034 156 AFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMnKQFNSTIIMVTHD-PSAASFAQRVIMLKDG 218
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKlNEVKAVCDTICVIRDG 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-202 |
1.38e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 83.42 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVS-KIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDS----ISGGTVEISGNEINQLSN 75
Cdd:COG4170 1 MPLLDIRNLTiEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 76 KKLAQFRKKELGFIFQD-YSVL-PTLTVKENIM--LPLSVQK---------MKKDEME-------KNYQDVTEAlgiydl 135
Cdd:COG4170 81 RERRKIIGREIAMIFQEpSSCLdPSAKIGDQLIeaIPSWTFKgkwwqrfkwRKKRAIEllhrvgiKDHKDIMNS------ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 136 sdkYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD 202
Cdd:COG4170 155 ---YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-201 |
1.68e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 9 VSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqlSNKKLAQFRkkeLGF 88
Cdd:PRK13536 47 VSKSYGDK---AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARAR---IGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 89 IFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADE 168
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190
....*....|....*....|....*....|...
gi 515743034 169 PTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTH 201
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLAR-GKTILLTTH 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-220 |
1.76e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIygtkqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNkklAQF 81
Cdd:COG1129 255 VVLEVEGLSVG-------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSP---RDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKELGFIFQD---YSVLPTLTVKENIMLPlSVQK------MKKDEMEKNYQDVTEALGIydlsdKYPS------EISGG 146
Cdd:COG1129 325 IRAGIAYVPEDrkgEGLVLDLSIRENITLA-SLDRlsrgglLDRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 147 QQQRTAAARAFVHQPSIIFADEPT-----GAldsKSA-QDLLHRLEDMNKqfnsTIIMVTHD-PSAASFAQRVIMLKDGD 219
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTrgidvGA---KAEiYRLIRELAAEGK----AVIVISSElPELLGLSDRILVMREGR 471
|
.
gi 515743034 220 I 220
Cdd:COG1129 472 I 472
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-201 |
1.95e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIY-GTKqkfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInQLSNKKLA 79
Cdd:PRK11288 2 SPYLSFDGIGKTFpGVK----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 80 QfrkkELG--FIFQDYSVLPTLTVKENIML---PLSVQKMKKDEMEKNYQDVTEALGIyDLSDKYP-SEISGGQQQRTAA 153
Cdd:PRK11288 77 L----AAGvaIIYQELHLVPEMTVAENLYLgqlPHKGGIVNRRLLNYEAREQLEHLGV-DIDPDTPlKYLSIGQRQMVEI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515743034 154 ARAFVHQPSIIFADEPTGALDSKSAQDL---LHRLEDMNKqfnsTIIMVTH 201
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLfrvIRELRAEGR----VILYVSH 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-218 |
1.98e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 25 INFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSiSGGTVEISGNEINQLSNKKLAQFRkkelGFIFQDYSVLPTLTVKEN 104
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 105 IMLPLSvQKMKKDEMEKNYQDVTEALGiydLSDKYP---SEISGGQQQRTAAARAF--VHqPSI------IFADEPTGAL 173
Cdd:COG4138 90 LALHQP-AGASSEAVEQLLAQLAEALG---LEDKLSrplTQLSGGEWQRVRLAAVLlqVW-PTInpegqlLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515743034 174 D--SKSAQD-LLHRLedmnKQFNSTIIMVTHDPS-AASFAQRVIMLKDG 218
Cdd:COG4138 165 DvaQQAALDrLLREL----CQQGITVVMSSHDLNhTLRHADRVWLLKQG 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-245 |
2.16e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.99 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQKfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLsnkKLAQFR 82
Cdd:PRK10789 313 ELDVNIRQFTYPQTDH-PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 KK-----ELGFIFQDysvlptlTVKENIML--PLSVQkmkkDEMEKNYQDVTEALGIYDLSDKYPSEI-------SGGQQ 148
Cdd:PRK10789 389 SRlavvsQTPFLFSD-------TVANNIALgrPDATQ----QEIEHVARLASVHDDILRLPQGYDTEVgergvmlSGGQK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 149 QRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfnSTIIMVTHDPSAASFAQRVIMLKDGDI-HSDIHQQ 227
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTEASEILVMQHGHIaQRGNHDQ 535
|
250 260
....*....|....*....|.
gi 515743034 228 SKTKSKFYNEII---QLQSAL 245
Cdd:PRK10789 536 LAQQSGWYRDMYryqQLEAAL 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-174 |
2.58e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSkiYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInqlSNKKLAQF 81
Cdd:COG3845 256 VVLEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI---TGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKELGFIFQD---YSVLPTLTVKENIMLPLSVQK-------MKKDEMEKNYQDVTEALGIydlsdKYPSE------ISG 145
Cdd:COG3845 331 RRLGVAYIPEDrlgRGLVPDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDV-----RTPGPdtparsLSG 405
|
170 180
....*....|....*....|....*....
gi 515743034 146 GQQQRTAAARAFVHQPSIIFADEPTGALD 174
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-220 |
3.44e-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: 80.23 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfRKKeLGFIFQDysvlPTL- 99
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---RSR-ISIIPQD----PVLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 100 --TVKENIMlPLSvqkMKKDEMeknYQDVTEALGIYDLSDKYP-----------SEISGGQQQRTAAARAFVHQPSIIFA 166
Cdd:cd03244 91 sgTIRSNLD-PFG---EYSDEE---LWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515743034 167 DEPTGALDSKSAQdLLHRLEdMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:cd03244 164 DEATASVDPETDA-LIQKTI-REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-220 |
6.04e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.57 E-value: 6.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYgTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQfrk 83
Cdd:PRK11160 339 LTLNNVSFTY-PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 kELGFIFQDYSVLPTlTVKENIMLPlsvqkmKKDEMEKNYQDVTEALGIYDLSDKYPS----------EISGGQQQRTAA 153
Cdd:PRK11160 415 -AISVVSQRVHLFSA-TLRDNLLLA------APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 154 ARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-202 |
8.41e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.08 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISG-----GTVEISGNEINQlSN 75
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE-RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 76 KKLAQFRKkELGFIFQDYSVLPtLTVKENIMLPLSV----QKMKKDEMeknyqdVTEALGIYDLSD-------KYPSEIS 144
Cdd:PRK14258 81 VNLNRLRR-QVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrPKLEIDDI------VESALKDADLWDeikhkihKSALDLS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515743034 145 GGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD 202
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-201 |
1.94e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTkqkFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSI--DSISGGTVEISGNEInQLSNKKL 78
Cdd:PRK13549 3 EYLLEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEEL-QASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 79 AQfrKKELGFIFQDYSVLPTLTVKENIML---PLSVQKMKKDEMEKNYQDVTEALGIyDLSDKYP-SEISGGQQQRTAAA 154
Cdd:PRK13549 79 TE--RAGIAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKL-DINPATPvGNLGLGQQQLVEIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515743034 155 RAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMnKQFNSTIIMVTH 201
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISH 201
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-244 |
2.47e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.92 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQKfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQfrk 83
Cdd:PRK10790 341 IDIDNVSFAYRDDNL--VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 kELGFIFQDYSVLPTlTVKENIMLplsvqkmKKDEMEKNYQDVTEALGIYDLSDKYPSEI-----------SGGQQQRTA 152
Cdd:PRK10790 416 -GVAMVQQDPVVLAD-TFLANVTL-------GRDISEEQVWQALETVQLAELARSLPDGLytplgeqgnnlSVGQKQLLA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 153 AARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfnSTIIMVTHDPSAASFAQRVIMLKDGD-IHSDIHQQSKTK 231
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQaVEQGTHQQLLAA 564
|
250
....*....|...
