|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-225 |
1.27e-86 |
|
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: 255.49 E-value: 1.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAK-PTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFR 80
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AENIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKALQQttepkpslqkeAIRLLTALGLSEPYHSKdVASLSIGQQQR 160
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRER-----------AEELLERVGLGDRLNHY-PSELSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDETLKPLFNRAISL 225
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIEL 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
2.47e-84 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 249.96 E-value: 2.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDAK-PTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVF 79
Cdd:COG1136 4 LLELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RAENIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKAlqqttepkpslQKEAIRLLTALGLSEpYHSKDVASLSIGQQQ 159
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKER-----------RERARELLERVGLGD-RLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDETLKPLFNRAISL 225
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRL 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
4.83e-62 |
|
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: 193.80 E-value: 4.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDAkpTLNI---PTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRD 77
Cdd:COG4181 8 IIELRGLTKTVGTGAG--ELTIlkgISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 78 VFRAENIGYIFQNFNLLPYLTPIENVTLGCEfsksrkqkaLQQTTEPkpslQKEAIRLLTALGLSE-----PyhskdvAS 152
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVMLPLE---------LAGRRDA----RARARALLERVGLGHrldhyP------AQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDETL 215
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-215 |
1.30e-55 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 176.78 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNdaKPTL-NIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVF 79
Cdd:COG2884 1 MIRFENVSKRYPGG--REALsDV-SLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RaENIGYIFQNFNLLPYLTPIENVTLgcefsksrkqkALQQTTEPKPSLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQ 159
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVAL-----------PLRVTGKSRKEIRRRVREVLDLVGLSDKAKAL-PHELSGGEQQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKlLFEQAKRANSTLVFVSHDETL 215
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIME-LLEEINRRGTTVLIATHDLEL 199
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-225 |
3.11e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 164.07 E-value: 3.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFR 80
Cdd:COG3638 2 MLELRNLSKRY--PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AEnIGYIFQNFNLLPYLTPIENVTLGC------------EFSKSRKQKALQqttepkpslqkeairLLTALGLSEPYHSK 148
Cdd:COG3638 80 RR-IGMIFQQFNLVPRLSVLTNVLAGRlgrtstwrsllgLFPPEDRERALE---------------ALERVGLADKAYQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 149 dVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD-ETLKPLFNRAISL 225
Cdd:COG3638 144 -ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQvDLARRYADRIIGL 220
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-215 |
4.77e-48 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 157.41 E-value: 4.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFR 80
Cdd:TIGR02673 1 MIEFHNVSKAY--PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQNFNLLPYLTPIENVTLgcefsksrkqkALQQTTEPKPSLQKEAIRLLTALGLSEPYHSKDVaSLSIGQQQR 160
Cdd:TIGR02673 79 -RRIGVVFQDFRLLPDRTVYENVAL-----------PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPE-QLSGGEQQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESfIKLLFEQAKRANSTLVFVSHDETL 215
Cdd:TIGR02673 146 VAIARAIVNSPPLLLADEPTGNLDPDLSER-ILDLLKRLNKRGTTVIVATHDLSL 199
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-222 |
6.06e-47 |
|
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: 155.05 E-value: 6.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVT--FKWHKNDAKPTLNIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDV 78
Cdd:cd03258 1 MIELKNVSkvFGDTGGKVTALKDV-SLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 FRAeNIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKALQQTTEpkpslqkeairLLTALGLSEPYHSKDvASLSIGQQ 158
Cdd:cd03258 80 ARR-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLE-----------LLELVGLEDKADAYP-AQLSGGQK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD-ETLKPLFNRA 222
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRV 211
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
25-225 |
4.06e-46 |
|
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: 152.00 E-value: 4.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAENIGYIFQNFNLLPYLTPIENVT 104
Cdd:TIGR03608 19 LTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENETVEENLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 105 LGCEFSK-SRKQKalqqttepkpslQKEAIRLLTALGLSEpYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:TIGR03608 99 LGLKYKKlSKKEK------------REKKKEALEKVGLNL-KLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490726575 184 DTANRESFIKLLFEQAKRaNSTLVFVSHDETLKPLFNRAISL 225
Cdd:TIGR03608 166 DPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-212 |
6.82e-45 |
|
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: 149.21 E-value: 6.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkptLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfra 81
Cdd:cd03259 1 LELKGLSKTYGSVRA---LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 eNIGYIFQNFNLLPYLTPIENVTLGCEFSKSrkqkalqqttePKPSLQKEAIRLLTALGLsEPYHSKDVASLSIGQQQRV 161
Cdd:cd03259 73 -NIGMVFQDYALFPHLTVAENIAFGLKLRGV-----------PKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHD 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
1.40e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.85 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDAKPTL--NIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqrdv 78
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTAldDV-SLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 fraENIGYIFQNFNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQ 158
Cdd:COG1116 80 ---PDRGVVFQEPALLPWLTVLDNVALG-----------LELRGVPKAERRERARELLELVGLAG-FEDAYPHQLSGGMR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-225 |
1.96e-44 |
|
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: 148.87 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRA 81
Cdd:cd03256 1 IEVENLSKTY--PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 EnIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKALQQttePKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQRV 161
Cdd:cd03256 79 Q-IGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGL---FPKEEKQRALAALERVGLLD-KAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDETL-KPLFNRAISL 225
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLaREYADRIVGL 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-212 |
1.20e-43 |
|
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: 146.08 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTL--NIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNtqrdvf 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAleDI-SLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 raeNIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKAlqqttepkpslQKEAIRLLTALGLSEpYHSKDVASLSIGQQQ 159
Cdd:cd03293 74 ---DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEA-----------RERAEELLELVGLSG-FENAYPHQLSGGMRQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-230 |
2.08e-43 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 146.08 E-value: 2.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAENIGYIFQNFNLLPYLTPIENVT 104
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 105 LgcefsksrkqKALQQTTEPKPSlQKEAIRLLTALGLSEPYHSKDvASLSIGQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:PRK10584 111 L----------PALLRGESSRQS-RNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490726575 185 TANRESFIKLLFEQAKRANSTLVFVSHDETLKPLFNRAISLV--SLQE 230
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVngQLQE 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-225 |
3.52e-43 |
|
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: 144.53 E-value: 3.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 3 ELDNVTFKWhKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvfRAE 82
Cdd:cd03225 1 ELKNLSFSY-PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 83 NIGYIFQN-----FNllpyLTPIENVTLGCEfsksrkqkalqQTTEPKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQ 157
Cdd:cd03225 76 KVGLVFQNpddqfFG----PTVEEEVAFGLE-----------NLGLPEEEIEERVEEALELVGLEG-LRDRSPFTLSGGQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHD-ETLKPLFNRAISL 225
Cdd:cd03225 140 KQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEGKTIIIVTHDlDLLLELADRVIVL 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
1.35e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 147.17 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDAKPTLNiptLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfr 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVS---LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aeNIGYIFQNFNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQR 160
Cdd:COG3842 78 --NVGMVFQDYALFPHLTVAENVAFG-----------LRMRGVPKAEIRARVAELLELVGLEG-LADRYPHQLSGGQQQR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-212 |
3.33e-42 |
|
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: 149.67 E-value: 3.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVT--FKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDV 78
Cdd:COG1123 260 LLEVRNLSkrYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 FRAEnIGYIFQN----FNllPYLTPIENVTLGCEFsksrkqkalqQTTEPKPSLQKEAIRLLTALGLSEPYHSKDVASLS 154
Cdd:COG1123 340 LRRR-VQMVFQDpyssLN--PRMTVGDIIAEPLRL----------HGLLSRAERRERVAELLERVGLPPDLADRYPHELS 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD 464
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-213 |
4.85e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.88 E-value: 4.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKwhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvFRA 81
Cdd:COG4619 1 LELEGLSFR---VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 EnIGYIFQNFNLLPYlTPIENVTLGCEFSKSRKQkalqqttepkpslQKEAIRLLTALGLSEPYHSKDVASLSIGQQQRV 161
Cdd:COG4619 75 Q-VAYVPQEPALWGG-TVRDNLPFPFQLRERKFD-------------RERALELLERLGLPPDILDKPVERLSGGERQRL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDE 213
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDP 191
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-212 |
1.61e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 141.35 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkptLNIPTLRIDKGEhIF-LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfr 80
Cdd:COG1131 1 IEVRGLTKRYGDKTA---LDGVSLTVEPGE-IFgLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQNFNLLPYLTPIENVTLgceFSKSRKQkalqqttePKPSLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQR 160
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRF---FARLYGL--------PRKEARERIDELLELFGLTDAADRK-VGTLSGGMKQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRaNSTLVFVSHD 212
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHY 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
1.97e-41 |
|
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: 140.24 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTfKWHKNDAKPTLNIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRa 81
Cdd:cd03292 1 IEFINVT-KTYPNGTAALDGI-NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLPYLTPIENVTLgcefsksrkqkALQQTTEPKPSLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQRV 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAF-----------ALEVTGVPPREIRKRVPAALELVGLSHKHRAL-PAELSGGEQQRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESfIKLLFEQAKRANSTLVFVSHDETL 215
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWE-IMNLLKKINKAGTTVVVATHAKEL 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-212 |
4.83e-41 |
|
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: 139.56 E-value: 4.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDN--VTFKwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDV 78
Cdd:cd03257 1 LLEVKNlsVSFP-TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 FRAEnIGYIFQNfnllPY--LTPIENVtlgcefsksRKQ--KALQ-QTTEPKPSLQKEAIRL-LTALGLSEPYHSKDVAS 152
Cdd:cd03257 80 RRKE-IQMVFQD----PMssLNPRMTI---------GEQiaEPLRiHGKLSKKEARKEAVLLlLVGVGLPEEVLNRYPHE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHD 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
5.29e-41 |
|
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: 138.09 E-value: 5.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkptLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRa 81
Cdd:cd03229 1 LELKNVSKRYGQKTV---LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 eNIGYIFQNFNLLPYLTPIENVTLGcefsksrkqkalqqttepkpslqkeairlltalglsepyhskdvasLSIGQQQRV 161
Cdd:cd03229 77 -RIGMVFQDFALFPHLTVLENIALG----------------------------------------------LSGGQQQRV 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHD 160
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-184 |
1.46e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 138.97 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVtfkwHKN-DAKPTL-NIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLnTLSNTQRDV 78
Cdd:COG1126 1 MIEIENL----HKSfGDLEVLkGI-SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 FRAEnIGYIFQNFNLLPYLTPIENVTLGCEfsKSRKQkalqqttePKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQ 158
Cdd:COG1126 75 LRRK-VGMVFQQFNLFPHLTVLENVTLAPI--KVKKM--------SKAEAEERAMELLERVGLAD-KADAYPAQLSGGQQ 142
|
170 180
....*....|....*....|....*.
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALD 184
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-212 |
1.68e-39 |
|
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: 136.47 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDN--VTFKwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLntlSNTQRDV 78
Cdd:COG1124 1 MLEVRNlsVSYG-QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 FRAeNIGYIFQNfnllPY--LTPIENVtlgcefsksrkQKALqqtTEP-----KPSLQKEAIRLLTALGLSEPYHSKDVA 151
Cdd:COG1124 77 FRR-RVQMVFQD----PYasLHPRHTV-----------DRIL---AEPlrihgLPDREERIAELLEQVGLPPSFLDRYPH 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490726575 152 SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG1124 138 QLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD 198
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-212 |
2.01e-39 |
|
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: 135.89 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFR 80
Cdd:TIGR02315 1 MLEVENLSKVY--PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AeNIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKALQQTTEPKpslQKEAIRLLTALGLSEpYHSKDVASLSIGQQQR 160
Cdd:TIGR02315 79 R-RIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEED---KERALSALERVGLAD-KAYQRADQLSGGQQQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQ 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-223 |
2.73e-39 |
|
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: 135.15 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntQRDVFRa 81
Cdd:COG1122 1 IELENLSFSY--PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN--LRELRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 eNIGYIFQN-FNLLPYLTPIENVTLGCE-FSKSRKQkalqqttepkpsLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQ 159
Cdd:COG1122 76 -KVGLVFQNpDDQLFAPTVEEDVAFGPEnLGLPREE------------IRERVEEALELVGLEH-LADRPPHELSGGQKQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHD-ETLKPLFNRAI 223
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELL-KRLNKEGKTVIIVTHDlDLVAELADRVI 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-213 |
1.18e-38 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 133.90 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfra 81
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 eNIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQkalqqttepkpSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQRV 161
Cdd:cd03300 73 -PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKA-----------EIKERVAEALDLVQLEG-YANRKPSQLSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDE 213
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQ 191
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
1.26e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.06 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhknDAKPTL-NIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsntqrdvf 79
Cdd:COG1121 6 AIELENLTVSY---GGRPVLeDV-SLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RAENIGYIFQNFNL---LPyLTPIENVTLGC--------EFSKSRKQKALQqttepkpslqkeairLLTALGLSEpYHSK 148
Cdd:COG1121 73 ARRRIGYVPQRAEVdwdFP-ITVRDVVLMGRygrrglfrRPSRADREAVDE---------------ALERVGLED-LADR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490726575 149 DVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHD-ETLKPLFNRAI 223
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTILVVTHDlGAVREYFDRVL 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-212 |
2.69e-38 |
|
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: 133.25 E-value: 2.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKndaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfr 80
Cdd:COG1120 1 MLEAENLSVGYGG---RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AENIGYIFQNFNLLPYLTPIENVTLGcefsksRK--QKALQQttePKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQ 158
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVALG------RYphLGLFGR---PSAEDREAVEEALERTGLEH-LADRPVDELSGGER 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHD 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-214 |
4.90e-38 |
|
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: 131.61 E-value: 4.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTLNiptLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDvfra 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLN---LDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 enIGYIFQNFNLLPYLTPIENVTLGCefsKSRKQkalqqttePKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQRV 161
Cdd:cd03301 74 --IAMVFQNYALYPHMTVYDNIAFGL---KLRKV--------PKDEIDERVREVAELLQIEH-LLDRKPKQLSGGQRQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDET 214
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQV 192
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-212 |
9.87e-38 |
|
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: 130.73 E-value: 9.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTfKWHKNdaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLnTLSNTQRDVFRA 81
Cdd:cd03262 1 IEIKNLH-KSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 EnIGYIFQNFNLLPYLTPIENVTLGceFSKSRKqkalqqttEPKPSLQKEAIRLLTALGLSEPYHSKDvASLSIGQQQRV 161
Cdd:cd03262 77 K-VGMVFQQFNLFPHLTVLENITLA--PIKVKG--------MSKAEAEERALELLEKVGLADKADAYP-AQLSGGQQQRV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHD 212
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELVGEVLDVM-KDLAEEGMTMVVVTHE 194
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-212 |
1.33e-37 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 131.52 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKndaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfr 80
Cdd:COG4555 1 MIEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKALQQTTEpkpslqkeairLLTALGLSEPYHSKdVASLSIGQQQR 160