gi 515743034 232 SKFYNEIIQLQSA 244
Cdd:PRK10790 565 QGRYWQMYQLQLA 577
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-220 |
3.20e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.68 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKI--YGT----KQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNeinQLSNK 76
Cdd:PRK15112 4 LLEVRNLSKTfrYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 77 KLAqFRKKELGFIFQD--YSVLPTLTVKENIMLPLSVQ-KMKKDEMEKNYQDVTEALGIY-DLSDKYPSEISGGQQQRTA 152
Cdd:PRK15112 81 DYS-YRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 153 AARAFVHQPSIIFADEPTGALD-SKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDmSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-220 |
4.40e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKQKFKAlhdINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQf 81
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKG---IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 rkkeLG--FIFQDYSVLPTLTVKENIMLPLSvqkmKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVH 159
Cdd:PRK15439 86 ----LGiyLVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 160 QPSIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-220 |
6.04e-17 |
|
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: 79.86 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfrKKELGFIFQDySVLPTLTV 101
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQD-TVLFNDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIML--PLSVQkmkkDEMEknyqDVTEALGIYD----LSDKYPSEI-------SGGQQQRTAAARAFVHQPSIIFADE 168
Cdd:COG5265 449 AYNIAYgrPDASE----EEVE----AAARAAQIHDfiesLPDGYDTRVgerglklSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515743034 169 PTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:COG5265 521 ATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRI 570
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-217 |
1.16e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.30 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 13 YGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEIsgNEINQLSNKKLAQFRKKeLGFIFQD 92
Cdd:PTZ00265 392 YDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSK-IGVVSQD 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 93 ySVLPTLTVKENIM----------------------------------------LPLSVQKMKKDE---MEKNYQ----- 124
Cdd:PTZ00265 469 -PLLFSNSIKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcagdLNDMSNTTDSNElieMRKNYQtikds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 125 ---DVTEALGIYD----LSDKY-------PSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNK 190
Cdd:PTZ00265 548 evvDVSKKVLIHDfvsaLPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
250 260
....*....|....*....|....*..
gi 515743034 191 QFNSTIIMVTHDPSAASFAQRVIMLKD 217
Cdd:PTZ00265 628 NENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-203 |
1.18e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.15 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 17 QKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVIssidsisggtveisgneINQLSNKKLAQFRKKELGFIFQDYSVL 96
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-----------------AGALKGTPVAGCVDVPDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 97 ptltvkENIMLPLSVQkmkkdemeknyqDVTEALGIYDLSDKY-----PSEISGGQQQRTAAARAFVHQPSIIFADEPTG 171
Cdd:COG2401 104 ------DAIGRKGDFK------------DAVELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|..
gi 515743034 172 ALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDP 203
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-220 |
1.65e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.52 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQKfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLsnkKLAQFRK 83
Cdd:PRK11176 342 IEFRNVTFTYPGKEV-PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY---TLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 K-----ELGFIFQDysvlptlTVKENIMLPlSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEI-------SGGQQQRT 151
Cdd:PRK11176 418 QvalvsQNVHLFND-------TIANNIAYA-RTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIgengvllSGGQRQRI 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 152 AAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-216 |
2.08e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQF--RKKELGFIFqdysvlPT 98
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpQSEEVDWSF------PV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 99 LTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSD---KYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDS 175
Cdd:PRK15056 96 LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEfrhRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515743034 176 KSAQ---DLLHRLEDMNKqfnsTIIMVTHD-PSAASFAQRVIMLK 216
Cdd:PRK15056 176 KTEAriiSLLRELRDEGK----TMLVSTHNlGSVTEFCDYTVMVK 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-220 |
6.62e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.33 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDS--ISGGTVEISGNEINQLSNKKLAqfrKKELGFIFQDYSVLPTL 99
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERA---RAGIFLAFQYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 100 TVKEniMLPLSVQKMKKDEM-----EKNYQDVTEALGI-YDLSDKYPSE-ISGGQQQRTAAARAFVHQPSIIFADEPTGA 172
Cdd:COG0396 93 SVSN--FLRTALNARRGEELsarefLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 173 LDSKSAQDLLHRLEDMNKQfNSTIIMVTH--------DPSaasfaqRVIMLKDGDI 220
Cdd:COG0396 171 LDIDALRIVAEGVNKLRSP-DRGILIITHyqrildyiKPD------FVHVLVDGRI 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-202 |
7.31e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGneinqlsnkklaq 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 frKKELGFIFQDYSVLPT--LTVKENIMLPLSVQKmkkdemeknyQDVTEALGIYD---LSDKYPSEISGGQQQRTAAAR 155
Cdd:PRK09544 66 --KLRIGYVPQKLYLDTTlpLTVNRFLRLRPGTKK----------EDILPALKRVQaghLIDAPMQKLSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515743034 156 AFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD 202
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-218 |
9.75e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.30 E-value: 9.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 29 VDKGEFVAIMGPSGSGKTTLLNVIS---SIDSISGGTVEISGNEINqlsnkklAQFRKKeLGFIFQDYSVLPTLTVKENI 105
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLD-------SSFQRS-IGYVQQQDLHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 106 M------LPLSVQKMKKDEmeknYQD-VTEALGIYDLSDKYPSEISGG----QQQRTAAARAFVHQP-SIIFADEPTGAL 173
Cdd:TIGR00956 858 RfsaylrQPKSVSKSEKME----YVEeVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPkLLLFLDEPTSGL 933
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515743034 174 DSKSAQ---DLLHRLEDMNKqfnsTIIMVTHDPSAASFAQ--RVIMLKDG 218
Cdd:TIGR00956 934 DSQTAWsicKLMRKLADHGQ----AILCTIHQPSAILFEEfdRLLLLQKG 979
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-221 |
1.42e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.21 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQlsnkKLAQFRKkELGFIFQDYSVLPTLT 100
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQ-SLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALD---SKS 177
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpysRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515743034 178 AQDLLhrledMNKQFNSTIIMVTHDPSAAS-FAQRVIMLKDGDIH 221
Cdd:TIGR01257 1100 IWDLL-----LKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLY 1139
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-220 |
1.52e-15 |
|
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: 72.83 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInqlSNKKLAQFRKKeLGFIFQDysvlPTL 99
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSS-LTIIPQD----PTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 100 ---TVKENimlpLSVQKMKKDEmeknyqDVTEALGIYDLSdkypSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSK 176
Cdd:cd03369 94 fsgTIRSN----LDPFDEYSDE------EIYGALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515743034 177 S---AQDLLHrlEDMNkqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:cd03369 160 TdalIQKTIR--EEFT---NSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-203 |
4.64e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFrkkeLGfiFQDySVLPTLTV 101
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY----LG--HRN-AMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIML--------PLSVqkmkkdemeknyQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGAL 173
Cdd:PRK13539 91 AENLEFwaaflggeELDI------------AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 515743034 174 DSkSAQDLL-----HRLEDmnkqfNSTIIMVTHDP 203
Cdd:PRK13539 159 DA-AAVALFaelirAHLAQ-----GGIVIAATHIP 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-220 |
8.22e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 15 TKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqfrKKELGFIFQ--- 91
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAV---KKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 92 DYSVLPTLTVKENIMLPLSVQKMK--------KDEMEKNY-QDVTEALGIYDLS-DKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:PRK09700 349 DNGFFPNFSIAQNMAISRSLKDGGykgamglfHEVDEQRTaENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 162 SIIFADEPTGALDSKSAQD---LLHRLEDMNKqfnsTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEiykVMRQLADDGK----VILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-202 |
1.22e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.84 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 7 NHVSKIYGTKQKFkaLHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEIS-GNEInqlsnkklaqfrkke 85