Cdd:COG4555 74 -RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEE-----------LIELLGLEEFLDRR-VGELSTGMKKK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHD 212
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREIL-RALKKEGKTVLFSSHI 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-212 |
2.22e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 133.28 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTfKWHKNDAKPTL---NIpTLRIDKGEhIF-LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQR 76
Cdd:COG1135 1 MIELENLS-KTFPTKGGPVTaldDV-SLTIEKGE-IFgIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 77 DVFRAeNIGYIFQNFNLLPYLTPIENVTLgcefsksrkqkALQQTTEPKPSLQKEAIRLLTALGLSepyHSKDV--ASLS 154
Cdd:COG1135 78 RAARR-KIGMIFQHFNLLSSRTVAENVAL-----------PLEIAGVPKAEIRKRVAELLELVGLS---DKADAypSQLS 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfeqaKRANS----TLVFVSHD 212
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLL----KDINRelglTIVLITHE 200
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-214 |
2.22e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 133.66 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfr 80
Cdd:COG3839 3 SLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aeNIGYIFQNFNLLPYLTPIENVTLGCefsKSRKqkalqqttEPKPSLQKEAIRLLTALGLsEPYHSKDVASLSIGQQQR 160
Cdd:COG3839 76 --NIAMVFQSYALYPHMTVYENIAFPL---KLRK--------VPKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRE---SFIKLLFeqaKRANSTLVFVSHDET 214
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLRVemrAEIKRLH---RRLGTTTIYVTHDQV 195
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
20-225 |
4.70e-37 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 129.07 E-value: 4.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 20 LNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAENIGYIFQNFNLLPYLTP 99
Cdd:NF038007 21 LNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILRRELIGYIFQSFNLIPHLSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 100 IENVTLGCEF----SKSRKQKALQqttepkpslqkeairLLTALGLSEPYHSKDvASLSIGQQQRVAAARAFIGSPELII 175
Cdd:NF038007 101 FDNVALPLKYrgvaKKERIERVNQ---------------VLNLFGIDNRRNHKP-MQLSGGQQQRVAIARAMVSNPALLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 176 ADEPTSALDTANRESfiklLFEQAKRAN---STLVFVSHDETLKPLFNRAISL 225
Cdd:NF038007 165 ADEPTGNLDSKNARA----VLQQLKYINqkgTTIIMVTHSDEASTYGNRIINM 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-211 |
7.83e-37 |
|
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: 127.11 E-value: 7.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqRDVFRa 81
Cdd:cd03228 1 IEFKNVSFS-YPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNfnllPYL---TPIENVtlgcefsksrkqkalqqttepkpslqkeairlltalglsepyhskdvasLSIGQQ 158
Cdd:cd03228 76 KNIAYVPQD----PFLfsgTIRENI-------------------------------------------------LSGGQR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKraNSTLVFVSH 211
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAH 153
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-225 |
1.31e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.39 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAENIGYIFQNFNLLPYLTPIENV 103
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEFSKSRKQKAlqqttepkpslQKEAIRLLTALGLSEPYHSKDvASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:PRK11629 109 AMPLLIGKKKPAEI-----------NSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490726575 184 DTANRESFIKLLFEQAKRANSTLVFVSHDETLKPLFNRAISL 225
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-216 |
1.44e-36 |
|
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: 135.73 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqRDVFRa 81
Cdd:COG2274 474 IELENVSFR-YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLpYLTPIENVTLGcefsksrkqkalqqttEPKPSLQkEAIRLLTALGLSE-----P--YHSK---DVA 151
Cdd:COG2274 549 RQIGVVLQDVFLF-SGTIRENITLG----------------DPDATDE-EIIEAARLAGLHDfiealPmgYDTVvgeGGS 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490726575 152 SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfeQAKRANSTLVFVSHD-ETLK 216
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIAHRlSTIR 674
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-212 |
2.14e-36 |
|
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: 127.84 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhkNDAKptLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDvfra 81
Cdd:cd03299 1 LKVENLSKDW--KEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 enIGYIFQNFNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQRV 161
Cdd:cd03299 73 --ISYVPQNYALFPHMTVYKNIAYG-----------LKKRKVDKKEIERKVLEIAEMLGIDHLLNRK-PETLSGGEQQRV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-225 |
2.52e-36 |
|
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: 127.26 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 3 ELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLntlsntQRDVFRae 82
Cdd:cd03235 1 EVEDLTVSY---GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL------EKERKR-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 83 nIGYIFQNFNLLPYLtPI---ENVTLGCE--------FSKSRKQKALQqttepkpslqkeairLLTALGLSEpYHSKDVA 151
Cdd:cd03235 70 -IGYVPQRRSIDRDF-PIsvrDVVLMGLYghkglfrrLSKADKAKVDE---------------ALERVGLSE-LADRQIG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 152 SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHD-ETLKPLFNRAISL 225
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDlGLVLEYFDRVLLL 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-212 |
3.41e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.18 E-value: 3.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNdakpTLNIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVfr 80
Cdd:COG3840 1 MLRLDDLTYRYGDF----PLRF-DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aeniGYIFQNFNLLPYLTPIENVTLGceFSKSRKQKALQqttepkpslQKEAIRLLTALGLSEpYHSKDVASLSIGQQQR 160
Cdd:COG3840 74 ----SMLFQENNLFPHLTVAQNIGLG--LRPGLKLTAEQ---------RAQVEQALERVGLAG-LLDRLPGQLSGGQRQR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-212 |
4.43e-36 |
|
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: 127.42 E-value: 4.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvFRa 81
Cdd:cd03295 1 IEFENVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLPYLTPIENVTLGCEFSKsrkqkalqqttEPKPSLQKEAIRLLTALGLsEPYHSKD--VASLSIGQQQ 159
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLK-----------WPKEKIRERADELLALVGL-DPAEFADryPHELSGGQQQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD 195
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-223 |
5.75e-36 |
|
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: 5.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqRDVFRa 81
Cdd:cd03245 3 IEFRNVSFSY-PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLpYLTPIENVTLGCEFSKSRkqkalqqttepkpslqkEAIRLLTALGLSE--PYHSKDVA-------- 151
Cdd:cd03245 78 RNIGYVPQDVTLF-YGTLRDNITLGAPLADDE-----------------RILRAAELAGVTDfvNKHPNGLDlqigergr 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 152 SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfeQAKRANSTLVFVSHDETLKPLFNRAI 223
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERL--RQLLGDKTLIIITHRPSLLDLVDRII 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-212 |
6.06e-36 |
|
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: 126.85 E-value: 6.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRA 81
Cdd:cd03261 1 IELRGLTKSF---GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 eNIGYIFQNFNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRL-LTALGLsEPYHSKDVASLSIGQQQR 160
Cdd:cd03261 78 -RMGMLFQSGALFDSLTVFENVAFP-----------LREHTRLSEEEIREIVLEkLEAVGL-RGAEDLYPAELSGGMKKR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHD 196
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
25-213 |
1.59e-35 |
|
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: 128.62 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDvfraenIGYIFQNFNLLPYLTPIENVT 104
Cdd:TIGR03265 25 LSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRD------YGIVFQSYALFPNLTVADNIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 105 LGCEFSKSRKQKALQQTTEpkpslqkeairLLTALGLSEPyHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:TIGR03265 99 YGLKNRGMGRAEVAERVAE-----------LLDLVGLPGS-ERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALD 166
|
170 180
....*....|....*....|....*....
gi 490726575 185 TANRESFIKLLFEQAKRANSTLVFVSHDE 213
Cdd:TIGR03265 167 ARVREHLRTEIRQLQRRLGVTTIMVTHDQ 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-212 |
2.72e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 125.21 E-value: 2.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNdakPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVfR 80
Cdd:PRK09493 1 MIEFKNVSKHFGPT---QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AEnIGYIFQNFNLLPYLTPIENVTLGCefSKSRKQKalqqttepKPSLQKEAIRLLTALGLSEPYHSKDvASLSIGQQQR 160
Cdd:PRK09493 77 QE-AGMVFQQFYLFPHLTALENVMFGP--LRVRGAS--------KEEAEKQARELLAKVGLAERAHHYP-SELSGGQQQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRAnSTLVFVSHD 212
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHE 195
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-181 |
2.77e-35 |
|
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: 122.37 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 20 LNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNtlsNTQRDVFRAEnIGYIFQNFNLLPYLTP 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT---DDERKSLRKE-IGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 100 IENVTLGCEFSKSRKQKALQQttepkpslqkeAIRLLTALGLSEPYHSK---DVASLSIGQQQRVAAARAFIGSPELIIA 176
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDAR-----------AEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLL 145
|
....*
gi 490726575 177 DEPTS 181
Cdd:pfam00005 146 DEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
6.73e-35 |
|
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: 122.12 E-value: 6.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkptLNIPTLRIDKGEhIF-LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfr 80
Cdd:cd03230 1 IEVRNLSKRYGKKTA---LDDISLTVEKGE-IYgLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQNFNLLPYLTPIENVtlgcefsksrkqkalqqttepkpslqkeairlltalglsepyhskdvaSLSIGQQQR 160
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL------------------------------------------------KLSGGMKQR 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRaNSTLVFVSHD 212
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHI 154
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-225 |
1.14e-34 |
|
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: 121.20 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 3 ELDNVTFKWHKndaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDvfraE 82
Cdd:cd00267 1 EIENLSFRYGG---RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 83 NIGYIFQnfnllpyltpienvtlgcefsksrkqkalqqttepkpslqkeairlltalglsepyhskdvasLSIGQQQRVA 162
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------------------LSGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490726575 163 AARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRaNSTLVFVSHD-ETLKPLFNRAISL 225
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDpELAELAADRVIVL 153
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-225 |
3.23e-34 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 121.43 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKwhKNDaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsntQRDVFR 80
Cdd:COG4133 2 MLEAENLSCR--RGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD----AREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKAlqqttepkpslqkEAIRLLTALGLsEPYHSKDVASLSIGQQQR 160
Cdd:COG4133 75 -RRLAYLGHADGLKPELTVRENLRFWAALYGLRADRE-------------AIDEALEAVGL-AGLADLPVRQLSAGQKRR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHDEtLKPLFNRAISL 225
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELI-AAHLARGGAVLLTTHQP-LELAAARVLDL 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-212 |
3.91e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 127.95 E-value: 3.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvfRA 81
Cdd:COG4988 337 IELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS----WR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNfnllPYL---TPIENVTLGC-EFSKSRKQKALQQTtepkpslqkEAIRLLTAL--GLSEPyhskdV----A 151
Cdd:COG4988 411 RQIAWVPQN----PYLfagTIRENLRLGRpDASDEELEAALEAA---------GLDEFVAALpdGLDTP-----LgeggR 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490726575 152 SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKraNSTLVFVSHD 212
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR 531
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-212 |
4.58e-34 |
|
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: 122.75 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEhIF-LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAENIGYIFQNFNLLPYLTPIEN 102
Cdd:cd03294 44 SLDVREGE-IFvIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 103 VTLGCEFS----KSRKQKALQQttepkpslqkeairlLTALGLsEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADE 178
Cdd:cd03294 123 VAFGLEVQgvprAEREERAAEA---------------LELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 490726575 179 PTSALDTANR----ESFIKLLFEQAKransTLVFVSHD 212
Cdd:cd03294 187 AFSALDPLIRremqDELLRLQAELQK----TIVFITHD 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-213 |
5.29e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 121.05 E-value: 5.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKwhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTP---SSGNIRILNRDLNTLSNTQRd 77
Cdd:COG4136 1 MLSLENLTIT---LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 78 vfraeNIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKalqqttepkpslQKEAIRLLTALGLSEpYHSKDVASLSIGQ 157
Cdd:COG4136 77 -----RIGILFQDDLLFPHLSVGENLAFALPPTIGRAQR------------RARVEQALEEAGLAG-FADRDPATLSGGQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDE 213
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDE 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-225 |
7.17e-34 |
|
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: 127.57 E-value: 7.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvfRA 81
Cdd:COG4987 334 LELEDVSFRYP-GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD----LR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNfnllPYL--TPI-ENVTLGCEfsksrkqkalqQTTEpkpslqKEAIRLLTALGLSEPYHSKDV-------- 150
Cdd:COG4987 409 RRIAVVPQR----PHLfdTTLrENLRLARP-----------DATD------EELWAALERVGLGDWLAALPDgldtwlge 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 151 --ASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKraNSTLVFVSHDETLKPLFNRAISL 225
Cdd:COG4987 468 ggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVL 542
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-212 |
1.55e-33 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 120.09 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRID---KGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNT------LSNTQRdvfraeNIGYIFQNFNLL 94
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQR------KIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 95 PYLTPIENVTLGCEFSKSRKQKalQQTTEpkpslqkeairLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELI 174
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDR--ISVDE-----------LLDLLGLDHLLNRY-PAQLSGGEKQRVALARALAAQPELL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 490726575 175 IADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHD 191
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-214 |
1.78e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 123.29 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTLNiptLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDvfra 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLN---LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 enIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKALQQTtepkpslqKEAIRLLTALGLSEPYhskdVASLSIGQQQRV 161
Cdd:PRK11432 80 --ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRV--------KEALELVDLAGFEDRY----VDQISGGQQQRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDET 214
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQS 198
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-213 |
1.86e-33 |
|
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: 120.52 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 18 PTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLntlsnTQRDVfRAENIGYIFQNFNLLPYL 97
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-----TDVPV-QERNVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 98 TPIENVTLGCEFSKSRKQKalqqttePKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQRVAAARAFIGSPELIIAD 177
Cdd:cd03296 90 TVFDNVAFGLRVKPRSERP-------PEAEIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 490726575 178 EPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDE 213
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQ 197
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-212 |
2.35e-33 |
|
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: 120.08 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhknDAKPTL-NIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVF 79
Cdd:COG1127 5 MIEVRNLTKSF---GDRVVLdGV-SLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RAEnIGYIFQNFNLLPYLTPIENVTLGcefsksrkqkaLQQTTE-PKPSLQKEAIRLLTALGLSE-----PyhskdvASL 153
Cdd:COG1127 81 RRR-IGMLFQGGALFDSLTVFENVAFP-----------LREHTDlSEAEIRELVLEKLELVGLPGaadkmP------SEL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490726575 154 SIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHD 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-212 |
2.36e-33 |
|
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: 125.40 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPS---SGNIRILNRDLNTLSNTQRd 77
Cdd:COG1123 4 LLEVRDLSVR-YPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 78 vfrAENIGYIFQNFnlLPYLTPienVTLGCEFSKsrkqkALQQTTEPKPSLQKEAIRLLTALGLsEPYHSKDVASLSIGQ 157
Cdd:COG1123 82 ---GRRIGMVFQDP--MTQLNP---VTVGDQIAE-----ALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHD 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
24-223 |
3.08e-33 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 125.99 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAENIGYIFQNFNLLPYLTPIENV 103
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAAQNV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEFSKSRKQKALQQttepkpslqkeAIRLLTALGLSEPYHSKDvASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:PRK10535 108 EVPAVYAGLERKQRLLR-----------AQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490726575 184 DTANRESFIKLLfEQAKRANSTLVFVSHDETLKPLFNRAI 223
Cdd:PRK10535 176 DSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-225 |
3.40e-33 |
|
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: 120.19 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGN-IRILNRDLntlsnTQRDVF 79
Cdd:COG1119 3 LLELRNVTVRR---GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERR-----GGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 --RAeNIGYI---FQNFnlLPYLTPIENV-------TLGcefsksrkqkaLQQttEPKPSLQKEAIRLLTALGLSEpYHS 147
Cdd:COG1119 75 elRK-RIGLVspaLQLR--FPRDETVLDVvlsgffdSIG-----------LYR--EPTDEQRERARELLELLGLAH-LAD 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726575 148 KDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD-ETLKPLFNRAISL 225
Cdd:COG1119 138 RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHvEEIPPGITHVLLL 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-212 |
3.69e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 119.73 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkptLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLN---TLSNTQRDV 78
Cdd:COG4161 3 IQLKNINCFYGSHQA---LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 FRaENIGYIFQNFNLLPYLTPIENVTLG-CEFSKSRKQKAlqqttepkpslQKEAIRLLTALGLSE-----PYHskdvas 152
Cdd:COG4161 80 LR-QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQA-----------REKAMKLLARLRLTDkadrfPLH------ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALD---TANRESFIKLLfeqaKRANSTLVFVSHD 212
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQVVEIIREL----SQTGITQVIVTHE 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
4.29e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 119.97 E-value: 4.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWH-KNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLntlsnTQRDVF 79
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RaeniGYIFQNFNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQ 159
Cdd:COG4525 78 R----GVVFQKDALLPWLNVLDNVAFG-----------LRLRGVPKAERRARAEELLALVGLAD-FARRRIWQLSGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-212 |
7.30e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.41 E-value: 7.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTLNiptLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLntlsNTQRDVfRA 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVS---LEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLPP-RE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQRV 161
Cdd:COG1118 75 RRVGFVFQHYALFPHMTVAENIAFG-----------LRVRPPSKAEIRARVEELLELVQLEGLADRY-PSQLSGGQRQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHD 193
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-212 |
9.52e-33 |
|
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: 116.77 E-value: 9.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 3 ELDNVTFKWHKNDAkptLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfrAE 82
Cdd:cd03214 1 EVENLSVGYGGRTV---LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL----AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 83 NIGYIFQnfnllpyltpienvtlgcefsksrkqkalqqttepkpslqkeAIRLLTALGLSEpyhsKDVASLSIGQQQRVA 162
Cdd:cd03214 74 KIAYVPQ------------------------------------------ALELLGLAHLAD----RPFNELSGGERQRVL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490726575 163 AARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHD 157
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-211 |
1.15e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.15 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHkndakptlNIP---TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRD 77
Cdd:PRK10771 1 MLKLTDITWLYH--------HLPmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 78 VfraeniGYIFQNFNLLPYLTPIENVTLGCEfsksrkqKALQQTTEPKPSLQKEAIRlltaLGLsEPYHSKDVASLSIGQ 157
Cdd:PRK10771 73 V------SMLFQENNLFSHLTVAQNIGLGLN-------PGLKLNAAQREKLHAIARQ----MGI-EDLLARLPGQLSGGQ 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSH 211
Cdd:PRK10771 135 RQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-212 |
1.41e-32 |
|
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: 120.16 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGI---NTPSSGNIRILNRDLNTLSNTQRDVFRAENIGYIFQNfnllPY--LT 98
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKELRKIRGREIQMIFQD----PMtsLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 99 PIenVTLGcefsksrkqkalQQTTEP--------KPSLQKEAIRLLTALGLSEPyhsKDVAS-----LSIGQQQRVAAAR 165
Cdd:COG0444 101 PV--MTVG------------DQIAEPlrihgglsKAEARERAIELLERVGLPDP---ERRLDrypheLSGGMRQRVMIAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490726575 166 AFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-213 |
2.20e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 120.82 E-value: 2.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTfkwhKN-DAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVfr 80
Cdd:PRK09452 15 VELRGIS----KSfDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aeniGYIFQNFNLLPYLTPIENVTLGCefsksRKQKALQQTTEPKpslQKEAIRL--LTALGLSEPyhskdvASLSIGQQ 158
Cdd:PRK09452 89 ----NTVFQSYALFPHMTVFENVAFGL-----RMQKTPAAEITPR---VMEALRMvqLEEFAQRKP------HQLSGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANR---ESFIKLLfeqAKRANSTLVFVSHDE 213
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRkqmQNELKAL---QRKLGITFVFVTHDQ 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-212 |
2.49e-32 |
|
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: 116.84 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTfKWHKNDAKPTLNIPTLRIDKGEhIF-LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLntlsNTQRDVFR 80
Cdd:cd03263 1 LQIRNLT-KTYKKGTKPAVDDLSLNVYKGE-IFgLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQNFNLLPYLTPIENVTLGCEF-SKSRKQkalqqttepkpsLQKEAIRLLTALGLsEPYHSKDVASLSIGQQQ 159
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLkGLPKSE------------IKEEVELLLRVLGL-TDKANKRARTLSGGMKR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfeQAKRANSTLVFVSHD 212
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLI--LEVRKGRSIILTTHS 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-223 |
6.18e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 116.77 E-value: 6.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDakpTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLS--NTQRDV 78
Cdd:PRK11264 3 AIEVKNLVKKFHGQT---VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 FRA--ENIGYIFQNFNLLPYLTPIENVTLGCEFSKSrkqkalqqttEPKPSLQKEAIRLLTALGLSepyhSKDVA---SL 153
Cdd:PRK11264 80 IRQlrQHVGFVFQNFNLFPHRTVLENIIEGPVIVKG----------EPKEEATARARELLAKVGLA----GKETSyprRL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490726575 154 SIGQQQRVAAARAFIGSPELIIADEPTSALD---TANRESFIKLLFEQaKRansTLVFVSHDETL-KPLFNRAI 223
Cdd:PRK11264 146 SGGQQQRVAIARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQE-KR---TMVIVTHEMSFaRDVADRAI 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
6.27e-32 |
|
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: 116.38 E-value: 6.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNV--TFKWHKNDAK--PTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRD--LNTLSNT 74
Cdd:COG4778 4 LLEVENLskTFTLHLQGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 75 QRDVF--RAENIGYIFQNFNLLPYLTPIENVTlgcefsksrkqKALQQTTEPKPSLQKEAIRLLTALGLSEPYHSKDVAS 152
Cdd:COG4778 84 PREILalRRRTIGYVSQFLRVIPRVSALDVVA-----------EPLLERGVDREEARARARELLARLNLPERLWDLPPAT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHDE 213
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELI-EEAKARGTAIIGIFHDE 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-211 |
1.12e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 118.36 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNV--TFKWHKNdAKPTLNIPTLRIDKGEhIF-LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRD 77
Cdd:PRK11153 1 MIELKNIskVFPQGGR-TIHALNNVSLHIPAGE-IFgVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 78 VFRaENIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKALQQTTEpkpslqkeairLLTALGLSEpYHSKDVASLSIGQ 157
Cdd:PRK11153 79 KAR-RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTE-----------LLELVGLSD-KADRYPAQLSGGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSH 211
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-212 |
3.32e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 114.73 E-value: 3.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkptLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRA 81
Cdd:PRK11124 3 IQLNGINCFYGAHQA---LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 --ENIGYIFQNFNLLPYLTPIENVTLG-CEFSKSRKQKALQQttepkpslqkeAIRLLTALGLSE-----PYHskdvasL 153
Cdd:PRK11124 80 lrRNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALAR-----------AEKLLERLRLKPyadrfPLH------L 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 154 SIGQQQRVAAARAFIGSPELIIADEPTSALD---TANRESFIKLLFEqakrANSTLVFVSHD 212
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAE----TGITQVIVTHE 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-212 |
4.99e-31 |
|
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: 114.07 E-value: 4.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvFRAeNIGYIFQNFNLLPYLTPIENV 103
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--ARL-GIGRTFQIPRLFPELTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEFSKSRKQKALQQTTEpKPSLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:cd03219 97 MVAAQARTGSGLLLARARRE-EREARERAEELLERVGLADLADRP-AGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180
....*....|....*....|....*....
gi 490726575 184 DTANRESFIKLLfEQAKRANSTLVFVSHD 212
Cdd:cd03219 175 NPEETEELAELI-RELRERGITVLLVEHD 202
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-216 |
1.45e-30 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 114.42 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTfkwhK--NDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALlagIN---TPSSGNIRILNRDLNTLSNTQ 75
Cdd:COG1125 1 MIEFENVT----KryPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRM---INrliEPTSGRILIDGEDIRDLDPVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 76 --RdvfraeNIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKALQQTTEpkpslqkeairLLTALGLS-EPYHSKDVAS 152
Cdd:COG1125 74 lrR------RIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDE-----------LLELVGLDpEEYRDRYPHE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRES----FIKLlfeQAKRaNSTLVFVSHD--ETLK 216
Cdd:COG1125 137 LSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQlqdeLLRL---QREL-GKTIVFVTHDidEALK 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-212 |
3.52e-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: 111.13 E-value: 3.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkptLNIPTLRIDKGEHIFLhGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsntQRDVFRA 81
Cdd:cd03264 1 LQLENLTKRYGKKRA---LDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 EnIGYIFQNFNLLPYLTPIENVtlgcefsksRKQKALQQTtePKPSLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQRV 161
Cdd:cd03264 73 R-IGYLPQEFGVYPNFTVREFL---------DYIAWLKGI--PSKEVKARVDEVLELVNLGDRAKKK-IGSLSGGMRRRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAkrANSTLVFVSHD 212
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHI 188
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-212 |
6.42e-30 |
|
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: 111.12 E-value: 6.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFkWHKNDAkpTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGIN-----TPSSGNIRILNRDLNTLSNTQR 76
Cdd:cd03260 1 IELRDLNV-YYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 77 DVFRaeNIGYIFQNFNLLPyLTPIENVTLGCEFSKSRKQKALQQTTEpkpslqkeaiRLLTALGLSEPYHSK-DVASLSI 155
Cdd:cd03260 78 ELRR--RVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVE----------EALRKAALWDEVKDRlHALGLSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 156 GQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRAnsTLVFVSHD 212
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHN 199
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-184 |
2.36e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.49 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDAkptLNIPTLRIDKGEHIFLHGPSGVGKSTLL----ALLAGINTPSSgNIRILNRDLNTLSNTQR 76
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA---LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGS-HIELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 77 DVFRAE-NIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKALQQTTepkPSLQKEAIRLLTALGLSEPYHSKdVASLSI 155
Cdd:PRK09984 80 DIRKSRaNTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFT---REQKQRALQALTRVGMVHFAHQR-VSTLSG 155
|
170 180
....*....|....*....|....*....
gi 490726575 156 GQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-213 |
4.79e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.19 E-value: 4.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGE-HIFLhGPSGVGKSTLLALLAGINTPSSGNIRILNRDLntlsnTQRDVFRAEN--IGYIFQNFNLLPYLTPI 100
Cdd:COG1129 24 SLELRPGEvHALL-GENGAGKSTLMKILSGVYQPDSGEILLDGEPV-----RFRSPRDAQAagIAIIHQELNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 101 ENVTLGCEFSKSR--KQKALQqttepkpslqKEAIRLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIADE 178
Cdd:COG1129 98 ENIFLGREPRRGGliDWRAMR----------RRARELLARLGLDIDPDTP-VGDLSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 490726575 179 PTSALDTANRESFIKLLfEQAKRANSTLVFVSH--DE 213
Cdd:COG1129 167 PTASLTEREVERLFRII-RRLKAQGVAIIYISHrlDE 202
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-212 |
1.52e-28 |
|
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: 107.55 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLnTLSNTQRDVfraenigyIFQNFNLLPYLTPIENVT 104
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRMV--------VFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 105 LGC-----EFSKSRKQKALQQTtepkpslqkeairlLTALGLSEPYHsKDVASLSIGQQQRVAAARAFIGSPELIIADEP 179
Cdd:TIGR01184 77 LAVdrvlpDLSKSERRAIVEEH--------------IALVGLTEAAD-KRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190
....*....|....*....|....*....|...
gi 490726575 180 TSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHRVTVLMVTHD 174
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-211 |
1.71e-28 |
|
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: 105.76 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqRDVFRa 81
Cdd:cd03246 1 LEVENVSFR-YPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLPYlTPIENVtlgcefsksrkqkalqqttepkpslqkeairlltalglsepyhskdvasLSIGQQQRV 161
Cdd:cd03246 76 DHVGYLPQDDELFSG-SIAENI-------------------------------------------------LSGGQRQRL 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANrESFIKLLFEQAKRANSTLVFVSH 211
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEG-ERALNQAIAALKAAGATRIVIAH 154
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-213 |
2.93e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.40 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTfKWHKNDAkpTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVfra 81
Cdd:PRK10851 3 IEIANIK-KSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 eniGYIFQNFNLLPYLTPIENVTLGCEFSKSRKqkalqqttepKPS---LQKEAIRLLTALGLSepyHSKD--VASLSIG 156
Cdd:PRK10851 77 ---GFVFQHYALFRHMTVFDNIAFGLTVLPRRE----------RPNaaaIKAKVTQLLEMVQLA---HLADryPAQLSGG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 157 QQQRVAAARAFIGSPELIIADEPTSALDTANRE---SFIKLLFEQAKranSTLVFVSHDE 213
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKelrRWLRQLHEELK---FTSVFVTHDQ 197
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
24-212 |
3.15e-28 |
|
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: 107.05 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntQRDVFRAeNIGYIFQNFNLLPYLTPIENV 103
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP--PHRIARL-GIARTFQNPRLFPELTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEF-SKSRKQKALQQTTEPKPS---LQKEAIRLLTALGLSEpYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEP 179
Cdd:COG0411 101 LVAAHArLGRGLLAALLRLPRARREereARERAEELLERVGLAD-RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEP 179
|
170 180 190
....*....|....*....|....*....|...
gi 490726575 180 TSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG0411 180 AAGLNPEETEELAELIRRLRDERGITILLIEHD 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-213 |
6.06e-28 |
|
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: 107.96 E-value: 6.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 35 LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfraeNIGYIFQNFNLLPYLTPIENVTLGcefsksrk 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR------HINMVFQSYALFPHMTVEENVAFG-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 115 qkaLQQTTEPKPSLQKeaiRLLTALGLS--EPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFI 192
Cdd:TIGR01187 67 ---LKMRKVPRAEIKP---RVLEALRLVqlEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQ 140
|
170 180
....*....|....*....|.
gi 490726575 193 KLLFEQAKRANSTLVFVSHDE 213
Cdd:TIGR01187 141 LELKTIQEQLGITFVFVTHDQ 161
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-225 |
1.96e-27 |
|
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: 109.30 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqRDVFRa 81
Cdd:TIGR02857 322 LEFSGVSVAY--PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD---ADSWR- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNfnllPYLTP---IENVTLGC-EFSKSRKQKALQQTtepkpslqkEAIRLLTALGlsEPYHSK---DVASLS 154
Cdd:TIGR02857 396 DQIAWVPQH----PFLFAgtiAENIRLARpDASDAEIREALERA---------GLDEFVAALP--QGLDTPigeGGAGLS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRAnsTLVFVSHDETLKPLFNRAISL 225
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-212 |
2.50e-27 |
|
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: 107.11 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 33 IFlhGPSGVGKSTLLALLAGINTPSSGNIRILNRdlnTLSNTQRDVFRA---ENIGYIFQNFNLLPYLTPIENVTLGCEF 109
Cdd:COG4148 30 LF--GPSGSGKTTLLRAIAGLERPDSGRIRLGGE---VLQDSARGIFLPphrRRIGYVFQEARLFPHLSVRGNLLYGRKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 110 SKSRkqkalqqttEPKPSLQkEAIRLLtalGLsEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRE 189
Cdd:COG4148 105 APRA---------ERRISFD-EVVELL---GI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180
....*....|....*....|....
gi 490726575 190 SFIKLLfEQ-AKRANSTLVFVSHD 212
Cdd:COG4148 171 EILPYL-ERlRDELDIPILYVSHS 193
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-213 |
2.51e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.23 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDvfr 80
Cdd:PRK11607 19 LLEIRNLTKSF---DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aenIGYIFQNFNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQR 160
Cdd:PRK11607 93 ---INMMFQSYALFPHMTVEQNIAFG-----------LKQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDE 213
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQ 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-211 |
3.39e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 108.71 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhkNDAKPTL-NIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqRDVFR 80
Cdd:COG1132 340 IEFENVSFSY--PGDRPVLkDI-SLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQNFNLLpYLTPIENVTLGCefsksrkqkalqqttePKPSLQ--KEAIRLLTA----LGLSEPYHSKdV---- 150
Cdd:COG1132 414 -RQIGVVPQDTFLF-SGTIRENIRYGR----------------PDATDEevEEAAKAAQAhefiEALPDGYDTV-Vgerg 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 151 ASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTAN----RESFIKLlfeqakRANSTLVFVSH 211
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERL------MKGRTTIVIAH 533
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-225 |
8.19e-27 |
|
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: 102.57 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTLNIPtlridKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVfra 81
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFA-----QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 eniGYIFQNFNLLPYLTPIENVTLGceFSKSRKQKALQQttepkpslqkEAIRLLTA-LGLSEpYHSKDVASLSIGQQQR 160
Cdd:cd03298 73 ---SMLFQENNLFAHLTVEQNVGLG--LSPGLKLTAEDR----------QAIEVALArVGLAG-LEKRLPGELSGGERQR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD-ETLKPLFNRAISL 225
Cdd:cd03298 137 VALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQpEDAKRLAQRVVFL 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-214 |
1.23e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 105.11 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfraeNIGYIFQNFNLLPYLTPIENVT 104
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER------GVGMVFQSYALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 105 LGCEFSKSRKQKALQQTTEPKPSLQkeairlLTALGLSEPyhsKDvasLSIGQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:PRK11000 98 FGLKLAGAKKEEINQRVNQVAEVLQ------LAHLLDRKP---KA---LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190
....*....|....*....|....*....|...