Cdd:PRK11819 10 NRVSKVVPPKKQI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 86 lGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNY--------------------QDVTEALGIYDL---------- 135
Cdd:PRK11819 73 -GYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIYaayaepdadfdalaaeqgelQEIIDAADAWDLdsqleiamda 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 136 -----SDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDmnkqFNSTIIMVTHD 202
Cdd:PRK11819 152 lrcppWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD----YPGTVVAVTHD 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-223 |
3.29e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISG--------GTVEISGNEINQLSNKKLAQFRkkelgfifqdy 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLR----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 94 SVLP-------TLTVKENIMLPLSVQKMKKDEMEKNYQDVT-EALGIYD---LSDKYPSEISGGQQQRTAAARAFVH--- 159
Cdd:PRK13547 86 AVLPqaaqpafAFSAREIVLLGRYPHARRAGALTHRDGEIAwQALALAGataLVGRDVTTLSGGELARVQFARVLAQlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743034 160 ------QPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHSD 223
Cdd:PRK13547 166 phdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAH 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-215 |
3.68e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 23 HDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkklAQFRkKELGFIFQDYSVLPTLTVK 102
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR----DEYH-QDLLYLGHQPGIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 103 ENIMLPLSVQKMKKDEmeknyqDVTEAL------GIYDLSDKYpseISGGQQQRTAAARAFVHQPSIIFADEPTGALDSK 176
Cdd:PRK13538 93 ENLRFYQRLHGPGDDE------ALWEALaqvglaGFEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515743034 177 SAQDLLHRLEDMNKQfNSTIIMVTHDP-SAASFAQRVIML 215
Cdd:PRK13538 164 GVARLEALLAQHAEQ-GGMVILTTHQDlPVASDKVRKLRL 202
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-222 |
1.08e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 25 INFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSiSGGTVEISGNEINQLSNKKLAQFRkkelGFIFQDYSVLPTLTVKEn 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 105 iMLPLSV-QKMKKDEMEKNYQDVTEALGiydLSDKYPSEI---SGGQQQRTAAARAF--VHqPSI------IFADEPTGA 172
Cdd:PRK03695 89 -YLTLHQpDKTRTEAVASALNEVAEALG---LDDKLGRSVnqlSGGEWQRVRLAAVVlqVW-PDInpagqlLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515743034 173 LD--SKSAQDLLhrLEDMNKQfNSTIIMVTHDPS-AASFAQRVIMLKDGDIHS 222
Cdd:PRK03695 164 LDvaQQAALDRL--LSELCQQ-GIAVVMSSHDLNhTLRHADRVWLLKQGKLLA 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-220 |
1.16e-13 |
|
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: 70.36 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLN-VISSIDSISGgTVEISGNeinqlsnkklaqfrkkeLGFIFQDySVLPTLT 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEG-HVHMKGS-----------------VAYVPQQ-AWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIMLPLSVQkmkkdemEKNYQDVTEALGIYDLSDKYPS-----------EISGGQQQRTAAARAFVHQPSIIFADEP 169
Cdd:TIGR00957 715 LRENILFGKALN-------EKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515743034 170 TGALDSKSAQDLL-HRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:TIGR00957 788 LSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-203 |
1.72e-13 |
|
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: 67.13 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 25 INFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVeisgneinQLSNKKLAQFR---KKELGFIFQDYSVLPTLTV 101
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV--------LLNGGPLDFQRdsiARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENImlplsvQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDL 181
Cdd:cd03231 91 LENL------RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|..
gi 515743034 182 LHRLEDMNKQfNSTIIMVTHDP 203
Cdd:cd03231 165 AEAMAGHCAR-GGMVVLTTHQD 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-173 |
1.81e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqLSNKKLAQfrKKELGFIFQDYSVLPTL 99
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNGPKSSQ--EAGIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 100 TVKENIMLPLS-VQKMKKDEMEKNYQdvtEA------LGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGA 172
Cdd:PRK10762 95 TIAENIFLGREfVNRFGRIDWKKMYA---EAdkllarLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
.
gi 515743034 173 L 173
Cdd:PRK10762 172 L 172
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-220 |
2.31e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAqfrkKELGFIFQDYSVLPTLTV 101
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIML---PL--SVQKMKKDEMEKnyqdVTEAL---GIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGAL 173
Cdd:PRK10575 103 RELVAIgryPWhgALGRFGAADREK----VEEAIslvGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515743034 174 DSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQERGLTVIAVLHDINmAARYCDYLVALRGGEM 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-218 |
2.64e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 66.97 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLL-NVISSIDSISGgTVEISGNEINQLSNKKLAQFRKKELGFIFQDySVLPTLT 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEG-KVHWSNKNESEPSFEATRSRNRYSVAYAAQK-PWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIML--PLSVQKmkkdemeknYQDVTEALGIYDLSDKYP----SEI-------SGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:cd03290 95 VEENITFgsPFNKQR---------YKAVTDACSLQPDIDLLPfgdqTEIgerginlSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 168 EPTGALDSKSAQDLLHR-----LEDMNKqfnsTIIMVTHDPSAASFAQRVIMLKDG 218
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgilkfLQDDKR----TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-221 |
5.89e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.99 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 4 LNVNHVSKIYGTKQKFKalhDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNeinqlsnkklaqfrk 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFK---NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN--------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDYSvlPTLTVKENIMLPLSVQKMKKDemekNYQDVTEALGIY----DLSDKYPSEISGGQQQRTAAARAFVH 159
Cdd:PRK15064 382 ANIGYYAQDHA--YDFENDLTLFDWMSQWRQEGD----DEQAVRGTLGRLlfsqDDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 160 QPSIIFADEPTGALDSKSAQDLLHRLEdmnkQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIH 221
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALE----KYEGTLIFVSHDREfVSSLATRIIEITPDGVV 514
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-245 |
6.37e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 24 DINFSVDKGEFVAIMGPSGSGKTTLLNVI---------SSIDSISGGTVEIS------GNEINQLSNKKLAQFRKKELGF 88
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndHHIVFKNEHTNDMTneqdyqGDEEQNVGMKNVNEFSLTKEGG 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 89 IFQDYSV------------------------LPTLTVKENIMLPLSV-QKMKKDEMEKNYQDVTEALG-------IYDLS 136
Cdd:PTZ00265 1266 SGEDSTVfknsgkilldgvdicdynlkdlrnLFSIVSQEPMLFNMSIyENIKFGKEDATREDVKRACKfaaidefIESLP 1345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 137 DKYPSEI-------SGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFA 209
Cdd:PTZ00265 1346 NKYDTNVgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRS 1425
|
250 260 270
....*....|....*....|....*....|....*.
gi 515743034 210 QRVIMLKDGDIHSDIHQQSKTkskfYNEIIQLQSAL 245
Cdd:PTZ00265 1426 DKIVVFNNPDRTGSFVQAHGT----HEELLSVQDGV 1457
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-220 |
8.27e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 65.24 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDS--ISGGTVEISGNEINQLSNKKLAqfrKKELGFIFQDYSVLPTL 99
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERA---RLGIFLAFQYPPEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 100 TVKENImlplsvqkmkkdemeknyQDVTEALgiydlsdkypseiSGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQ 179
Cdd:cd03217 93 KNADFL------------------RYVNEGF-------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515743034 180 DLLHRLEDMNKQfNSTIIMVTHDPSAASF--AQRVIMLKDGDI 220
Cdd:cd03217 142 LVAEVINKLREE-GKSVLIITHYQRLLDYikPDRVHVLYDGRI 183
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-220 |
8.64e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.56 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 15 TKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSidSISGGTVE----ISGNEINQLSNKKLAqfrkkelGFIF 90
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdirISGFPKKQETFARIS-------GYCE 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 91 QDYSVLPTLTVKENIM------LPLSVQKMKK----DE-ME----KNYQDVTEAL-GIYDLSDKypseisggQQQRTAAA 154
Cdd:PLN03140 960 QNDIHSPQVTVRESLIysaflrLPKEVSKEEKmmfvDEvMElvelDNLKDAIVGLpGVTGLSTE--------QRKRLTIA 1031
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 155 RAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDmNKQFNSTIIMVTHDPSA---ASFAQRVIMLKDGDI 220
Cdd:PLN03140 1032 VELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdifEAFDELLLMKRGGQV 1099
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-204 |
1.00e-12 |
|
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: 67.47 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 24 DINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTveisgneinqlsnkkLAQFRKKELGFIFQD-YSVLPTLtvK 102
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR---------------LTKPAKGKLFYVPQRpYMTLGTL--R 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 103 ENIMLPLSVQKMKKDEMEKnyQDVTEALGIYDLSD------------KYPSEISGGQQQRTAAARAFVHQPSIIFADEPT 170
Cdd:TIGR00954 533 DQIIYPDSSEDMKRRGLSD--KDLEQILDNVQLTHilereggwsavqDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|....