gi 490726575 185 TANResfIKLLFEQA---KRANSTLVFVSHDET 214
Cdd:PRK11000 166 AALR---VQMRIEISrlhKRLGRTMIYVTHDQV 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-212 |
1.26e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 103.24 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVtfkWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqrdvfr 80
Cdd:PRK11248 1 MLQISHL---YADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AENiGYIFQNFNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQR 160
Cdd:PRK11248 70 AER-GVVFQNEGLLPWRNVQDNVAFG-----------LQLAGVEKMQRLEIAHQMLKKVGLEG-AEKRYIWQLSGGQRQR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK11248 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-212 |
2.12e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.45 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 4 LDNVTFKWHKNDakpTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqrdvfraEN 83
Cdd:PRK11247 15 LNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR---------ED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 84 IGYIFQNFNLLPYLTPIENVTLGCefsksrkqkalqqttepKPSLQKEAIRLLTALGLSEpyHSKD-VASLSIGQQQRVA 162
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGLGL-----------------KGQWRDAALQALAAVGLAD--RANEwPAALSGGQKQRVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 163 AARAFIGSPELIIADEPTSALDTANR---ESFIKLLFEQakrANSTLVFVSHD 212
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRiemQDLIESLWQQ---HGFTVLLVTHD 193
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-225 |
2.95e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 100.79 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 3 ELDNVTFKWHKNdaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNtlsntQRDvfRAE 82
Cdd:cd03226 1 RIENISFSYKKG--TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-----AKE--RRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 83 NIGYIFQNFNllpYLTPIENVTLGCEFSKSRKQKALQQTTEpkpslqkeairLLTALGLSEpYHSKDVASLSIGQQQRVA 162
Cdd:cd03226 72 SIGYVMQDVD---YQLFTDSVREELLLGLKELDAGNEQAET-----------VLKDLDLYA-LKERHPLSLSGGQKQRLA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490726575 163 AARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVfVSHD-ETLKPLFNRAISL 225
Cdd:cd03226 137 IAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIV-ITHDyEFLAKVCDRVLLL 199
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-212 |
5.37e-26 |
|
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: 101.76 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKND--AKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVF 79
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RaENIGYIFQN-----FNLlpylTPIENVTLGCE-FSKSrKQKALQQTtepkpslqKEAIRLLtalGLSEPYHSKDVASL 153
Cdd:TIGR04521 81 R-KKVGLVFQFpehqlFEE----TVYKDIAFGPKnLGLS-EEEAEERV--------KEALELV---GLDEEYLERSPFEL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490726575 154 SIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:TIGR04521 144 SGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHS 202
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-212 |
9.63e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 102.12 E-value: 9.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAEnIGYIFQNfnllPY--LTPIE 101
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRR-MQMVFQD----PYasLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 102 NV--TLGcefsksrkqKALQ-QTTEPKPSLQKEAIRLLTALGLSePYHskdvAS-----LSIGQQQRVAAARAFIGSPEL 173
Cdd:COG4608 113 TVgdIIA---------EPLRiHGLASKAERRERVAELLELVGLR-PEH----ADrypheFSGGQRQRIGIARALALNPKL 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 490726575 174 IIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG4608 179 IVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-212 |
1.73e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRIlnrdlntlsntQRDVfraeNIGYIFQNFNLLPYLTPIENV 103
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----------PKGL----RIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGceFS-----KSRKQKALQQTTEPKPSLQK------------------EAIRLLTALGLSEPYHSKDVASLSIGQQQR 160
Cdd:COG0488 83 LDG--DAelralEAELEELEAKLAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTanrESfIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDL---ES-IEWLEEFLKNYPGTVLVVSHD 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-215 |
2.86e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.79 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 30 GEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAEnIGYIFQNFNLLPYLTPIENVTLGCEF 109
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTVYDNVAIPLII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 110 SKSRKQkalqqttepkpSLQKEAIRLLTALGLSEPYHSKDVaSLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRE 189
Cdd:PRK10908 107 AGASGD-----------DIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180
....*....|....*....|....*.
gi 490726575 190 SFIKlLFEQAKRANSTLVFVSHDETL 215
Cdd:PRK10908 175 GILR-LFEEFNRVGVTVLMATHDIGL 199
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-226 |
8.46e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.81 E-value: 8.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFkwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRiLNRDLNTLSNTQRdvfr 80
Cdd:COG4178 362 ALALEDLTL--RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-RPAGARVLFLPQR---- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aenigyifqnfnllPYLtPIenVTLgcefsksrkqkaLQQTTEPKPSLQ---KEAIRLLTALGLSEPYHSKDVAS----- 152
Cdd:COG4178 435 --------------PYL-PL--GTL------------REALLYPATAEAfsdAELREALEAVGLGHLAERLDEEAdwdqv 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfeQAKRANSTLVFVSHDETLKPLFNRAISLV 226
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELT 557
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-212 |
6.72e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 97.61 E-value: 6.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTfkwhKN-DAK-PTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDv 78
Cdd:PRK11650 3 GLKLQAVR----KSyDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 fraenIGYIFQNFNLLPYLTPIENVTLGCefsKSRKQkalqqttePKPSLQK---EAIRLltaLGLsEPYHSKDVASLSI 155
Cdd:PRK11650 78 -----IAMVFQNYALYPHMSVRENMAYGL---KIRGM--------PKAEIEErvaEAARI---LEL-EPLLDRKPRELSG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 156 GQQQRVAAARAFIGSPELIIADEPTSALDTANR-----EsfIKLLfeqAKRANSTLVFVSHD 212
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRvqmrlE--IQRL---HRRLKTTSLYVTHD 194
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-212 |
6.72e-24 |
|
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: 99.05 E-value: 6.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRIlnrDLNTLSNTQRDVFrA 81
Cdd:COG4618 331 LSVENLTVV-PPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL---DGADLSQWDREEL-G 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLPYlTPIENVtlgCEFsksrkqkalqqtTEPKPSLQKEAIRLLTA----LGLSEPYHSK---DVASLS 154
Cdd:COG4618 406 RHIGYLPQDVELFDG-TIAENI---ARF------------GDADPEKVVAAAKLAGVhemiLRLPDGYDTRigeGGARLS 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHD 212
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKARGATVVVITHR 526
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-211 |
1.21e-23 |
|
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: 94.60 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDlntLSNTQRDVFRa 81
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQN---FNllpyLTPIENVTLGCefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEPYHSKdVAS----LS 154
Cdd:cd03253 75 RAIGVVPQDtvlFN----DTIGYNIRYGR----------PDATDEEVIEAAKAAQIHDKIMRFPDGYDTI-VGErglkLS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKraNSTLVFVSH 211
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAH 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-211 |
1.52e-23 |
|
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: 93.97 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTfKWHKNDAKPTLNIP--TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsnTQRDV 78
Cdd:cd03266 1 MITADALT-KRFRDVKKTVQAVDgvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK---EPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 FRaeNIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKQKALQQTTEpkpslqkeairLLTALGLsEPYHSKDVASLSIGQQ 158
Cdd:cd03266 77 RR--RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEE-----------LADRLGM-EELLDRRVGGFSTGMR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSH 211
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI-RQLRALGKCILFSTH 194
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-211 |
2.10e-23 |
|
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: 94.28 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkptLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGIN--TPS---SGNIRILNRDLNtlsNTQR 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEA---LKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlVPGvriEGKVLFDGQDIY---DKKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 77 DVFRA-ENIGYIFQNFNLLPyLTPIENVTLGCEFSKSRKQKALQQTTEPkpSLQKEAI------RLltalglsepyhSKD 149
Cdd:TIGR00972 76 DVVELrRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEE--SLKKAALwdevkdRL-----------HDS 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 150 VASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKraNSTLVFVSH 211
Cdd:TIGR00972 142 ALGLSGGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKK--KYTIVIVTH 201
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-211 |
2.20e-23 |
|
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: 93.50 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvfraenIGYIFQNFNLLPYLTPIENV 103
Cdd:cd03269 20 SFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR--------IGYLPEERGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEFSKSRKQKAlqqttepkpslQKEAIRLLTALGLSEpYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:cd03269 92 VYLAQLKGLKKEEA-----------RRRIDEWLERLELSE-YANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180
....*....|....*....|....*...
gi 490726575 184 DTANRESFIKLLFEQaKRANSTLVFVSH 211
Cdd:cd03269 160 DPVNVELLKDVIREL-ARAGKTVILSTH 186
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-212 |
5.50e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.03 E-value: 5.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLntlsnTQRDVFR 80
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-----TEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 A-ENIGYIFQN-FNLLPYLTPIENVTLGCEfsksRKQKALQQTTEPkpslQKEAIRLltaLGLSEpYHSKDVASLSIGQQ 158
Cdd:PRK13650 79 IrHKIGMVFQNpDNQFVGATVEDDVAFGLE----NKGIPHEEMKER----VNEALEL---VGMQD-FKEREPARLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHD 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
5.56e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.90 E-value: 5.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvFR 80
Cdd:PRK13632 7 MIKVENVSFSY-PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE---IR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQN-FNLLPYLTPIENVTLGCEFSKSrkqkalqqttepKPSLQKEAIRLLTALGLSEPYHSKDVASLSIGQQQ 159
Cdd:PRK13632 83 -KKIGIIFQNpDNQFIGATVEDDIAFGLENKKV------------PPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHD 202
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-211 |
5.58e-23 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 92.93 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvFRA 81
Cdd:cd03252 1 ITFEHVRFRY-KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW---LRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 EnIGYIFQNfNLLPYLTPIENVTLgcefsksrkqkalqqtTEPKPSLQK--EAIRLLTA----LGLSEPYHS---KDVAS 152
Cdd:cd03252 77 Q-VGVVLQE-NVLFNRSIRDNIAL----------------ADPGMSMERviEAAKLAGAhdfiSELPEGYDTivgEQGAG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfeQAKRANSTLVFVSH 211
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNM--HDICAGRTVIIIAH 195
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
25-184 |
5.91e-23 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 93.33 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRI--------LNRDLNTLSNTQRDV--FRAeNIGYIFQNFNLL 94
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVggeeirlkPDRDGELVPADRRQLqrIRT-RLGMVFQSFNLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 95 PYLTPIENVT------LGcefsKSRKQkALQQttepkpslqkeAIRLLTALGLsepYHSKDV--ASLSIGQQQRVAAARA 166
Cdd:COG4598 108 SHMTVLENVIeapvhvLG----RPKAE-AIER-----------AEALLAKVGL---ADKRDAypAHLSGGQQQRAAIARA 168
|
170
....*....|....*...
gi 490726575 167 FIGSPELIIADEPTSALD 184
Cdd:COG4598 169 LAMEPEVMLFDEPTSALD 186
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-185 |
1.22e-22 |
|
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: 91.91 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKnDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLN--TLSNTQRdvf 79
Cdd:cd03251 1 VEFKNVTFRYPG-DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 raeNIGYIFQNFNLLpYLTPIENVTLGcefsksrKQKALQQTTEpkpslqkEAIRLLTAL----GLSEPYHSK---DVAS 152
Cdd:cd03251 77 ---QIGLVSQDVFLF-NDTVAENIAYG-------RPGATREEVE-------EAARAANAHefimELPEGYDTVigeRGVK 138
|
170 180 190
....*....|....*....|....*....|...
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDT 185
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-212 |
2.09e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.95 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNT--QRDVFRAENI-------GYIFQNFNLL 94
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgQLKVADKNQLrllrtrlTMVFQHFNLW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 95 PYLTPIENVTlgcefsksrkQKALQQTTEPKPSLQKEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELI 174
Cdd:PRK10619 105 SHMTVLENVM----------EAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 490726575 175 IADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHD 212
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIM-QQLAEEGKTMVVVTHE 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-212 |
2.84e-22 |
|
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: 93.25 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 35 LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNtlSNTQRDVFRAEN--IGYIFQNFNLLPYLTPIENVTLGCEFSKS 112
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLPPEKrrIGYVFQEARLFPHLSVRGNLRYGMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 113 rkqkalqqttepkPSLQKEAIRLLTALGLsEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFI 192
Cdd:TIGR02142 106 -------------SERRISFERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180
....*....|....*....|
gi 490726575 193 KLLFEQAKRANSTLVFVSHD 212
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHS 191
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-214 |
3.73e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.35 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGniRILNRDLNTLSNTQRDVfr 80
Cdd:PRK13648 7 IIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQAITDDNFEKL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AENIGYIFQNfnllpyltPiENVTLGcEFSKSRKQKALQQTTEPKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQR 160
Cdd:PRK13648 82 RKHIGIVFQN--------P-DNQFVG-SIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLE-RADYEPNALSGGQKQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDET 214
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS 204
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
27-212 |
5.16e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.05 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 27 IDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlSNTQrdvFRAENIGYIFQNFN--LLPYLT------ 98
Cdd:COG4167 36 LEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY-GDYK---YRCKHIRMIFQDPNtsLNPRLNigqile 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 99 -PienvtlgcefsksrkqkaLQQTTEPKPSLQKEAIRL-LTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIA 176
Cdd:COG4167 112 eP------------------LRLNTDLTAEEREERIFAtLRLVGLLPEHANFYPHMLSSGQKQRVALARALILQPKIIIA 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 490726575 177 DEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG4167 174 DEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-212 |
5.23e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.90 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 13 KNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAEnIGYIFQN-- 90
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDsi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 91 --FNllPYLT-------PIENVTlgcEFSKSRKQKALQQttepkpslqkeairLLTALGLSEPYHSKDVASLSIGQQQRV 161
Cdd:PRK10419 100 saVN--PRKTvreiirePLRHLL---SLDKAERLARASE--------------MLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHD 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-211 |
9.36e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.78 E-value: 9.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTfkwhK-------NDakptlNIpTLRIDKGE-HIFLhGPSGVGKSTLLALLAGINTPSSGNIRILNRDLnTLS 72
Cdd:COG3845 5 ALELRGIT----KrfggvvaND-----DV-SLTVRPGEiHALL-GENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 73 NTqRDVFRAeNIGYIFQNFNLLPYLTPIENVTLGcefsksrkqkalqqtTEPKPSLQ---KEAIRLLTALglSEPYH--- 146
Cdd:COG3845 73 SP-RDAIAL-GIGMVHQHFMLVPNLTVAENIVLG---------------LEPTKGGRldrKAARARIREL--SERYGldv 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 147 --SKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSH 211
Cdd:COG3845 134 dpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEIL-RRLAAEGKSIIFITH 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-212 |
1.15e-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: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRilnrdlntlsntqrdvfR 80
Cdd:COG0488 315 VLELEGLSKSY---GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-----------------L 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AEN--IGYIFQNFNLL-PYLTPIENVtlgcefsksrkQKALQQTTEpkpslqKEAIRLLTALGLSEPYHSKDVASLSIGQ 157
Cdd:COG0488 375 GETvkIGYFDQHQEELdPDKTVLDEL-----------RDGAPGGTE------QEVRGYLGRFLFSGDDAFKPVGVLSGGE 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLL--FEqakranSTLVFVSHD 212
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALddFP------GTVLLVSHD 488
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-219 |
1.29e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 92.37 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsNTQRDVFRAeNIGYIFQNFNLLPYLTPIENV 103
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF--NGPKSSQEA-GIGIIHQELNLIPQLTIAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEFSKS------RKQKAlqqttepkpslqkEAIRLLTALGLSepYHSKD-VASLSIGQQQRVAAARAFIGSPELIIA 176
Cdd:PRK10762 101 FLGREFVNRfgridwKKMYA-------------EADKLLARLNLR--FSSDKlVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490726575 177 DEPTSALDTANRESFIKLLFEqAKRANSTLVFVSHdeTLKPLF 219
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRE-LKSQGRGIVYISH--RLKEIF 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
24-183 |
2.01e-21 |
|
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: 88.26 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvFRAeNIGYIFQNFNLLPYLTPIENV 103
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARA-GIGYVPEGRRIFPELTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEFsksRKQKALQQTTEpkpslqkEAIRLLTALGlsEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:cd03224 97 LLGAYA---RRRAKRKARLE-------RVYELFPRLK--ERRKQL-AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-212 |
2.90e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.40 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVT--FKWHK--NDAkptlnipTLRIDKGEhIF-LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNtlsntq 75
Cdd:COG4152 1 MLELKGLTkrFGDKTavDDV-------SFTVPKGE-IFgLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 76 RDVFRaeNIGYifqnfnlLP-----YltpienvtlgcefsksRKQKALQQTT-------EPKPSLQKEAIRLLTALGLSE 143
Cdd:COG4152 67 PEDRR--RIGY-------LPeerglY----------------PKMKVGEQLVylarlkgLSKAEAKRRADEWLERLGLGD 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726575 144 pYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRaNSTLVFVSHD 212
Cdd:COG4152 122 -RANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQ 188
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-218 |
3.73e-21 |
|
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: 87.03 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsntQRDVfRAENIGYIFQNFNLLPYLTPIENV 103
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE----QRDE-PHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEFSKSRKQKALQqttepkpslqkeairLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:TIGR01189 95 HFWAAIHGGAQRTIED---------------ALAAVGLTGFEDLP-AAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 490726575 184 DTANRESFIKLLFEQAKRANSTLVFVSHDETLKPL 218
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-212 |
6.37e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.09 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAENIGYIFQNFNLLPYLTPIENV 103
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEFSKSrkqkalqqttePKPSLQKEAIRLLTALGLsEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:PRK10070 128 AFGMELAGI-----------NAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180
....*....|....*....|....*....
gi 490726575 184 DTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-226 |
8.70e-21 |
|
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: 85.28 E-value: 8.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKwhKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILnrdlntlsnTQRDVFra 81
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP---------EGEDLL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 enigYIFQnfnlLPYLTPienVTLgcefsksrkqkalqqttepkpslqKEAIRlltalglsepYHSKDVasLSIGQQQRV 161
Cdd:cd03223 68 ----FLPQ----RPYLPL---GTL------------------------REQLI----------YPWDDV--LSGGEQQRL 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESfiklLFEQAKRANSTLVFVSHDETLKPLFNRAISLV 226
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDR----LYQLLKELGITVISVGHRPSLWKFHDRVLDLD 161
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-212 |
1.13e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.93 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTL-SNTQRDVfr 80
Cdd:PRK13640 6 VEFKHVSFTY-PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLtAKTVWDI-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AENIGYIFQN-FNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQQ 159
Cdd:PRK13640 83 REKVGIVFQNpDNQFVGATVGDDVAFG-----------LENRAVPRPEMIKIVRDVLADVGMLD-YIDSEPANLSGGQKQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-212 |
1.21e-20 |
|
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: 89.74 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTL-LALLAGIntPSSGNIRILNRDLNTLSNTQRDVFRAEnIGYIFQNfnllPY--LTPI 100
Cdd:COG4172 306 SLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQD----PFgsLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 101 ENVTlgcefsksrkqkalQQTTEP----KPSLQKE-----AIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSP 171
Cdd:COG4172 379 MTVG--------------QIIAEGlrvhGPGLSAAerrarVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEP 444
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490726575 172 ELIIADEPTSALDTANRESFIKLLFE-QAKRaNSTLVFVSHD 212
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQILDLLRDlQREH-GLAYLFISHD 485
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-225 |
1.26e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.01 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsntQRDVFrAENIGYIFQNFNLLPYLTPIENVT 104
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF----QRDSI-ARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 105 LGCEF-SKSRKQKALQQTTepkpslqkeairlLTALGlsepyhSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:cd03231 96 FWHADhSDEQVEEALARVG-------------LNGFE------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490726575 184 DTANRESFIKLLFEQAKRANSTLVFVSHDETLKPLFNRAISL 225
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-211 |
1.45e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.45 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKND---AKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRD 77
Cdd:PRK13633 4 MIKCKNVSYKYESNEestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 78 VFRAeniGYIFQN-FNLLPYLTPIENVTLGCEfsksrkqkalqqttepKPSLQKEAIRL-----LTALGLSEpYHSKDVA 151
Cdd:PRK13633 84 RNKA---GMVFQNpDNQIVATIVEEDVAFGPE----------------NLGIPPEEIRErvdesLKKVGMYE-YRRHAPH 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 152 SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSH 211
Cdd:PRK13633 144 LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-212 |
1.98e-20 |
|
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: 85.88 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTLNiptLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfra 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVS---FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLPYLTPIENVTLgcefsksrkQKALQQTtePKPSLQKEAIRLLTALGLSEPYHsKDVASLSIGQQQRV 161
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYI---------HARLYGV--PGAERRERIDELLDFVGLLEAAD-RLVKTYSGGMRRRL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHY 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-185 |
2.69e-20 |
|
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: 85.74 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNdaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqRDVFRa 81
Cdd:cd03254 3 IEFENVNFSYDEK--KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNfnllPYL---TPIENVTLGCEFSKSRKQKALQQTTEPKPSLQKEAIRLLTALGlsepyhsKDVASLSIGQQ 158
Cdd:cd03254 77 SMIGVVLQD----TFLfsgTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLG-------ENGGNLSQGER 145
|
170 180
....*....|....*....|....*..
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDT 185
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDT 172
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-186 |
5.23e-20 |
|
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: 84.58 E-value: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKndaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNrdlntlSNTQRDVFRA 81
Cdd:cd03268 1 LKTNDLTKTYGK---KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG------KSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLPYLTPIENVTLGCEFSKSRKqkalqqttepkpslqKEAIRLLTALGLSEPYHSKdVASLSIGQQQRV 161
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRK---------------KRIDEVLDVVGLKDSAKKK-VKGFSLGMKQRL 135
|
170 180
....*....|....*....|....*
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTA 186
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPD 160
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-211 |
5.81e-20 |
|
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: 83.25 E-value: 5.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqrdVFRAEN--IGYIFQnfnllpyltpie 101
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS-----PRDARRagIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 102 nvtlgcefsksrkqkalqqttepkpslqkeairlltalglsepyhskdvasLSIGQQQRVAAARAFIGSPELIIADEPTS 181
Cdd:cd03216 83 ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190
....*....|....*....|....*....|
gi 490726575 182 ALDTANRESFIKLLfEQAKRANSTLVFVSH 211
Cdd:cd03216 112 ALTPAEVERLFKVI-RRLRAQGVAVIFISH 140
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-211 |
6.40e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.85 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTqrdVFRa 81
Cdd:PRK10790 341 IDIDNVSFAYR--DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLR- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLPYlTPIENVTLGCEFSKSRKQKALqqttepkpslqkEAIRLLT-ALGLSEPYHSK---DVASLSIGQ 157
Cdd:PRK10790 415 QGVAMVQQDPVVLAD-TFLANVTLGRDISEEQVWQAL------------ETVQLAElARSLPDGLYTPlgeQGNNLSVGQ 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfeQAKRANSTLVFVSH 211
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL--AAVREHTTLVVIAH 533
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-215 |
6.68e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.47 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 33 IFlhGPSGVGKSTLLALLAGINTPSSGNIRILNRdlnTLSNTQRDVFRA---ENIGYIFQNFNLLPYLTPIENVTLGCef 109
Cdd:PRK11144 29 IF--GRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLFDAEKGICLPpekRRIGYVFQDARLFPHYKVRGNLRYGM-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 110 sksrkqkalqqttepKPSLQKEAIRLLTALGLsEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRE 189
Cdd:PRK11144 102 ---------------AKSMVAQFDKIVALLGI-EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180
....*....|....*....|....*...
gi 490726575 190 SFIKLLFEQAKRANSTLVFVSH--DETL 215
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHslDEIL 193
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-212 |
8.09e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.17 E-value: 8.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 37 GPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAEnIGYIFQNfnllPY--LTPienvtlgcefsksrK 114
Cdd:PRK11308 48 GESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQK-IQIVFQN----PYgsLNP--------------R 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 115 QKALQQTTEP--------KPSLQKEAIRLLTALGLsEPYHSKDVASL-SIGQQQRVAAARAFIGSPELIIADEPTSALDT 185
Cdd:PRK11308 109 KKVGQILEEPllintslsAAERREKALAMMAKVGL-RPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180
....*....|....*....|....*..
gi 490726575 186 ANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-212 |
1.16e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.44 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKndaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQ----R 76
Cdd:PRK13548 2 MLEARNLSVRLGG---RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 77 DVFRaenigyifQNFNLLPYLTPIENVTLGCEfSKSRKQKALQQTTEpkpslqkEAIRLLTALGLSE-PYHskdvaSLSI 155
Cdd:PRK13548 79 AVLP--------QHSSLSFPFTVEEVVAMGRA-PHGLSRAEDDALVA-------AALAQVDLAHLAGrDYP-----QLSG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726575 156 GQQQRVAAARAFI------GSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK13548 138 GEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHD 200
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-219 |
1.38e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.90 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 11 WHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGniRILnRDLNTLSNTQRDVFR-AENIGYIFQ 89
Cdd:PRK13636 13 YNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSG--RIL-FDGKPIDYSRKGLMKlRESVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 90 N-FNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLsEPYHSKDVASLSIGQQQRVAAARAFI 168
Cdd:PRK13636 90 DpDNQLFSASVYQDVSFG-----------AVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 169 GSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDETLKPLF 219
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLY 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
1.59e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.40 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNtlSNTQRDVfRA 81
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKWV-RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 EnIGYIFQN-----FNllpyLTPIENVTLGCEFSKSRKQKALQQTtepkpslqKEAIRLLTALGLSE--PYHskdvasLS 154
Cdd:PRK13647 80 K-VGLVFQDpddqvFS----STVWDDVAFGPVNMGLDKDEVERRV--------EEALKAVRMWDFRDkpPYH------LS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRAnSTLVFVSHD 212
Cdd:PRK13647 141 YGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQG-KTVIVATHD 197
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-212 |
2.01e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.14 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRAEnIGYIFQNfnLLPYLTPieNV 103
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQD--PLASLNP--RM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGcefsksrkqkalQQTTEP----KPSLQKEAIR-----LLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELI 174
Cdd:PRK15079 116 TIG------------EIIAEPlrtyHPKLSRQEVKdrvkaMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 490726575 175 IADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-201 |
2.14e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsntQRDVFRAenigyifqnfNLL--------- 94
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR----QRDEYHQ----------DLLylghqpgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 95 PYLTPIENVTLGCefsksrkqkALQQTTEPkpslqkEAIR-LLTALGLSE----PyhskdVASLSIGQQQRVAAARAFIG 169
Cdd:PRK13538 87 TELTALENLRFYQ---------RLHGPGDD------EALWeALAQVGLAGfedvP-----VRQLSAGQQRRVALARLWLT 146
|
170 180 190
....*....|....*....|....*....|..
gi 490726575 170 SPELIIADEPTSALDTANRESFIKLLFEQAKR 201
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQHAEQ 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-212 |
3.40e-19 |
|
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: 85.51 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKS----TLLALLAGINTPSSGNIRILNRDLNTLSNTQ-RDVfRAENIGYIFQ------Nfnl 93
Cdd:COG4172 31 FDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElRRI-RGNRIAMIFQepmtslN--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 94 lPYLTpIEnvtlgcefsksrkqkalQQTTEP--------KPSLQKEAIRLLTALGLSEP------Y-HSkdvasLSIGQQ 158
Cdd:COG4172 107 -PLHT-IG-----------------KQIAEVlrlhrglsGAAARARALELLERVGIPDPerrldaYpHQ-----LSGGQR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
3.43e-19 |
|
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: 85.49 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntQRDVFRA 81
Cdd:TIGR02868 335 LELRDLSAGY--PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD--QDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 enIGYIFQNfnllPYL---TPIENVTLGC-EFSKSRKQKALqqttepkpslqkEAIRL---LTAL--GLSEPYHSkDVAS 152
Cdd:TIGR02868 411 --VSVCAQD----AHLfdtTVRENLRLARpDATDEELWAAL------------ERVGLadwLRALpdGLDTVLGE-GGAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFeqAKRANSTLVFVSHDE 213
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL--AALSGRTVVLITHHL 530
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-212 |
3.98e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.24 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSG--NIRILNR--DLNTLSNTQRDvfRAEN-IGYIFQNFNLLPYLT 98
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEwvDMTKPGPDGRG--RAKRyIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 99 PIENVT--LGCEFsksrkqkalqqttePKPSLQKEAIRLLTALGLSEPYH----SKDVASLSIGQQQRVAAARAFIGSPE 172
Cdd:TIGR03269 382 VLDNLTeaIGLEL--------------PDELARMKAVITLKMVGFDEEKAeeilDKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490726575 173 LIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHD 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-211 |
4.16e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTqrdvFRAEN-IGYIFQNFNLLPYLTPIEN 102
Cdd:PRK09700 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK----LAAQLgIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 103 VTLGcefsKSRKQKALQQTTEPKPSLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIADEPTSA 182
Cdd:PRK09700 101 LYIG----RHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEK-VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180
....*....|....*....|....*....
gi 490726575 183 LDTANREsFIKLLFEQAKRANSTLVFVSH 211
Cdd:PRK09700 176 LTNKEVD-YLFLIMNQLRKEGTAIVYISH 203
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-212 |
5.10e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.14 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNtlSNTQRDVFRa 81
Cdd:PRK13635 6 IRVEHISFRY-PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS--EETVWDVRR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 eNIGYIFQN-FNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQK---EAIRL--LTALGLSEPYHskdvasLSI 155
Cdd:PRK13635 82 -QVGMVFQNpDNQFVGATVQDDVAFG-----------LENIGVPREEMVErvdQALRQvgMEDFLNREPHR------LSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 156 GQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHD 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-211 |
5.32e-19 |
|
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: 80.82 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVfra 81
Cdd:cd03247 1 LSINNVSFSYPEQE-QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 enIGYIFQNfnllPYLtpienvtlgceFSKSrkqkalqqttepkpslqkeairLLTALGlsepyhskdvASLSIGQQQRV 161
Cdd:cd03247 77 --ISVLNQR----PYL-----------FDTT----------------------LRNNLG----------RRFSGGERQRL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKraNSTLVFVSH 211
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITH 155
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-211 |
7.37e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 82.39 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkptL-NIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGIN--TPS---SGNIRILNRDLNtlsNTQ 75
Cdd:COG1117 12 IEVRNLNVYYGDKQA---LkDI-NLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDGEDIY---DPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 76 RDV--FRAeNIGYIFQNFNLLP---YltpiENVTLGCEFSKSRKQKALQQTTEPkpSLQKEAI------RLltalglsep 144
Cdd:COG1117 85 VDVveLRR-RVGMVFQKPNPFPksiY----DNVAYGLRLHGIKSKSELDEIVEE--SLRKAALwdevkdRL--------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 145 yhSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALD---TANRESFIKLLfeqakRANSTLVFVSH 211
Cdd:COG1117 149 --KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpisTAKIEELILEL-----KKDYTIVIVTH 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-211 |
9.00e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.51 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGiNTPSSGNIRILNRDLNTLSNTQrdvFRaENIGYIFQNfNLLPYLTPIENV 103
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPES---WR-KHLSWVGQN-PQLPHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLG-CEFSKSRKQKALQQttepkpSLQKEAIRLLtALGLSEPYhSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSA 182
Cdd:PRK11174 444 LLGnPDASDEQLQQALEN------AWVSEFLPLL-PQGLDTPI-GDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180
....*....|....*....|....*....
gi 490726575 183 LDtANRESFIKLLFEQAKRANSTLvFVSH 211
Cdd:PRK11174 516 LD-AHSEQLVMQALNAASRRQTTL-MVTH 542
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
1.01e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.43 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRIlnrDLNTLSNTQRDVFR 80
Cdd:PRK13639 1 ILETRDLKYSY--PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI---KGEPIKYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 A-ENIGYIFQNF-NLLPYLTPIENVTLG---CEFSKSRKQKALqqttepkpslqKEAirlLTALGLsEPYHSKDVASLSI 155
Cdd:PRK13639 76 VrKTVGIVFQNPdDQLFAPTVEEDVAFGplnLGLSKEEVEKRV-----------KEA---LKAVGM-EGFENKPPHHLSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 156 GQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRAnSTLVFVSHDETLKPLFNRAISLVS 227
Cdd:PRK13639 141 GQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMS 211
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-215 |
1.85e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 82.48 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 26 RIDKGEHIFLHGPSGVGKS-TLLALLAGINTP---SSGNIRILNRDLNTLSNTQRDVFRAENIGYIFQNfnLLPYLTPIe 101
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQD--PMTSLNPC- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 102 nVTLGCEFSKSRKqkaLQQTTEPKPSLQKeAIRLLTALGLSEPYHSKDV--ASLSIGQQQRVAAARAFIGSPELIIADEP 179
Cdd:PRK11022 106 -YTVGFQIMEAIK---VHQGGNKKTRRQR-AIDLLNQVGIPDPASRLDVypHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 490726575 180 TSALDTANRESFIKLLFEQAKRANSTLVFVSHDETL 215
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLAL 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-211 |
2.21e-18 |
|
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: 80.66 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvFRa 81
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW---LR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLpYLTPIENVTLGcefsksrKQKALQQTTEpkpslqkEAIRLLTA----LGLSEPYHSK--DVAS-LS 154
Cdd:cd03249 77 SQIGLVSQEPVLF-DGTIAENIRYG-------KPDATDEEVE-------EAAKKANIhdfiMSLPDGYDTLvgERGSqLS 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALDTANrESFIKLLFEQAKRANSTLVfVSH 211
Cdd:cd03249 142 GGQKQRIAIARALLRNPKILLLDEATSALDAES-EKLVQEALDRAMKGRTTIV-IAH 196
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-215 |
2.78e-18 |
|
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: 78.26 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKndaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRdlntlsntqrdvfra 81
Cdd:cd03221 1 IELENLSKTYGG---KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQnfnllpyltpienvtlgcefsksrkqkalqqttepkpslqkeairlltalglsepyhskdvasLSIGQQQRV 161
Cdd:cd03221 63 VKIGYFEQ---------------------------------------------------------------LSGGEKMRL 79
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANRESFIKLLfeqaKRANSTLVFVSHDETL 215
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYF 129
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-211 |
3.18e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKND--AKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDV 78
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 FRAENIGYIFQ-NFNLLPYLTPIENVTLGCEFSKSRKQKAlqqttepkpslQKEAIRLLTALGLSEPYHSKDVASLSIGQ 157
Cdd:PRK13643 81 PVRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKA-----------EKIAAEKLEMVGLADEFWEKSPFELSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDTANRESFIKlLFEQAKRANSTLVFVSH 211
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTH 202
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-212 |
3.49e-18 |
|
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: 80.07 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRdlntLSNTQRDVFRAeNIGYIF-QNFNLLPYLTPIEN 102
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKFLR-RIGVVFgQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 103 VTLgcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSA 182
Cdd:cd03267 116 FYL------------LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190
....*....|....*....|....*....|
gi 490726575 183 LDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHY 213
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-211 |
4.73e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 4.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 4 LDNVTFKWHKndakptlniptlridkGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNtLSNTqRDVFRAeN 83
Cdd:PRK11288 20 LDDISFDCRA----------------GQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-FAST-TAALAA-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 84 IGYIFQNFNLLPYLTPIENVTLGCEFSKS----RKQkalqqttepkpsLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQ 159
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPHKGgivnRRL------------LNYEAREQLEHLGVDIDPDTP-LKYLSIGQRQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALdtANREsfIKLLF---EQAKRANSTLVFVSH 211
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSL--SARE--IEQLFrviRELRAEGRVILYVSH 198
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-211 |
2.10e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.42 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 35 LHGPSGVGKSTLLallagintpssgniRILNRDLNTLSNTQ---------RDVFRAE------NIGYIFQNFNLLPYLTP 99
Cdd:PRK14247 34 LMGPSGSGKSTLL--------------RVFNRLIELYPEARvsgevyldgQDIFKMDvielrrRVQMVFQIPNPIPNLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 100 IENVTLGCEFSKSRKQKA-LQQTTepKPSLQKEAIRLLTALGLSEPyhskdVASLSIGQQQRVAAARAFIGSPELIIADE 178
Cdd:PRK14247 100 FENVALGLKLNRLVKSKKeLQERV--RWALEKAQLWDEVKDRLDAP-----AGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190
....*....|....*....|....*....|...