gi 515743034 171 GALdsksAQDLLHRLEDMNKQFNSTIIMVTHDPS 204
Cdd:TIGR00954 611 SAV----SVDVEGYMYRLCREFGITLFSVSHRKS 640
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-202 |
1.71e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.98 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKIYGTKQ-KFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSI--DSISGGTVEISGNEIN--QLSN 75
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDgWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkDNWRVTADRMRFDDIDllRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 76 KKlaqfRKKELG----FIFQD-YSVL-PTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEAL------GIYDLSD---KYP 140
Cdd:PRK15093 81 RE----RRKLVGhnvsMIFQEpQSCLdPSERVGRQLMQNIPGWTYKGRWWQRFGWRKRRAIellhrvGIKDHKDamrSFP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 141 SEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHD 202
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHD 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-201 |
2.00e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.20 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInqlsNKKLAQFrKKELGFIFQDYSVLPTLTV 101
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTY-QKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMLPLsvqkmkkdEMEKNYQDVTEALGIYDLSD--KYPSE-ISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSA 178
Cdd:PRK13540 92 RENCLYDI--------HFSPGAVGITELCRLFSLEHliDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|...
gi 515743034 179 QDLLHRLEDMNKQfNSTIIMVTH 201
Cdd:PRK13540 164 LTIITKIQEHRAK-GGAVLLTSH 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-237 |
2.42e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 18 KFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISS-IDSISGG-TVEISGNEINQLSNKKlaqFRKKELGFIFQDYSV 95
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIGvEGVITYDGITPEEIKK---HYRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 96 LPTLTVKENIMLplsVQKMK----------KDEMEKNYQDVTEAlgIYDLSDKYPSE--------ISGGQQQRTAAARAF 157
Cdd:TIGR00956 150 FPHLTVGETLDF---AARCKtpqnrpdgvsREEYAKHIADVYMA--TYGLSHTRNTKvgndfvrgVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 158 VHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFA--QRVIMLKDGDIhsdIHQQSKTKSKFY 235
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYElfDKVIVLYEGYQ---IYFGPADKAKQY 301
|
..
gi 515743034 236 NE 237
Cdd:TIGR00956 302 FE 303
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-201 |
6.06e-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: 65.42 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIY-GTKQKfkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInqLSNKKLAQf 81
Cdd:TIGR01257 1937 ILRLNELTKVYsGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVH- 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 rkKELGFIFQDYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQP 161
Cdd:TIGR01257 2012 --QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515743034 162 SIIFADEPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTH 201
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSH 2128
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-218 |
6.79e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.93 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGneinqlsnkklaqfrkkELGFIFQDYSVLPTlTV 101
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMLPLSVQKMKKDEMEKNYQdVTEALGIYDLSDKYP-----SEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSK 176
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACQ-LEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515743034 177 SAQDLLHRLedMNKQF-NSTIIMVTHDPSAASFAQRVIMLKDG 218
Cdd:TIGR01271 583 TEKEIFESC--LCKLMsNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-224 |
7.21e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVI-SSIDSISGGTVEISGNEINqlsNKKLAQF 81
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVD---IRNPAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKELGFIFQD---YSVLPTLTVKENIMLPL--SVQKMKKDEMEKNYQDVTEALGIYDLSDKYP----SEISGGQQQRTA 152
Cdd:TIGR02633 334 IRAGIAMVPEDrkrHGIVPILGVGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 153 AARAFVHQPSIIFADEPTGALDSkSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDIHSDI 224
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDV-GAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKGDF 485
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-220 |
8.89e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqlsNKKLAQFRKKELGFIFQDYS----VLp 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV---TRSPQDGLANGIVYISEDRKrdglVL- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 98 TLTVKENIMLPlSVQKMKKDEMEKNYQDVTEALG--IYDLSDKYPS------EISGGQQQRTAAARAFVHQPSIIFADEP 169
Cdd:PRK10762 344 GMSVKENMSLT-ALRYFSRAGGSLKHADEQQAVSdfIRLFNIKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515743034 170 TGALDSkSAQDLLHRLEDMNKQFNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK10762 423 TRGVDV-GAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-219 |
1.23e-11 |
|
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: 60.85 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 31 KGEFVAIMGPSGSGKTTLLN-VISSIDSISGGTVEISGNEInqlsnkklaqfrkkelgfifqdysvlptltvkenimlpl 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 110 svqkmkkdemeknyQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLL-----HR 184
Cdd:smart00382 42 --------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515743034 185 LEDMNKQFNSTIIMVTHDPS------AASFAQRVIMLKDGD 219
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLIL 148
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-243 |
3.26e-11 |
|
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: 61.80 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGneinqlsnkklaqfrkkELGFIFQDYSVLPTlTV 101
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMLPLSVQkmkkdemEKNYQDVTEALGIYDLSDKYPSE-----------ISGGQQQRTAAARAFVHQPSIIFADEPT 170
Cdd:cd03291 115 KENIIFGVSYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 171 GALDSKSAQDLLHRLEdMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDihsdihqqsktkSKFYNEIIQLQS 243
Cdd:cd03291 188 GYLDVFTEKEIFESCV-CKLMANKTRILVTSKMEHLKKADKILILHEGS------------SYFYGTFSELQS 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-222 |
4.14e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISsidsisgGTVEISGNEINQLSNKKLAQFR----KKELGFIFqDYsvlp 97
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDGRIIYEQDLIVARLQqdppRNVEGTVY-DF---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 98 tltVKENI-----MLP----LSVQkMKKDEMEKNY------QDVTEALGIYDL--------------SDKYPSEISGGQQ 148
Cdd:PRK11147 87 ---VAEGIeeqaeYLKryhdISHL-VETDPSEKNLnelaklQEQLDHHNLWQLenrinevlaqlgldPDAALSSLSGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 149 QRTAAARAFVHQPSIIFADEPTGALDSksaqDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDIHS 222
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSfIRNMATRIVDLDRGKLVS 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-246 |
4.31e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.62 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSiSGGTVEISGNEINQLSnkkLAQFRKKeLGFIFQDYSVLpTLTV 101
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVT---LQTWRKA-FGVIPQKVFIF-SGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMlplSVQKMKKDEMEKnyqdVTEALGIYDLSDKYPSE-----------ISGGQQQRTAAARAFVHQPSIIFADEPT 170
Cdd:TIGR01271 1309 RKNLD---PYEQWSDEEIWK----VAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 171 GALDSKSAQDLLHRLEdmnKQF-NSTIIMVTHDPSAASFAQRVIMLKDGDIhsdihQQSKTKSKFYNEIIQLQSALG 246
Cdd:TIGR01271 1382 AHLDPVTLQIIRKTLK---QSFsNCTVILSEHRVEALLECQQFLVIEGSSV-----KQYDSIQKLLNETSLFKQAMS 1450
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-202 |
8.66e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQKFKalhDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEIsGNEInqlsnkklaqfr 82
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLID---DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 83 kkELGFIFQDYSVL-PTLTVKENIMLPLSVQKMKKDEM-EKNYqdvteaLGIYDLS----DKYPSEISGGQQQRTAAARA 156
Cdd:TIGR03719 386 --KLAYVDQSRDALdPNKTVWEEISGGLDIIKLGKREIpSRAY------VGRFNFKgsdqQKKVGQLSGGERNRVHLAKT 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515743034 157 FVHQPSIIFADEPTGALDSksaqDLLHRLEDMNKQFNSTIIMVTHD 202
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD 499
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-220 |
9.46e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 23 HDINFSVDKGEFVAIMGPSGSGKT----TLLNVISSIDSISGGTVEISGNEInqlsnkKLAQFRKKELGFIFQD----YS 94
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV------APCALRGRKIATIMQNprsaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 95 VLPTLT--VKEnimlplSVQKMKKDEMEKNYQDVTEALGIYD---LSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEP 169
Cdd:PRK10418 94 PLHTMHthARE------TCLALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515743034 170 TGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPS-AASFAQRVIMLKDGDI 220
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGRI 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-220 |
1.25e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLN-VISSIDSISGGTVEISGN--EINQLSnkklaqfrkkelgFIFQdysvlpt 98
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTvaYVPQVS-------------WIFN------- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 99 LTVKENIM--LPLSVQKMKKDEMEKNYQDVTEALGIYDLSD--KYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALD 174
Cdd:PLN03130 693 ATVRDNILfgSPFDPERYERAIDVTALQHDLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515743034 175 SKSAQDLLHR-LEDMNKqfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PLN03130 773 AHVGRQVFDKcIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-220 |
2.35e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfrKKELGFIFQDySVLPTLTV 101
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL----RRVLSIIPQS-PVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMlPLSvqkmkkdemEKNYQDVTEAL---GIYDLSDKYP-----------SEISGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:PLN03232 1327 RFNID-PFS---------EHNDADLWEALeraHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515743034 168 EPTGALDSKSaQDLLHRleDMNKQFNS-TIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PLN03232 1397 EATASVDVRT-DSLIQR--TIREEFKScTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-201 |
3.48e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQfrkKELGFIFQDYSVLPTL 99
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 100 TVKENIML---PLSVQKMKKDEMEKNYQDVTEALGI-YDLSDKYpSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDS 175
Cdd:PRK10982 89 SVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIdIDPRAKV-ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180
....*....|....*....|....*.