gi 490726575 179 PTSALDTANRESFIKLLFEQAKraNSTLVFVSH 211
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKK--DMTIVLVTH 203
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-212 |
2.11e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGInTPSSGNIRILNRDLNTLSNTQRDVFRAenigYIFQNFNLLP------YL 97
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRA----YLSQQQSPPFampvfqYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 98 tpienvtlgcefsksrkqkALQQTTEPKPSLQKEAIRLLT-ALGLsEPYHSKDVASLSIGQQQRVAAARAFI-------G 169
Cdd:COG4138 91 -------------------ALHQPAGASSEAVEQLLAQLAeALGL-EDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490726575 170 SPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHD 212
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLL-RELCQQGITVVMSSHD 192
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-211 |
2.32e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 80.06 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhkNDaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNirilnrDLnTLSNTQR----- 76
Cdd:PRK10938 261 IVLNNGVVSY--ND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSN------DL-TLFGRRRgsget 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 77 --DVFRaeNIGYIFQNFNLlPYL--TPIENVTLGCEFSKSrkqKALQQTTEpkpSLQKEAIRLLTALGLSE-----PYHS 147
Cdd:PRK10938 331 iwDIKK--HIGYVSSSLHL-DYRvsTSVRNVILSGFFDSI---GIYQAVSD---RQQKLAQQWLDILGIDKrtadaPFHS 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 148 kdvasLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRE---SFIKLLFEQakrANSTLVFVSH 211
Cdd:PRK10938 402 -----LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVLISE---GETQLLFVSH 460
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-211 |
2.99e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 78.25 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKND--AKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVF 79
Cdd:PRK13649 3 INLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RAENIGYIFQnF--NLLPYLTPIENVTLGCEFSKSRKQKALQqttepkpsLQKEAIRLltaLGLSEPYHSKDVASLSIGQ 157
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEA--------LAREKLAL---VGISESLFEKNPFELSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDTANRESFIKlLFEQAKRANSTLVFVSH 211
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVTH 203
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
24-180 |
4.55e-17 |
|
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: 76.79 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfRAENIGYIFQNFNLLPYLTPIENV 103
Cdd:TIGR03410 20 SLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER---ARAGIAYVPQGREIFPRLTVEENL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 104 TLGCEFSKSRKQKALQQTTEPKPSLQKeairLLTALGlsepyhskdvASLSIGQQQRVAAARAFIGSPELIIADEPT 180
Cdd:TIGR03410 97 LTGLAALPRRSRKIPDEIYELFPVLKE----MLGRRG----------GDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-188 |
5.68e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.43 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNV--TFKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdv 78
Cdd:COG1101 1 MLELKNLskTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 fRAENIGYIFQNfnllPY------LTPIENVTL--------GCEFSKSRKQKAlqqttepkpsLQKEAIRLLtALGLSEP 144
Cdd:COG1101 78 -RAKYIGRVFQD----PMmgtapsMTIEENLALayrrgkrrGLRRGLTKKRRE----------LFRELLATL-GLGLENR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490726575 145 YHSKdVASLSIGQQQRVAAARAFIGSPELIIADEPTSALD--TANR 188
Cdd:COG1101 142 LDTK-VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpkTAAL 186
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-212 |
6.84e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.44 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLntlsnTQRDVFR 80
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL-----TAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 -AENIGYIFQN-FNLLPYLTPIENVTLGcefsksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQ 158
Cdd:PRK13642 79 lRRKIGMVFQNpDNQFVGATVEDDVAFG-----------MENQGIPREEMIKRVDEALLAVNMLD-FKTREPARLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-211 |
7.20e-17 |
|
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: 75.67 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTF---KWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAG--INTPSSGNIRILNRDLntlsntQR 76
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL------DK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 77 DVFRAEnIGYIFQNFNLLPYLTPIENvtlgcefsksrkqkalqqttepkpslqkeairLLTALGLSepyhskdvaSLSIG 156
Cdd:cd03213 78 RSFRKI-IGYVPQDDILHPTLTVRET--------------------------------LMFAAKLR---------GLSGG 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 157 QQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRaNSTLVFVSH 211
Cdd:cd03213 116 ERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIH 169
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-212 |
1.34e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.56 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQ--RDV 78
Cdd:PRK13644 1 MIRLENVSYSY--PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgiRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 fraenIGYIFQNfnllPYL-----TPIENVTLGCEfsksrkqkalqQTTEPKPSLQKEAIRLLTALGLsEPYHSKDVASL 153
Cdd:PRK13644 79 -----VGIVFQN----PETqfvgrTVEEDLAFGPE-----------NLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 154 SIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESF---IKLLFEQAKransTLVFVSHD 212
Cdd:PRK13644 138 SGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVlerIKKLHEKGK----TIVYITHN 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
17-184 |
1.49e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.97 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 17 KPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLallagintpssgniRILNR--DLN-TLSNTQRDVFRAEN---------- 83
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLL--------------RSINRmnDLNpEVTITGSIVYNGHNiysprtdtvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 84 ----IGYIFQNFNLLPyLTPIENVTLGCEFSKSRKQKALQQTTEPkpSLQKEAI------RLL-TALGLSEpyhskdvas 152
Cdd:PRK14239 84 lrkeIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEK--SLKGASIwdevkdRLHdSALGLSG--------- 151
|
170 180 190
....*....|....*....|....*....|..
gi 490726575 153 lsiGQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:PRK14239 152 ---GQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-212 |
1.66e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKwhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvFR 80
Cdd:PRK10247 7 LLQLQNVGYL---AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQNfnllPYL---TPIENVTLGCEFsksRKQKalqqttePKPslqKEAIRLLTALGLSEPYHSKDVASLSIGQ 157
Cdd:PRK10247 81 -QQVSYCAQT----PTLfgdTVYDNLIFPWQI---RNQQ-------PDP---AIFLDDLERFALPDTILTKNIAELSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
6-212 |
1.70e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.07 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 6 NVTFKWHKND--AKPTLNIpTLRidKGEHIFLHGPSGVGKS----TLLALLAGiNTPSSGNIRILNRDLNTLSNTQRDVF 79
Cdd:PRK09473 19 RVTFSTPDGDvtAVNDLNF-SLR--AGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKELNKL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RAENIGYIFQN--FNLLPYLTPIENVTlgcEFSKSRKQKALQQTTEpkpslqkEAIRLLTALGLSE--------PYHskd 149
Cdd:PRK09473 95 RAEQISMIFQDpmTSLNPYMRVGEQLM---EVLMLHKGMSKAEAFE-------ESVRMLDAVKMPEarkrmkmyPHE--- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726575 150 vasLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK09473 162 ---FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-211 |
1.86e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.56 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSN-------- 73
Cdd:PRK11160 339 LTLNNVSFTYP-DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEaalrqais 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 74 --TQR-DVFRAenigyifqnfnllpylTPIENVTLGC-EFSKSRKQKALQQTTEPKpsLQKEAIRLLTALG-LSEPyhsk 148
Cdd:PRK11160 418 vvSQRvHLFSA----------------TLRDNLLLAApNASDEALIEVLQQVGLEK--LLEDDKGLNAWLGeGGRQ---- 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726575 149 dvasLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKraNSTLVFVSH 211
Cdd:PRK11160 476 ----LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH 532
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-212 |
2.03e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRidKGEHIFLHGPSGVGKSTL-LALLAGINtpSSGNIRILNRDLNTLSNTQRDVFRAEnIGYIFQNFN--LLPYLTPI 100
Cdd:PRK15134 308 TLR--PGETLGLVGESGSGKSTTgLALLRLIN--SQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPNssLNPRLNVL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 101 ENVTLGCEFsksrKQKALQqttepkpSLQKEA--IRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADE 178
Cdd:PRK15134 383 QIIEEGLRV----HQPTLS-------AAQREQqvIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190
....*....|....*....|....*....|....
gi 490726575 179 PTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-201 |
3.72e-16 |
|
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: 74.61 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGI--NTPS-SGNIRILNRDLNtlsntqRDVFRaENIGYIFQNFNLLPYLTPI 100
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGRveGGGTtSGQILFNGQPRK------PDQFQ-KCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 101 ENVT------LGCEFSKSRKQKalqqttepkpslqKEAIRLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELI 174
Cdd:cd03234 100 ETLTytailrLPRKSSDAIRKK-------------RVEDVLLRDLALTRIGGNL-VKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180
....*....|....*....|....*....
gi 490726575 175 IADEPTSALD--TANreSFIKLLFEQAKR 201
Cdd:cd03234 166 ILDEPTSGLDsfTAL--NLVSTLSQLARR 192
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-211 |
4.74e-16 |
|
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: 73.66 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKN--DAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRdlntlsntqrdvf 79
Cdd:cd03250 1 ISVEDASFTWDSGeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 raenIGYIFQNfnllPYL---TPIENVTLGCEFSKSRKQKALQQTtepkpSLQKEaIRLLTALGLSEpYHSKDVaSLSIG 156
Cdd:cd03250 68 ----IAYVSQE----PWIqngTIRENILFGKPFDEERYEKVIKAC-----ALEPD-LEILPDGDLTE-IGEKGI-NLSGG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490726575 157 QQQRVAAARAFIGSPELIIADEPTSALD--TANResfiklLFEQ----AKRANSTLVFVSH 211
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDahVGRH------IFENcilgLLLNNKTRILVTH 186
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-211 |
6.18e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.70 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKND--AKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVF 79
Cdd:PRK13637 3 IKIENLTHIYMEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RaeNIGYIFQ--NFNLLPyltpiENVTLGCEFSKSRkqkaLQQTTEPKPSLQKEAIRLLtalGLS-EPYHSKDVASLSIG 156
Cdd:PRK13637 83 K--KVGLVFQypEYQLFE-----ETIEKDIAFGPIN----LGLSEEEIENRVKRAMNIV---GLDyEDYKDKSPFELSGG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 157 QQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSH 211
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSH 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-211 |
6.34e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.12 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 20 LNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGInTPS---SGNIRILNRDLNtlSNTQRDVFRAeNIGYIFQNFNLLPY 96
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQ--ASNIRDTERA-GIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 97 LTPIENVTLGCEFSKSRKQKalqqttepKPSLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIA 176
Cdd:PRK13549 97 LSVLENIFLGNEITPGGIMD--------YDAMYLRAQKLLAQLKLDINPATP-VGNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190
....*....|....*....|....*....|....*
gi 490726575 177 DEPTSALDTANRESFIKLLfEQAKRANSTLVFVSH 211
Cdd:PRK13549 168 DEPTASLTESETAVLLDII-RDLKAHGIACIYISH 201
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-216 |
1.13e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNdakptLNiptLRIDKGEHIFLHGPSGVGKSTLLALLAGI--NTPSSGNIRILNRDLNtlsntqrdvf 79
Cdd:COG2401 36 VELRVVERYVLRD-----LN---LEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPDNQFG---------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 raenigyifQNFNLlpyltpIENVTLGCEFsksrkqkalqqttepkpslqKEAIRLLTALGLSEPY-HSKDVASLSIGQQ 158
Cdd:COG2401 98 ---------REASL------IDAIGRKGDF--------------------KDAVELLNAVGLSDAVlWLRRFKELSTGQK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALD--TANRESFIklLFEQAKRANSTLVFVSHDETLK 216
Cdd:COG2401 143 FRFRLALLLAERPKLLVIDEFCSHLDrqTAKRVARN--LQKLARRAGITLVVATHHYDVI 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-225 |
1.34e-15 |
|
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: 75.22 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINT--PSSGniRILNR------------- 66
Cdd:TIGR03269 1 IEVKNLTKKF---DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSG--RIIYHvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 67 -------------------DLNTLSNTQRDVFRaENIGYIFQ-NFNLLPYLTPIENVTlgcefsksrkqKALQQTTEPKP 126
Cdd:TIGR03269 76 skvgepcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVL-----------EALEEIGYEGK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 127 SLQKEAIRLLTALGLSepYHSKDVA-SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANST 205
Cdd:TIGR03269 144 EAVGRAVDLIEMVQLS--HRITHIArDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS 221
|
250 260
....*....|....*....|.
gi 490726575 206 LVFVSH-DETLKPLFNRAISL 225
Cdd:TIGR03269 222 MVLTSHwPEVIEDLSDKAIWL 242
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-188 |
1.36e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.48 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTfKWHKNdaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfra 81
Cdd:PRK13536 42 IDLAGVS-KSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNLLPYLTPIENVTLgceFSKSRKQKAlQQTTEPKPSLQKEAiRLltalglsEPYHSKDVASLSIGQQQRV 161
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLV---FGRYFGMST-REIEAVIPSLLEFA-RL-------ESKADARVSDLSGGMKRRL 181
|
170 180
....*....|....*....|....*..
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTANR 188
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHAR 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-212 |
2.36e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.32 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 4 LDNVTFKwhkndakptlniptlrIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDL--NTLSNTQRDVFRa 81
Cdd:PRK13641 23 LDNISFE----------------LEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpETGNKNLKKLRK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 eNIGYIFQnF--NLLPYLTPIENVTLGCEFSKSRKQKALQQttepkpslqkeAIRLLTALGLSEPYHSKDVASLSIGQQQ 159
Cdd:PRK13641 86 -KVSLVFQ-FpeAQLFENTVLKDVEFGPKNFGFSEDEAKEK-----------ALKWLKKVGLSEDLISKSPFELSGGQMR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKlLFEQAKRANSTLVFVSHD 212
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHN 204
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-212 |
2.52e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRaENIGYIFQNFNLLPYLTPIENV 103
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEfsksrkqkalQQTTEPKPSLQKEAIRLLTALGLSEPYHSKDvASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:PRK11831 106 AYPLR----------EHTQLPAPLLHSTVMMKLEAVGLRGAAKLMP-SELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180
....*....|....*....|....*....
gi 490726575 184 DTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK11831 175 DPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-211 |
3.86e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.75 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 27 IDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDL-NTLSNTQRDVFRaENIGYIFQnF--NLLPYLTPIENV 103
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLR-KKVGIVFQ-FpeHQLFEETVEKDI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLG-CEFSKSrKQKALQqttepkpsLQKEAIRLLtalGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSA 182
Cdd:PRK13634 108 CFGpMNFGVS-EEDAKQ--------KAREMIELV---GLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180
....*....|....*....|....*....
gi 490726575 183 LDTANRESFIKLLFEQAKRANSTLVFVSH 211
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-212 |
4.49e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.00 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 15 DAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsntQRDVFRAENI------GYIF 88
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF----GKDIFQIDAIklrkevGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 89 QNFNLLPYLTPIENVTLGCEFSKSRKQKALQQTTEpkpslqkEAIRlltALGLSEPYHSK---DVASLSIGQQQRVAAAR 165
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVE-------ECLR---KVGLWKEVYDRlnsPASQLSGGQQQRLTIAR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490726575 166 AFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRAnsTLVFVSHD 212
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHN 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-211 |
4.68e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.80 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLAL---LAGINTPS--SGNIRILNRDLNTLSNTQRDVFRaeNIGYIFQNFNLLPYLTP 99
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIYSPDVDPIEVRR--EVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 100 IENVTLGCEFSK-SRKQKALQQTTE---PKPSLQKEAIRLLtalglsepyhsKDVAS-LSIGQQQRVAAARAFIGSPELI 174
Cdd:PRK14267 103 YDNVAIGVKLNGlVKSKKELDERVEwalKKAALWDEVKDRL-----------NDYPSnLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 490726575 175 IADEPTSALDTANRESFIKLLFEQAKraNSTLVFVSH 211
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTH 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
7.83e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.04 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhkNDAKPT----LNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsNTQRD 77
Cdd:PRK13651 3 IKVKNIVKIF--NKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKN--KKKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 78 VFRAENIGYIFQnfnlLPYLTPIENVT-----LGCEFSKSRKQkALQQTTE------------PKPSLQKEAIRLLTALG 140
Cdd:PRK13651 79 EKEKVLEKLVIQ----KTRFKKIKKIKeirrrVGVVFQFAEYQ-LFEQTIEkdiifgpvsmgvSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 141 LSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKlLFEQAKRANSTLVFVSHD 212
Cdd:PRK13651 154 LDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE-IFDNLNKQGKTIILVTHD 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-212 |
1.05e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.86 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGInTPSSGNI-----RILNRDLNTLSNTQRDVFRAENIGYIFQNfnllP--YL 97
Cdd:COG4170 28 LTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPRERRKIIGREIAMIFQE----PssCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 98 TPIENV-----------TLGCEFSKSRKQKalqqttepkpslQKEAIRLLTALGLsePYHSKDVAS----LSIGQQQRVA 162
Cdd:COG4170 103 DPSAKIgdqlieaipswTFKGKWWQRFKWR------------KKRAIELLHRVGI--KDHKDIMNSypheLTEGECQKVM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490726575 163 AARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-211 |
1.16e-14 |
|
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: 72.55 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhkNDAKPTLNIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFR 80
Cdd:TIGR02633 1 LLEMKGIVKTF--GGVKALDGI-DLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AeNIGYIFQNFNLLPYLTPIENVTLGCEFSksrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEPYHSKDVASLSIGQQQR 160
Cdd:TIGR02633 78 A-GIVIIHQELTLVPELSVAENIFLGNEIT-------LPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSH 211
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDII-RDLKAHGVACVYISH 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-212 |
1.28e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 30 GEHIFLHGPSGVGKSTL-LALLAGINTpSSGNIRILNRDLNTLSNTQRDVFRaENIGYIFQNfnllPYLTPIENVTLGCE 108
Cdd:PRK10261 350 GETLSLVGESGSGKSTTgRALLRLVES-QGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQD----PYASLDPRQTVGDS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 109 FSKSRKQKALQQTTEPkpslQKEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANR 188
Cdd:PRK10261 424 IMEPLRVHGLLPGKAA----AARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180
....*....|....*....|....
gi 490726575 189 ESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHD 523
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-227 |
1.44e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.35 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 37 GPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsntQRDVFRaENIGYIFQNFNLLPYLTPIENVTLGCEFsKSRKQK 116
Cdd:TIGR01257 963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVR-QSLGMCPQHNILFHHLTVAEHILFYAQL-KGRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 117 ALQqttepkpsLQKEAirLLTALGLSEPyHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLF 196
Cdd:TIGR01257 1037 EAQ--------LEMEA--MLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|.
gi 490726575 197 EQakRANSTLVFVSHDETLKPLFNRAISLVS 227
Cdd:TIGR01257 1106 KY--RSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-211 |
1.71e-14 |
|
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: 69.83 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqRDVFRa 81
Cdd:cd03244 3 IEFKNVSLR-YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQN---------FNLLPYltpienvtlgCEFSKSRKQKALQQTtepkpSLQKEAIRLLTALGLsepYHSKDVAS 152
Cdd:cd03244 78 SRISIIPQDpvlfsgtirSNLDPF----------GEYSDEELWQALERV-----GLKEFVESLPGGLDT---VVEEGGEN 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEqaKRANSTLVFVSH 211
Cdd:cd03244 140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAH 196
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-184 |
1.72e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.88 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 15 DAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRIlnrdlNTLSNTQRDvfRAENIGYIFQNFNLL 94
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-----DGKTATRGD--RSRFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 95 PYLTPIENVTLGCEFSKSRKQKAlqqttepkPSlqkeaiRLLTALGLSEpYHSKDVASLSIGQQQRVAAARAFIGSPELI 174
Cdd:PRK13543 95 ADLSTLENLHFLCGLHGRRAKQM--------PG------SALAIVGLAG-YEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|
gi 490726575 175 IADEPTSALD 184
Cdd:PRK13543 160 LLDEPYANLD 169
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
37-211 |
1.93e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 37 GPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTqrdvFRAENIGYIFQNFNllPYLTPIENVTLGCEFSksrkqk 116
Cdd:PRK15112 46 GENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS----YRSQRIRMIFQDPS--TSLNPRQRISQILDFP------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 117 aLQQTTEPKPSLQKEAIRL-LTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLL 195
Cdd:PRK15112 114 -LRLNTDLEPEQREKQIIEtLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLM 192
|
170
....*....|....*..
gi 490726575 196 FE-QAKRANSTLVFVSH 211
Cdd:PRK15112 193 LElQEKQGISYIYVTQH 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
24-180 |
2.74e-14 |
|
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: 69.63 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSnTQRdvfRAEN-IGYIFQNFNLLPYLTPIEN 102
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP-PHR---IARLgIGYVPEGRRIFPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 103 VTLGCEFSKSRKQ--KALQQTTEPKPSLqKEairLLTALGlsepyhskdvASLSIGQQQRVAAARAFIGSPELIIADEPT 180
Cdd:COG0410 99 LLLGAYARRDRAEvrADLERVYELFPRL-KE---RRRQRA----------GTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-211 |
2.84e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.20 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLN--TLSNTQrdvf 79
Cdd:PRK11176 342 IEFRNVTFTYPGKE-VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLR---- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 raENIGYIFQNFNLLPYlTPIENVTLGCEFSKSRKQKalqqttepkpslqKEAIRLLTALGLSEPY-HSKDV------AS 152
Cdd:PRK11176 417 --NQVALVSQNVHLFND-TIANNIAYARTEQYSREQI-------------EEAARMAYAMDFINKMdNGLDTvigengVL 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 153 LSIGQQQRVAAARAFI-GSPELIIaDEPTSALDTANRESFIKLLFEQAKraNSTLVFVSH 211
Cdd:PRK11176 481 LSGGQRQRIAIARALLrDSPILIL-DEATSALDTESERAIQAALDELQK--NRTSLVIAH 537
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-225 |
3.07e-14 |
|
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: 69.10 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 4 LDNVTFKwhkndakptlniptlrIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLsntqrdvfraeN 83
Cdd:cd03220 38 LKDVSFE----------------VPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----------G 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 84 IGYIFQnfnllPYLTPIENVTLGCEFS-KSRKQKAlqqttepkpslQKEA-IRLLTALG--LSEPyhskdVASLSIGQQQ 159
Cdd:cd03220 91 LGGGFN-----PELTGRENIYLNGRLLgLSRKEID-----------EKIDeIIEFSELGdfIDLP-----VKTYSSGMKA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRAnSTLVFVSHDE-TLKPLFNRAISL 225
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQG-KTVILVSHDPsSIKRLCDRALVL 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-212 |
3.25e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.66 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKndaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvfr 80
Cdd:PRK11231 2 TLRTENLTVGYGT---KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aenigyIFQNFNLLP--YLTPiENVT------------------LGCEfSKSRKQKALQQTtepkpSLQKEAIRLLTalg 140
Cdd:PRK11231 74 ------LARRLALLPqhHLTP-EGITvrelvaygrspwlslwgrLSAE-DNARVNQAMEQT-----RINHLADRRLT--- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 141 lsepyhskdvaSLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHD 212
Cdd:PRK11231 138 -----------DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLM-RELNTQGKTVVTVLHD 197
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-212 |
3.62e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.12 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVT--FKWHKNDA--KPTL---------------NIpTLRIDKGEHI-FLhGPSGVGKSTLLALLAGINTPSSGN 60
Cdd:COG4586 1 IIEVENLSktYRVYEKEPglKGALkglfrreyreveavdDI-SFTIEPGEIVgFI-GPNGAGKSTTIKMLTGILVPTSGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 61 IRILNRDlntlSNTQRDVFrAENIGYIF-QNFNLLPYLTPIENVTLgcefsksrkQKALQQTtePKPSLQKEAIRLLTAL 139
Cdd:COG4586 79 VRVLGYV----PFKRRKEF-ARRIGVVFgQRSQLWWDLPAIDSFRL---------LKAIYRI--PDAEYKKRLDELVELL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 140 GLsEPYHSKDVASLSIGQQQR--VAAarAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG4586 143 DL-GELLDTPVRQLSLGQRMRceLAA--ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-207 |
5.91e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.38 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhkNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntqRDVFRa 81
Cdd:PRK13657 335 VEFDDVSFSY--DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQN---FNllpyLTPIENVTLGC------EFSKSRKQKALQQTTEPKPSlqkeaiRLLTALGlsepyhsKDVAS 152
Cdd:PRK13657 409 RNIAVVFQDaglFN----RSIEDNIRVGRpdatdeEMRAAAERAQAHDFIERKPD------GYDTVVG-------ERGRQ 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDtANRESFIKLLFEQAKRANSTLV 207
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALD-VETEAKVKAALDELMKGRTTFI 525
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-212 |
6.10e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.42 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDA--KPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRIlnRDLNTLSNTQRDVF 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RA--ENIGYIFQnfnlLPYLTPIE-NVTLGCEFSKSRKQKALQQTTEpkpslqkEAIRLLTALGLSEPYHSKDVASLSIG 156
Cdd:PRK13646 81 RPvrKRIGMVFQ----FPESQLFEdTVEREIIFGPKNFKMNLDEVKN-------YAHRLLMDLGFSRDVMSQSPFQMSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490726575 157 QQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-215 |
6.83e-14 |
|
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: 67.46 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRidKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfRAENIGYIfqnfnllpyltpienv 103
Cdd:cd03215 22 EVR--AGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYV---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 tlgcefSKSRKQKALqqttepkpsLQKEAIRLLTALGlsepyhskdvASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:cd03215 81 ------PEDRKREGL---------VLDLSVAENIALS----------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190
....*....|....*....|....*....|...
gi 490726575 184 DTANRESFIKLLFEQAKRANSTLVFVS-HDETL 215
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVLLISSeLDELL 168
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-213 |
6.96e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.00 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKN--DAKPtLNiptLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRIlnrDLNTLSNTQRDVF 79
Cdd:PRK10522 323 LELRNVTFAYQDNgfSVGP-IN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL---DGKPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 RAEnIGYIFQNFNLLPYLtpienvtLGcefsksrkqkalQQTTEPKPSLqkeAIRLLTALGLSEPYHSKD----VASLSI 155
Cdd:PRK10522 396 RKL-FSAVFTDFHLFDQL-------LG------------PEGKPANPAL---VEKWLERLKMAHKLELEDgrisNLKLSK 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 156 GQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDE 213
Cdd:PRK10522 453 GQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD 510
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-223 |
1.58e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.31 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 30 GEHIFLHGPSGVGKSTLLALLAGINTPS---SGNIRILNRDLNtlsntqRDVFRAENiGYIFQNFNLLPYLTPIENVT-- 104
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID------AKEMRAIS-AYVQQDDLFIPTLTVREHLMfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 105 ----LGCEFSKSRKQKALQQttepkpslqkeairLLTALGLSEPYHSK-----DVASLSIGQQQRVAAARAFIGSPELII 175
Cdd:TIGR00955 124 ahlrMPRRVTKKEKRERVDE--------------VLQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490726575 176 ADEPTSALDTANRESFIKLLFEQAKRAnSTLVFVSHDET--LKPLFNRAI 223
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKG-KTIICTIHQPSseLFELFDKII 238
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-211 |
1.58e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 69.37 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNtqrdVFRA 81
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH----HYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNfnllPYL---TPIENVTLGCEFSKSRKQKALQQTTEPKPSLQKEAIRLLTALGlsepyhsKDVASLSIGQQ 158
Cdd:TIGR00958 555 RQVALVGQE----PVLfsgSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVG-------EKGSQLSGGQK 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANResfiKLLFEQAKRANSTLVFVSH 211
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAH 672
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-212 |
1.87e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.96 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKS-TLLALLAGINTPS----SGNIRILNRD-LNTLSNTQRDVfRAENIGYIFQNfnLLPYL 97
Cdd:PRK15134 29 SLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESlLHASEQTLRGV-RGNKIAMIFQE--PMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 98 TPIENVtlgcefsksrkQKALQQTTEPKPSLQKEA-----IRLLTALGLSEPyhSKDVA----SLSIGQQQRVAAARAFI 168
Cdd:PRK15134 106 NPLHTL-----------EKQLYEVLSLHRGMRREAargeiLNCLDRVGIRQA--AKRLTdyphQLSGGERQRVMIAMALL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490726575 169 GSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHN 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-211 |
1.91e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 35 LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvfrAENIG-YIF-QNFNLLPYLTPIENVTLGCefskS 112
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-----AHQLGiYLVpQEPLLFPNLSVKENILFGL----P 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 113 RKQKALQQTTEpkpslqkeairLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESfi 192
Cdd:PRK15439 113 KRQASMQKMKQ-----------LLAALGCQLDLDSS-AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETER-- 178
|
170 180
....*....|....*....|..
gi 490726575 193 klLFEQAKRANST---LVFVSH 211
Cdd:PRK15439 179 --LFSRIRELLAQgvgIVFISH 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-201 |
2.41e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 30 GEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDlntlsntQRDVFRAENIGYI-FQNFnLLPYLTPIENVtlgcE 108
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-------IDDPDVAEACHYLgHRNA-MKPALTVAENL----E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 109 FsksrkQKALQQTTEPKPSlqkEAirlLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANR 188
Cdd:PRK13539 96 F-----WAAFLGGEELDIA---AA---LEAVGLAPLAHLP-FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170
....*....|...
gi 490726575 189 ESFIKLLFEQAKR 201
Cdd:PRK13539 164 ALFAELIRAHLAQ 176
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-188 |
3.09e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfraENIGYIFQNFNLLPYLTPIENV 103
Cdd:PRK13537 27 SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-----QRVGVVPQFDNLDPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLgceFSKSRKQKAlQQTTEPKPSLQKEAiRLltalglsEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:PRK13537 102 LV---FGRYFGLSA-AAARALVPPLLEFA-KL-------ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
....*
gi 490726575 184 DTANR 188
Cdd:PRK13537 170 DPQAR 174
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
30-212 |
3.10e-13 |
|
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: 66.78 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 30 GEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRD-----LNTLSNTQRDVFRAENIGYIFQNfnllpyltPIENVT 104
Cdd:TIGR02323 29 GEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLMRTEWGFVHQN--------PRDGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 105 LGCEFSKSRKQKALQQTTEPKPSLQKEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:TIGR02323 101 MRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLD 180
|
170 180
....*....|....*....|....*...
gi 490726575 185 TANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:TIGR02323 181 VSVQARLLDLLRGLVRDLGLAVIIVTHD 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
34-211 |
3.69e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.57 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 34 FLHGPSGVGKSTLLALLAGINTPSSGNIRI--------LNRDLNTLSNTQRDVFRAEN----IGYIFQNFNLLPYLTPIE 101
Cdd:PRK13631 56 FIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkKNNHELITNPYSKKIKNFKElrrrVSMVFQFPEYQLFKDTIE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 102 -NVTLGcefsksrkQKALQQttePKPSLQKEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPT 180
Cdd:PRK13631 136 kDIMFG--------PVALGV---KKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPT 204
|
170 180 190
....*....|....*....|....*....|.