gi 515743034 176 KSAQDLLHRLEDMnKQFNSTIIMVTH 201
Cdd:PRK10982 168 KEVNHLFTIIRKL-KERGCGIVYISH 192
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
22-245 |
5.85e-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: 58.33 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISgGTVEISGNEINQLSnkkLAQFRKKeLGFIFQDYSVLpTLTV 101
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVP---LQKWRKA-FGVIPQKVFIF-SGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMlplSVQKMKKDEMEKnyqdVTEALGIYDLSDKYPSE-----------ISGGQQQRTAAARAFVHQPSIIFADEPT 170
Cdd:cd03289 94 RKNLD---PYGKWSDEEIWK----VAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743034 171 GALDSKSAQDLLHRLEdmnKQF-NSTIIMVTHDPSAASFAQRVIMLKDGDIhsdihQQSKTKSKFYNEIIQLQSAL 245
Cdd:cd03289 167 AHLDPITYQVIRKTLK---QAFaDCTVILSEHRIEAMLECQRFLVIEENKV-----RQYDSIQKLLNEKSHFKQAI 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-218 |
1.16e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSIsgGTVEisgNEInqLSNKKLAQFRK----KELG--FIFQDY 93
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPH--GSYE---GEI--LFDGEVCRFKDirdsEALGivIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 94 SVLPTLTVKENIMLPLSVQK---MKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPT 170
Cdd:NF040905 88 ALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515743034 171 GALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKDG 218
Cdd:NF040905 168 AALNEEDSAALLDLLLELKAQ-GITSIIISHKlNEIRRVADSITVLRDG 215
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-202 |
1.55e-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: 56.61 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 32 GEFVAIMGPSGSGKTTLLNVISS--IDSISGGTVEISGNEInqlsnkkLAQFRKKELgfifQDY---------------- 93
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGklKPNLGKFDDPPDWDEI-------LDEFRGSEL----QNYftkllegdvkvivkpq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 94 --SVLPTlTVKENIMLPLSvqkmKKDEMEKnYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTG 171
Cdd:cd03236 95 yvDLIPK-AVKGKVGELLK----KKDERGK-LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|....
gi 515743034 172 ALDSK---SAQDLLHRLEDMNKqfnsTIIMVTHD 202
Cdd:cd03236 169 YLDIKqrlNAARLIRELAEDDN----YVLVVEHD 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-213 |
2.11e-09 |
|
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: 56.26 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 17 QKFKALHDINFSVDKGEF-----VAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInqlSNKKlaqfrkkelGFIFQ 91
Cdd:cd03237 5 TMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYKP---------QYIKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 92 DYSVlptlTVKENIMlplsvqKMKKDEMEKNY--QDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEP 169
Cdd:cd03237 73 DYEG----TVRDLLS------SITKDFYTHPYfkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515743034 170 TGALDSKS---AQDLLHRLEDMNKqfnSTIIMVTHDPSAASF-AQRVI 213
Cdd:cd03237 143 SAYLDVEQrlmASKVIRRFAENNE---KTAFVVEHDIIMIDYlADRLI 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-174 |
2.80e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 25 INFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRkKELGFIFQDYSVLptltvkEN 104
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYL-GHLPGLKADLSTL------EN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 105 IMLPLSVQKMKKDEMEKNYQDVteaLGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALD 174
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-220 |
3.08e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLN-VISSIDSISGGTVEISGN--EINQLSnkklaqfrkkelgFIFQdysvlpt 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSvaYVPQVS-------------WIFN------- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 99 LTVKENIMLPlsvqkmKKDEMEKNYQDVTEALGIYDLsDKYPSE-----------ISGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:PLN03232 693 ATVRENILFG------SDFESERYWRAIDVTALQHDL-DLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515743034 168 EPTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PLN03232 766 DPLSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-201 |
3.19e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.80 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 19 FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDS--ISGGTVEISGNEINQLSNKKLAQfrkkeLG-FI-FQdYS 94
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERAH-----LGiFLaFQ-YP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 95 V-LPTLTVKENIMLPL-SVQK-MKKDEME--KNYQDVTEALGIYDLSDKYPSE-----ISGGQQQRTAAARAFVHQPSII 164
Cdd:CHL00131 94 IeIPGVSNADFLRLAYnSKRKfQGLPELDplEFLEIINEKLKLVGMDPSFLSRnvnegFSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515743034 165 FADEPTGALDS---KSAQDLLHRLEDMNKqfnsTIIMVTH 201
Cdd:CHL00131 174 ILDETDSGLDIdalKIIAEGINKLMTSEN----SIILITH 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-243 |
8.15e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVskiygTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKK----- 77
Cdd:PRK10982 250 ILEVRNL-----TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 78 --LAQFRKKELGfIFQDY-----SVLPTLTVKENIMLPLSVQKMKKDEmeknyQDVTEALGIYDLSDKYP-SEISGGQQQ 149
Cdd:PRK10982 325 faLVTEERRSTG-IYAYLdigfnSLISNIRNYKNKVGLLDNSRMKSDT-----QWVIDSMRVKTPGHRTQiGSLSGGNQQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 150 RTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDIHSDIhqqsK 229
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIV----D 474
|
250
....*....|....
gi 515743034 230 TKSKFYNEIIQLQS 243
Cdd:PRK10982 475 TKTTTQNEILRLAS 488
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-220 |
1.04e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 23 HDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqLSNKKLA---------QFRKKElGFIfqdy 93
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSPRDAiragimlcpEDRKAE-GII---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 94 svlPTLTVKENI-------MLPLSVQKMKKDEMEknyqdvTEALGIYDLSDKYPS------EISGGQQQRTAAARAFVHQ 160
Cdd:PRK11288 344 ---PVHSVADNInisarrhHLRAGCLINNRWEAE------NADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743034 161 PSIIFADEPTGALD--SKSA-QDLLHRLEDMNKqfnsTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK11288 415 MKVILLDEPTRGIDvgAKHEiYNVIYELAAQGV----AVLFVSSDlPEVLGVADRIVVMREGRI 474
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-202 |
1.56e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 31 KGEFVAIMGPSGSGKTTLLNVISsidsisGGTVEISGNEINQLS-NKKLAQFRKKELGFIFQDYSvlptltvKENI---- 105
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILS------GELKPNLGDYDEEPSwDEVLKRFRGTELQDYFKKLA-------NGEIkvah 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 106 ------MLPLSVQKMKKDEMEKN-----YQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALD 174
Cdd:COG1245 165 kpqyvdLIPKVFKGTVRELLEKVdergkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|.
gi 515743034 175 SK---SAQDLLHRLEDMNKqfnsTIIMVTHD 202
Cdd:COG1245 245 IYqrlNVARLIRELAEEGK----YVLVVEHD 271
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-202 |
1.65e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 2 PILNVNHVSKIYGTKqkfKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISsidsisgGTVEISGNEINQLSNKKLAQF 81
Cdd:PRK10636 311 PLLKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA-------GELAPVSGEIGLAKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 82 RKKELGFIFQDYSVLPTLTvkenimlplsvqKMKKDEMEKNYQDVTEALGIY-DLSDKYPSEISGGQQQRTAAARAFVHQ 160
Cdd:PRK10636 381 AQHQLEFLRADESPLQHLA------------RLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQR 448
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515743034 161 PSIIFADEPTGALDSKSAQDLLHRLEDmnkqFNSTIIMVTHD 202
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALID----FEGALVVVSHD 486
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-202 |
1.91e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 24 DINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISgneinqlSNKKLAQFRKKELGFIfqDYSVLPTLTvke 103
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS-------AKVRMAVFSQHHVDGL--DLSSNPLLY--- 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 104 nimlplsvqkmkkdeMEKNYQDVTEA-----LGIYDLSDKYPSE----ISGGQQQRTAAARAFVHQPSIIFADEPTGALD 174
Cdd:PLN03073 595 ---------------MMRCFPGVPEQklrahLGSFGVTGNLALQpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180
....*....|....*....|....*...
gi 515743034 175 SKSAQDLLHRLedmnKQFNSTIIMVTHD 202
Cdd:PLN03073 660 LDAVEALIQGL----VLFQGGVLMVSHD 683
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-174 |
4.44e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkLAQFRKKeLGFIFQDySVLPTLTV 101
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKV-LGIIPQA-PVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMlPLSvqkmkkdemEKNYQDVTEALGIYDLSD-------KYPSEI-------SGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:PLN03130 1330 RFNLD-PFN---------EHNDADLWESLERAHLKDvirrnslGLDAEVseagenfSVGQRQLLSLARALLRRSKILVLD 1399
|
....*..
gi 515743034 168 EPTGALD 174
Cdd:PLN03130 1400 EATAAVD 1406
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-220 |
7.02e-08 |
|
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: 51.83 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfrKKELGFIFQDySVLPTLTV 101
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL----RSRLSIILQD-PILFSGSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENImlplsvqkmkkdEMEKNYQDVT--EALGIYDLSDKYPS--------------EISGGQQQRTAAARAFVHQPSIIF 165
Cdd:cd03288 112 RFNL------------DPECKCTDDRlwEALEIAQLKNMVKSlpggldavvteggeNFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515743034 166 ADEPTGALDsKSAQDLLHRLEdMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:cd03288 180 MDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-170 |
8.67e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.43 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 19 FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqlsNKKLAQfRKKeLGFIFQDYSVLPT 98
Cdd:NF033858 279 FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIAT-RRR-VGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743034 99 LTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPT 170
Cdd:NF033858 354 LTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-217 |
9.36e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLAQFRKKElgfiFQDysvlptl 99
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE----WQR------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 100 tvKENIMLP-------LSVQKMKKDEMEKNY--QDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPT 170
Cdd:PRK10938 86 --NNTDMLSpgeddtgRTTAEIIQDEVKDPArcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515743034 171 GALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKD 217
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-233 |
1.14e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 3 ILNVNHVSKIYGTKQKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVI-SSIDSISGGTVEISGNEIN-QLSNKKLAQ 80
Cdd:PRK13549 259 ILEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKiRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 81 F-------RKKelgfifqdYSVLPTLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPS------EISGGQ 147
Cdd:PRK13549 339 GiamvpedRKR--------DGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelaiaRLSGGN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 148 QQRTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRLEDMNKQFNStIIMVTHD-PSAASFAQRVIMLKDGDIHSDIHQ 226
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVA-IIVISSElPEVLGLSDRVLVMHEGKLKGDLIN 489
|
....*..
gi 515743034 227 QSKTKSK 233
Cdd:PRK13549 490 HNLTQEQ 496
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-220 |
1.51e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 24 DINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKlaqfrKKELGFI-----------FQD 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVylpedrqssglYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 93 YSV---LPTLTVKEnimLPLSVQKMKKDEMEKNYQdvtEALGI-YDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADE 168
Cdd:PRK15439 356 APLawnVCALTHNR---RGFWIKPARENAVLERYR---RALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515743034 169 PTGALDSKSAQDLLHRLEDMNKQfNSTIIMVTHD-PSAASFAQRVIMLKDGDI 220
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-220 |
1.95e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.43 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEinqlsnkklaqfrkkelGFIFQDYSVLPTLT 100
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------------ALIAISSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKSAQD 180
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515743034 181 LLHRLEDMNKQfNSTIIMVTHDPSAA-SFAQRVIMLKDGDI 220
Cdd:PRK13545 182 CLDKMNEFKEQ-GKTIFFISHSLSQVkSFCTKALWLHYGQV 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-65 |
2.93e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 2.93e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGTKQKFKalhDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEI 65
Cdd:PRK11819 327 AENLSKSFGDRLLID---DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-229 |
3.57e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVIS-------SIDSISGGTVEISGNEINQLsnkklaqfrKKELGF----IF 90
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgySNDLTLFGRRRGSGETIWDI---------KKHIGYvsssLH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 91 QDYSVlpTLTVKeNIML-----PLSVQKMKKDEMEKNYQDVTEALGIYD-LSDKYPSEISGGQQQRTAAARAFVHQPSII 164
Cdd:PRK10938 347 LDYRV--STSVR-NVILsgffdSIGIYQAVSDRQQKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLL 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 165 FADEPTGALDSKSAQDLLHRLEDMNKQFNSTIIMVTHDPSAA--SFAQRVIMLKDGDIHSdiHQQSK 229
Cdd:PRK10938 424 ILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDApaCITHRLEFVPDGDIYR--YVQTK 488
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-202 |
4.60e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.62 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 17 QKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINqLSNKKLAQFRKkELGFIFQDYSVL 96
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQ-QVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 97 PTLT-VKENIMLPLSVQKMKKDEMEKNyqdVTEALGIYDLSD--KYPSE-ISGGQQQRTAAARAFVHQPSIIFADEPTGA 172
Cdd:PRK13638 90 IFYTdIDSDIAFSLRNLGVPEAEITRR---VDEALTLVDAQHfrHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190
....*....|....*....|....*....|
gi 515743034 173 LDSKSAQDLLHRLEDMNKQFNSTIIMvTHD 202
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIIS-SHD 195
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-170 |
5.64e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 6 VNHVSKIYGtkqKFKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQlsnkklAQFRK-- 83
Cdd:NF033858 4 LEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD------ARHRRav 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 ------------KELgfifqdYsvlPTLTVKENI-----MLPLSvqkmkKDEMEKNYQDVTEALGIYDLSDKYPSEISGG 146
Cdd:NF033858 75 cpriaympqglgKNL------Y---PTLSVFENLdffgrLFGQD-----AAERRRRIDELLRATGLAPFADRPAGKLSGG 140
|
170 180
....*....|....*....|....
gi 515743034 147 QQQRTAAARAFVHQPSIIFADEPT 170
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPT 164
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-213 |
5.74e-07 |
|
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: 48.47 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 21 ALHDINFSVDKGEFVAIMGPSGSGKTTLLNvissidsisggtvEISGNEINQLSNKKLAQFRKKELGFIFQdysvLPTLt 100
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFSRNKLIFIDQ----LQFL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 101 VKENI-MLPLSvQKMkkdemeknyqdvtealgiydlsdkypSEISGGQQQRTA-AARAFVHQPSIIFA-DEPTGALDSks 177
Cdd:cd03238 72 IDVGLgYLTLG-QKL--------------------------STLSGGELQRVKlASELFSEPPGTLFIlDEPSTGLHQ-- 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 515743034 178 aQDLLHRLEDMNK--QFNSTIIMVTHDPSAASFAQRVI 213
Cdd:cd03238 123 -QDINQLLEVIKGliDLGNTVILIEHNLDVLSSADWII 159
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-220 |
6.77e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.94 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkLAQFRKKeLGFIFQDySVLPTLTV 101
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFK-ITIIPQD-PVLFSGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMlPLSvqkmkkdemEKNYQDVTEALGIYDLSDKYPSE--------------ISGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:TIGR00957 1377 RMNLD-PFS---------QYSDEEVWWALELAHLKTFVSALpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515743034 168 EPTGALDSKSaQDLLHrlEDMNKQFNS-TIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:TIGR00957 1447 EATAAVDLET-DNLIQ--STIRTQFEDcTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-202 |
7.35e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.78 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 28 SVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEisgneinqlSNKKLA---QfrkkelgFIFQDYSvlptLTVKEN 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---------EDLKISykpQ-------YISPDYD----GTVEEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 105 IMlplsvqKMKKDEMEKNY--QDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSK---SAQ 179
Cdd:COG1245 422 LR------SANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVA 495
|
170 180
....*....|....*....|...
gi 515743034 180 DLLHRLEDMNKqfnSTIIMVTHD 202
Cdd:COG1245 496 KAIRRFAENRG---KTAMVVDHD 515
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-202 |
9.40e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 31 KGEFVAIMGPSGSGKTTLLNVISsidsisGGTVEISGNEINQLSNKK-LAQFRKKELGFIFQDYS--------------V 95
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILS------GELIPNLGDYEEEPSWDEvLKRFRGTELQNYFKKLYngeikvvhkpqyvdL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 96 LPTL---TVKEniMLplsvqkMKKDEmEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGA 172
Cdd:PRK13409 172 IPKVfkgKVRE--LL------KKVDE-RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|...
gi 515743034 173 LDSK---SAQDLLHRLEDmnkqfNSTIIMVTHD 202
Cdd:PRK13409 243 LDIRqrlNVARLIRELAE-----GKYVLVVEHD 270
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-220 |
1.17e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVeisgneinqlsnkklaqFRKKELGFIFQDYSVLpTLTV 101
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------------WAERSIAYVPQQAWIM-NATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMLplsvqkmKKDEMEKNYQDVT-----EAlGIYDLSDKYPSEI-------SGGQQQRTAAARAFVHQPSIIFADEP 169
Cdd:PTZ00243 738 RGNILF-------FDEEDAARLADAVrvsqlEA-DLAQLGGGLETEIgekgvnlSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515743034 170 TGALDSKSAQDLLHRLEdMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PTZ00243 810 LSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-201 |
2.07e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSID--SISGGTVEISGNEINQLSNKKlaqfRKKELGFIFQDYSV-LPt 98
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED----RAGEGIFMAFQYPVeIP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 99 lTVKENIMLPLSVQKMKKdemeknYQDvTEALGIYDLSD---------KYPSEI---------SGGQQQRTAAARAFVHQ 160
Cdd:PRK09580 92 -GVSNQFFLQTALNAVRS------YRG-QEPLDRFDFQDlmeekiallKMPEDLltrsvnvgfSGGEKKRNDILQMAVLE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515743034 161 PSIIFADEPTGALDS---KSAQDLLHRLEDMNKQFnstiIMVTH 201
Cdd:PRK09580 164 PELCILDESDSGLDIdalKIVADGVNSLRDGKRSF----IIVTH 203
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-213 |
2.18e-06 |
|
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: 47.25 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTL-------------LNVISS-------------IDSISGGTVEISgneINQlsn 75
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAyarqflgqmdkpdVDSIEGLSPAIA---IDQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 76 KKLAQFRKKELGFIFQDYSVLPTLTVKENIMLPLSVqkmkkdemeknYQDVteALGIYDLSDKYPSeISGGQQQRTAAAR 155
Cdd:cd03270 85 KTTSRNPRSTVGTVTEIYDYLRLLFARVGIRERLGF-----------LVDV--GLGYLTLSRSAPT-LSGGEAQRIRLAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 156 AFVHQ-PSIIFA-DEPTGALDSKSAQDLLHRLEDMNKQFNsTIIMVTHDPSAASFAQRVI 213
Cdd:cd03270 151 QIGSGlTGVLYVlDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHVI 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-174 |
2.23e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSNKKLaqfrKKELGFIFQDySVLPTLTV 101
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL----RRQFSMIPQD-PVLFDGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 102 KENIMlPLsvqkmkkdeMEKNYQDVTEALGIYDLSDKYPSEISG--------------GQQQRTAAARAFVHQPS-IIFA 166
Cdd:PTZ00243 1401 RQNVD-PF---------LEASSAEVWAALELVGLRERVASESEGidsrvleggsnysvGQRQLMCMARALLKKGSgFILM 1470
|
....*...
gi 515743034 167 DEPTGALD 174
Cdd:PTZ00243 1471 DEATANID 1478
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
144-222 |
2.99e-06 |
|
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: 46.45 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 144 SGGQQQ------RTAAARAFVHQPSIIFADEPTGALDSKSAQDLLHRL-EDMNKQFNSTIIMVTHDPS---AASFAQRVI 213
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIiEERKSQKNFQLIVITHDEElvdAADHIYRVE 196
|
....*....
gi 515743034 214 mlKDGDIHS 222
Cdd:cd03240 197 --KDGRQKS 203
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-202 |
3.02e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 19 FKALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEisgneinqlsnkklaqfRKKELGFIFQDYSVLPT 98
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 99 LTVKENIMLPLSVQKMKKDEMEKNYQDVTE--ALG--IYDLSDKYpseiSGGQQQRTAAARAFVHQPSIIFADEPTGALD 174
Cdd:PRK13546 100 LTGIENIEFKMLCMGFKRKEIKAMTPKIIEfsELGefIYQPVKKY----SSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180
....*....|....*....|....*...
gi 515743034 175 SKSAQDLLHRLEDMNKQfNSTIIMVTHD 202
Cdd:PRK13546 176 QTFAQKCLDKIYEFKEQ-NKTIFFVSHN 202
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-232 |
3.90e-06 |
|
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: 47.49 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 25 INFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEINQLSnkkLAQFRKKelgF--IFQDYSVLPTLTVK 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN---REAYRQL---FsaVFSDFHLFDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 103 ENIMLPLSVQK-MKKDEMEknyqdvtEALGIYD--LSDKypsEISGGQQQRTAAARAFVHQPSIIFADEptGALDsksaQ 179
Cdd:COG4615 425 DGEADPARARElLERLELD-------HKVSVEDgrFSTT---DLSQGQRKRLALLVALLEDRPILVFDE--WAAD----Q 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 180 D----------LLHRLEDMNKqfnsTIIMVTHDPSAASFAQRVIMLKDGDIHSDIHQQSKTKS 232
Cdd:COG4615 489 DpefrrvfyteLLPELKARGK----TVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-202 |
6.89e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 39 GPSGSGKTTLLNVISSIDSISGGTVEISGNEinqlsnkKLAQFRKKElgFIFQDYSVLPTLtvkenIMLPLSVQKMKKD- 117
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDPNE-------RLGKLRQDQ--FAFEEFTVLDTV-----IMGHTELWEVKQEr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 118 -------EM-EKNYQDVTEALGIYDLSDKYP-----------------------SEISGGQQQRTAAARAFVHQPSIIFA 166
Cdd:PRK15064 100 driyalpEMsEEDGMKVADLEVKFAEMDGYTaearagelllgvgipeeqhyglmSEVAPGWKLRVLLAQALFSNPDILLL 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 515743034 167 DEPTGALDSksaqDLLHRLEDMNKQFNSTIIMVTHD 202
Cdd:PRK15064 180 DEPTNNLDI----NTIRWLEDVLNERNSTMIIISHD 211
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-220 |
7.98e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.50 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 16 KQKFkALHDINFSVDKGEFVAIMGPSGSGKTTLLNVISSIDSISGGTVEISGNEInqlSNKKLAQFRKKeLGFIFQDYSv 95
Cdd:PRK10522 334 DNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKL-FSAVFTDFH- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 96 lptltvkenimlpLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSE--------ISGGQQQRTAAARAFVHQPSIIFAD 167
Cdd:PRK10522 408 -------------LFDQLLGPEGKPANPALVEKWLERLKMAHKLELEdgrisnlkLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 168 EptGALDSKSA------QDLLHRLEDMNKqfnsTIIMVTHDPSAASFAQRVIMLKDGDI 220
Cdd:PRK10522 475 E--WAADQDPHfrrefyQVLLPLLQEMGK----TIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
98-244 |
1.06e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 98 TLTVKENIMLPLSVQKMKKDEMEKNYQDVTEALGIYDLSDKYPSEISGGQQQRTAAARAFVHQPSIIFADEPTGALDSKS 177
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743034 178 AQDLLHRLEDMNKQFNSTIIMVTHDPSAASFAQRVIMLKDGDIHSDiHQQSKTKSKFYNEIIQLQSA 244
Cdd:NF000106 180 RNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD-GKVDELKTKVGGRTLQIRPA 245
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-202 |
1.41e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 24 DINFSVDKGEFVAIMGPSGSGKTTLLNV-ISSIDSISG----GTveisgneinqlsnkklaqfrKKELGFIFQDYSVL-P 97
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQADSGrihcGT--------------------KLEVAYFDQHRAELdP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 98 TLTVKENImlplsvqKMKKDEMEKNYQDvTEALGiYdLSD--------KYP-SEISGGQQQRTAAARAFVHQPSIIFADE 168
Cdd:PRK11147 397 EKTVMDNL-------AEGKQEVMVNGRP-RHVLG-Y-LQDflfhpkraMTPvKALSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|....
gi 515743034 169 PTGALDSKSaqdlLHRLEDMNKQFNSTIIMVTHD 202
Cdd:PRK11147 467 PTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-213 |
6.21e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 6.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743034 143 ISGGQQQRTAAARAFVHQPSII--FADEPTGALDSKSAQDLLHRLEDMNKQFNsTIIMVTHDPSAASFAQRVI 213
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMISLADRII 548
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
143-216 |
6.22e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 6.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743034 143 ISGGQQQRTAAARAFVHQ-----PSIIFaDEPTGALDSKSAQDLLHRLEDMNKQFNSTIImVTHDPSAASFAQRVIMLK 216
Cdd:cd03227 78 LSGGEKELSALALILALAslkprPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAELADKLIHIK 154
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-201 |
2.08e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 1 MPILNVNHVSKiyGTKQKFKALHDINFSVDKG---------------EFVAIMGPSGSGKTTLLNVIS--SIDSISGGTV 63
Cdd:PLN03073 159 MPGVYVNHDGN--GGGPAIKDIHMENFSISVGgrdlivdasvtlafgRHYGLVGRNGTGKTTFLRYMAmhAIDGIPKNCQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 64 ------EISGNEINQL-----SNKKLAQFRKKELGFIFQDYSvLPTLTVKENIMLPlSVQKMKKDEMEKNYQDVTEALgi 132
Cdd:PLN03073 237 ilhveqEVVGDDTTALqcvlnTDIERTQLLEEEAQLVAQQRE-LEFETETGKGKGA-NKDGVDKDAVSQRLEEIYKRL-- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 133 yDLSDKYPSE-----------------------ISGGQQQRTAAARAFVHQPSIIFADEPTGALDsksaqdlLHR---LE 186
Cdd:PLN03073 313 -ELIDAYTAEaraasilaglsftpemqvkatktFSGGWRMRIALARALFIEPDLLLLDEPTNHLD-------LHAvlwLE 384
|
250
....*....|....*
gi 515743034 187 DMNKQFNSTIIMVTH 201
Cdd:PLN03073 385 TYLLKWPKTFIVVSH 399
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-174 |
2.24e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 20 KALHDINFSVDKGEFVAIMGPSGSGKTTLLNvissidSISG--------GTVEISGNEInQLSN------KKLAQFR--K 83
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAM------SVFGrsygrnisGTVFKDGKEV-DVSTvsdaidAGLAYVTedR 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 84 KELGFIFQDysvlptlTVKENIMLPlSVQKMKK----DEME--KNYQDVTEALGIydlsdKYPS------EISGGQQQRT 151
Cdd:NF040905 347 KGYGLNLID-------DIKRNITLA-NLGKVSRrgviDENEeiKVAEEYRKKMNI-----KTPSvfqkvgNLSGGNQQKV 413
|
170 180
....*....|....*....|...
gi 515743034 152 AAARAFVHQPSIIFADEPTGALD 174
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
142-219 |
4.42e-04 |
|
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: 39.86 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 142 EISGGQQQRTAAARAFVHQPSIIFADEPTGALDSK---SAQDLLHRLEDMNKQfnsTIIMVTHDPSAASFAQRVIMLKDG 218
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRLSEEGKK---TALVVEHDLAVLDYLSDRIHVFEG 147
|
.
gi 515743034 219 D 219
Cdd:cd03222 148 E 148
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
22-50 |
5.40e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 5.40e-04
10 20
....*....|....*....|....*....
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLN 50
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
23-219 |
1.78e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.40 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 23 HDINFS-VDKGEFVAIMGPSGSGKTTLLnvissiDSIS---GGTVEISGNEINQLSNKKLAQfRKKELGFIFQ----DYS 94
Cdd:cd03279 18 QVIDFTgLDNNGLFLICGPTGAGKSTIL------DAITyalYGKTPRYGRQENLRSVFAPGE-DTAEVSFTFQlggkKYR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 95 VLPTL-----TVKENIMLPlsvQKMKKDEMEKNYqdvtealgiydlsdkypSEISGGQQQRTAAARAF----VHQPS--- 162
Cdd:cd03279 91 VERSRgldydQFTRIVLLP---QGEFDRFLARPV-----------------STLSGGETFLASLSLALalseVLQNRgga 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743034 163 ---IIFADEPTGALDSKS---AQDLLHRLEDMNKqfnsTIIMVTHDPS-AASFAQRVIMLKDGD 219
Cdd:cd03279 151 rleALFIDEGFGTLDPEAleaVATALELIRTENR----MVGVISHVEElKERIPQRLEVIKTPG 210
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
22-50 |
2.33e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 2.33e-03
10 20
....*....|....*....|....*....
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLN 50
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
31-50 |
2.60e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 37.86 E-value: 2.60e-03
|
| rad3 |
TIGR00604 |
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ... |
9-118 |
3.40e-03 |
|
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are DNA-DNA helicases that funciton in the initiation of transcription and nucleotide excision repair as part of the TFIIH complex. 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: 273169 [Multi-domain] Cd Length: 705 Bit Score: 38.54 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743034 9 VSKIYGTKQKFkaLHDINFSVDKGEFVAIMGPSGSGKT-TLLNVISSIDSISGGTVEI-----SGNEINQLSN--KKLAQ 80
Cdd:TIGR00604 8 YEKIYPEQRSY--MRDLKRSLDRGDEAILEMPSGTGKTiSLLSLILAYQQEKPEVRKIiyasrTHSQLEQATEelRKLMS 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 515743034 81 FRKKELGFIfQDYSVLPtLTVKENIMLPLSVQKMKKDE 118
Cdd:TIGR00604 86 YRTPRIGEE-SPVSGLS-LASRKNLCLHPEVSKERQGK 121
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
29-54 |
6.51e-03 |
|
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 37.37 E-value: 6.51e-03
10 20
....*....|....*....|....*.
gi 515743034 29 VDKGEFVAIMGPSGSGKTTLLNVISS 54
Cdd:COG0630 287 LENGKSVLVAGGTASGKTTLLNALLS 312
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
22-50 |
6.51e-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: 37.21 E-value: 6.51e-03
10 20
....*....|....*....|....*....
gi 515743034 22 LHDINFSVDKGEFVAIMGPSGSGKTTLLN 50
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
13-49 |
6.96e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.07 E-value: 6.96e-03
10 20 30
....*....|....*....|....*....|....*...
gi 515743034 13 YGTKQKFKALHDINFSVDKGE-FVAIMGPSGSGKTTLL 49
Cdd:COG3267 23 FLSPSHREALARLEYALAQGGgFVVLTGEVGTGKTTLL 60
|
|
| |