gi 490726575 181 SALDTANRESFIKLLFEqAKRANSTLVFVSH 211
Cdd:PRK13631 205 AGLDPKGEHEMMQLILD-AKANNKTVFVITH 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-184 |
4.34e-13 |
|
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: 66.03 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfRAENIGYIFQNFNLLPYLTPIENV 103
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKR---ARLGIGYLPQEASIFRKLTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLgcefsksrkqkALQQTTEPKPSLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:cd03218 97 LA-----------VLEIRGLSKKEREEKLEELLEEFHITHLRKSK-ASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
.
gi 490726575 184 D 184
Cdd:cd03218 165 D 165
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-212 |
5.30e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 27 IDKGEHIFLHGPSGVGKSTLLALLAGInTPSSGNIRILNRDLNTLSNTQRDVFRAenigYIFQNFN---LLP---YLTpi 100
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRA----YLSQQQTppfAMPvfqYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 101 envtlgcefsksRKQKALQQTTEPKPSLQkeaiRLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFI-----GSPE--L 173
Cdd:PRK03695 92 ------------LHQPDKTRTEAVASALN----EVAEALGLDDKLGRS-VNQLSGGEWQRVRLAAVVLqvwpdINPAgqL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 490726575 174 IIADEPTSALDTANRESFIKLLFEQAkRANSTLVFVSHD 212
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHD 192
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-211 |
8.01e-13 |
|
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: 65.18 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSN-------- 73
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHkylhskvs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 74 --TQRDVFRA----ENIGYIFQnfnllpyltpienvtlGCEFSKSrkqKALQQTTEPKPSLQKEAIRLLTALGlsepyhs 147
Cdd:cd03248 92 lvGQEPVLFArslqDNIAYGLQ----------------SCSFECV---KEAAQKAHAHSFISELASGYDTEVG------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490726575 148 KDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRanSTLVFVSH 211
Cdd:cd03248 146 EKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAH 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-211 |
8.78e-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: 65.04 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNdaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRA 81
Cdd:cd03290 1 VQVTNGYFSWGSG--LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNfnllPYL---TPIENVTLGCEFSKSRkQKALQQTTEPKPSLQkeairlLTALGLSEPYHSKDVaSLSIGQQ 158
Cdd:cd03290 79 YSVAYAAQK----PWLlnaTVEENITFGSPFNKQR-YKAVTDACSLQPDID------LLPFGDQTEIGERGI-NLSGGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDT-----ANRESFIKLLfEQAKRansTLVFVSH 211
Cdd:cd03290 147 QRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFL-QDDKR---TLVLVTH 200
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-223 |
1.61e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.72 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDAKP-TL-------------------NIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGN 60
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSrSLkelllrrrrtrreefwalkDV-SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 61 IRILNR-----DLNTlsntqrdvfraeniGyifqnFNllPYLTPIENVTLGCE---FSKSRKQKALqqttepkpslqkEA 132
Cdd:COG1134 83 VEVNGRvsallELGA--------------G-----FH--PELTGRENIYLNGRllgLSRKEIDEKF------------DE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 133 IRLLTALG--LSEPyhskdVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRAnSTLVFVS 210
Cdd:COG1134 130 IVEFAELGdfIDQP-----VKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESG-RTVIFVS 203
|
250
....*....|....
gi 490726575 211 HD-ETLKPLFNRAI 223
Cdd:COG1134 204 HSmGAVRRLCDRAI 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-230 |
5.48e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 5 DNVTFKWHKNDAKPTLNIptlRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfrAENI 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTV---EIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV----ARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 85 GYIFQNFNLLPYLTPIENVTLGCE-----FSKSRKQkalqqttepkpslQKEAI-RLLTALGLSEpYHSKDVASLSIGQQ 158
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGRYphqplFTRWRKE-------------DEEAVtKAMQATGITH-LADQSVDTLSGGQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDetLKPLFNRAISLVSLQE 230
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHD--LNQACRYASHLIALRE 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-212 |
5.80e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.18 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTfkwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQR---- 76
Cdd:COG4604 1 MIEIKNVS---KRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELakrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 77 DVFRAENigyifqNFNLLpyLTPIENVTLGcEF--SKSRKQKALQQTTEpkpslqkEAIRLLTALGLSEPYhskdVASLS 154
Cdd:COG4604 78 AILRQEN------HINSR--LTVRELVAFG-RFpySKGRLTAEDREIID-------EAIAYLDLEDLADRY----LDELS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490726575 155 IGQQQrvaaaRAFIGspeLIIA--------DEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:COG4604 138 GGQRQ-----RAFIA---MVLAqdtdyvllDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-212 |
6.57e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 63.26 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 19 TLNIPTLRIDKgehiFLhGPSGVGKSTLLallagintpssgniRILNRdLNTLSNTQRD----VFRAEN----------- 83
Cdd:PRK14243 30 WLDIPKNQITA----FI-GPSGCGKSTIL--------------RCFNR-LNDLIPGFRVegkvTFHGKNlyapdvdpvev 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 84 ---IGYIFQNFNllPYLTPI-ENVTLGCEFS-----------KSRKQKALQQttEPKPSLQKEAIrlltalglsepyhsk 148
Cdd:PRK14243 90 rrrIGMVFQKPN--PFPKSIyDNIAYGARINgykgdmdelveRSLRQAALWD--EVKDKLKQSGL--------------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 149 dvaSLSIGQQQRVAAARAFIGSPELIIADEPTSALD---TANRESFIKLLFEQakranSTLVFVSHD 212
Cdd:PRK14243 151 ---SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDpisTLRIEELMHELKEQ-----YTIIIVTHN 209
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-213 |
9.07e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKndaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfr 80
Cdd:PRK13540 1 MLDVIELDFDYHD---QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQNFNLLPYLTPIENVTLGCEFSksrkqkalqqttepkpSLQKEAIRLLTALGLsEPYHSKDVASLSIGQQQR 160
Cdd:PRK13540 74 -KQLCFVGHRSGINPYLTLRENCLYDIHFS----------------PGAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVfVSHDE 213
Cdd:PRK13540 136 VALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLL-TSHQD 187
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-217 |
9.74e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 9.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRIlnrdlntlsntQRDVFRA 81
Cdd:TIGR00957 637 ITVHNATFTWARDLP-PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------KGSVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIfQNFNLLpyltpiENVTLGCEFSKSRKQKALqqttepkpslqkEAIRLLTALGLSEPYHSKDVA----SLSIGQ 157
Cdd:TIGR00957 705 PQQAWI-QNDSLR------ENILFGKALNEKYYQQVL------------EACALLPDLEILPSGDRTEIGekgvNLSGGQ 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490726575 158 QQRVAAARAFIGSPELIIADEPTSALDT-ANRESFIKLLFEQAKRANSTLVFVSHDETLKP 217
Cdd:TIGR00957 766 KQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGISYLP 826
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-212 |
1.17e-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: 63.42 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 37 GPSGVGKSTLLALLAGINTPSSGNIRIlnrdlntlsntQRDVfraeNIGYIFQNFNLLPYLTPIENVTLGC--------- 107
Cdd:TIGR03719 38 GLNGAGKSTLLRIMAGVDKDFNGEARP-----------QPGI----KVGYLPQEPQLDPTKTVRENVEEGVaeikdaldr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 108 -------------EFSK-SRKQKALQQ--------TTEPKPSLQKEAIRLltalglsePYHSKDVASLSIGQQQRVAAAR 165
Cdd:TIGR03719 103 fneisakyaepdaDFDKlAAEQAELQEiidaadawDLDSQLEIAMDALRC--------PPWDADVTKLSGGERRRVALCR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490726575 166 AFIGSPELIIADEPTSALDTanrESFIKLlfEQA-KRANSTLVFVSHD 212
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDA---ESVAWL--ERHlQEYPGTVVAVTHD 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-227 |
1.19e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSgnirilnrdlNTLSNTQRDVFRA 81
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE----------TSSVVIRGSVAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQnfnllpyLTPIENVTLGCEFSKSRKQKALQQTtepkpSLQKEaIRLLTALGLSEPyhSKDVASLSIGQQQRV 161
Cdd:PLN03232 685 PQVSWIFN-------ATVRENILFGSDFESERYWRAIDVT-----ALQHD-LDLLPGRDLTEI--GERGVNISGGQKQRV 749
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 162 AAARAFIGSPELIIADEPTSALDT-ANRESFIKLLFEQAKraNSTLVFVSHDETLKPLFNRAIsLVS 227
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELK--GKTRVLVTNQLHFLPLMDRII-LVS 813
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-216 |
1.82e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.33 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKP--TLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRI----LNRDLNTLSNTQ 75
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 76 RdvFRAEnIGYIFQNFNLLPYLTPIE-NVTLGCEFSKSRKQKALQQTTEpkpslqkeairLLTALGLSEPYHSKDVASLS 154
Cdd:PRK13645 87 R--LRKE-IGLVFQFPEYQLFQETIEkDIAFGPVNLGENKQEAYKKVPE-----------LLKLVQLPEDYVKRSPFELS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSH--DETLK 216
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHnmDQVLR 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-184 |
1.91e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAkptLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLntlsntqRD-VFR 80
Cdd:NF033858 2 ARLEGVSHRYGKTVA---LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-------ADaRHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AEN---IGYIFQNF--NLLPYLTPIENVTL-GCEFSKSRKQKAlQQTTEpkpslqkeairLLTALGLSePYHSKDVASLS 154
Cdd:NF033858 72 RAVcprIAYMPQGLgkNLYPTLSVFENLDFfGRLFGQDAAERR-RRIDE-----------LLRATGLA-PFADRPAGKLS 138
|
170 180 190
....*....|....*....|....*....|
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-183 |
2.37e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.43 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDAkptLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLnTLSNTQRdVFR 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQA---LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTAK-IMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aENIGYIFQNFNLLPYLTPIENVTLGCEF-SKSRKQKALQQTTEPKPSLQKEAIrlltalglsepyhsKDVASLSIGQQQ 159
Cdd:PRK11614 80 -EAVAIVPEGRRVFSRMTVEENLAMGGFFaERDQFQERIKWVYELFPRLHERRI--------------QRAGTMSGGEQQ 144
|
170 180
....*....|....*....|....
gi 490726575 160 RVAAARAFIGSPELIIADEPTSAL 183
Cdd:PRK11614 145 MLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-210 |
3.10e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEhIF--LhGPSGVGKSTLLALLAGINTPSSGNIRILNR--DLNTLSNTQRdvfraenIGYIFQNFNLLPYLTPI 100
Cdd:NF033858 287 FRIRRGE-IFgfL-GSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIATRRR-------VGYMSQAFSLYGELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 101 ENVTLGCE-FSKSRKQKAlqqttepkpslqkEAIR-LLTALGLsEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADE 178
Cdd:NF033858 358 QNLELHARlFHLPAAEIA-------------ARVAeMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
170 180 190
....*....|....*....|....*....|..
gi 490726575 179 PTSALDTANRESFIKLLFEQAKRANSTlVFVS 210
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSREDGVT-IFIS 454
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-215 |
4.84e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.77 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQ---RDVFRAenigyiFQNFNLLPYLTPIE 101
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRT------FQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 102 NVTLGC-EFSKSRKQKALQQTTEPKPSlQKEAIRL----LTALGLSEpYHSKDVASLSIGQQQRVAAARAFIGSPELIIA 176
Cdd:PRK11300 100 NLLVAQhQQLKTGLFSGLLKTPAFRRA-ESEALDRaatwLERVGLLE-HANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 490726575 177 DEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDETL 215
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-212 |
5.20e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 35 LHGPSGVGKSTLLALLAGINTPSSG-----NIRILNRDLNTLsntqRDV--FRaENIGYIFQNFNLLPyLTPIENVTLGC 107
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNY----RDVleFR-RRVGMLFQRPNPFP-MSIMDNVLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 108 EFSKSRKQKALQQTTEPKpslqkeairlLTALGLSEPYHSKDVAS---LSIGQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:PRK14271 126 RAHKLVPRKEFRGVAQAR----------LTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180
....*....|....*....|....*...
gi 490726575 185 TANRESFIKLLFEQAKRAnsTLVFVSHD 212
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRL--TVIIVTHN 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-212 |
5.30e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRilnrdlntlsntQRDVFR 80
Cdd:PRK09544 4 LVSLENVSVSF---GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aenIGYIFQNFNLLPYLtPIenvtlgcefsksrkqkALQQTTEPKPSLQKEAIrlLTALGLSEPYHSKD--VASLSIGQQ 158
Cdd:PRK09544 69 ---IGYVPQKLYLDTTL-PL----------------TVNRFLRLRPGTKKEDI--LPALKRVQAGHLIDapMQKLSGGET 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
37-217 |
6.60e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 37 GPSGVGKSTLLALLAGINTPSSGNIRILNRDLnTLSNTqRDVFRAenIGYIFQNFNLLPYLTPIE--------NVTLGCE 108
Cdd:PRK13652 37 GPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-TKENI-REVRKF--VGLVFQNPDDQIFSPTVEqdiafgpiNLGLDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 109 FSKSRKQKALQqttepkpslqkeairlltALGLSE-----PYHskdvasLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:PRK13652 113 TVAHRVSSALH------------------MLGLEElrdrvPHH------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190
....*....|....*....|....*....|....
gi 490726575 184 DTANRESFIKLLFEQAKRANSTLVFVSHDETLKP 217
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVP 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-212 |
7.90e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 6 NVTFKwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKS-TLLALLAGINTpSSGNIR----ILNR------DLNTLSNT 74
Cdd:PRK10261 19 NIAFM-QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQcdkmLLRRrsrqviELSEQSAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 75 QRDVFRAENIGYIFQNfnLLPYLTPIenVTLGCEFSKSRKqkaLQQTTEPKPSLqKEAIRLLTALGL--SEPYHSKDVAS 152
Cdd:PRK10261 97 QMRHVRGADMAMIFQE--PMTSLNPV--FTVGEQIAESIR---LHQGASREEAM-VEAKRMLDQVRIpeAQTILSRYPHQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 153 LSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHD 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-212 |
1.05e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.81 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 3 ELDNVTFKwhKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfRAE 82
Cdd:COG3845 259 EVENLSVR--DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER---RRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 83 NIGYI---------FQNFNLLpyltpiENVTLGcEFSKSRKQKalqqttepKPSLQKEAIRLLtALGLSEPYhskDV--- 150
Cdd:COG3845 334 GVAYIpedrlgrglVPDMSVA------ENLILG-RYRRPPFSR--------GGFLDRKAIRAF-AEELIEEF---DVrtp 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726575 151 ------ASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANREsFI-KLLFEQAkRANSTLVFVSHD 212
Cdd:COG3845 395 gpdtpaRSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIE-FIhQRLLELR-DAGAAVLLISED 461
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-212 |
1.47e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.28 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSS-----GNIRILNRDLN----TLS 72
Cdd:PRK14258 8 IKVNNLSFYY---DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYerrvNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 73 NTQRDVfraeniGYIFQNFNLLPyLTPIENVTLGCEFSKSRKQKALQQTTEpkpslqkEAIRllTALGLSEPYHS--KDV 150
Cdd:PRK14258 85 RLRRQV------SMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVE-------SALK--DADLWDEIKHKihKSA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 151 ASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK14258 149 LDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-184 |
1.81e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfRAENIGYIFQNFNLLPYLTPIENV 103
Cdd:PRK10895 23 SLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHAR---ARRGIGYLPQEASIFRRLSVYDNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEFsksRKQKALQQTTEPKPSLQKE--AIRLLTALGlsepyhskdvASLSIGQQQRVAAARAFIGSPELIIADEPTS 181
Cdd:PRK10895 100 MAVLQI---RDDLSAEQREDRANELMEEfhIEHLRDSMG----------QSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
...
gi 490726575 182 ALD 184
Cdd:PRK10895 167 GVD 169
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
25-184 |
1.95e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 59.86 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvfraenigyIFQNFNLLPyltpiENVT 104
Cdd:PRK09536 24 LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA-----------ASRRVASVP-----QDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 105 LGCEFSksrkqkaLQQTTE-----------PKPSLQKEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPEL 173
Cdd:PRK09536 88 LSFEFD-------VRQVVEmgrtphrsrfdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170
....*....|.
gi 490726575 174 IIADEPTSALD 184
Cdd:PRK09536 161 LLLDEPTASLD 171
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-197 |
2.52e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINtPS---SGNIrILNRDLNTLSNTqRDVfRAENIGYIFQNFNLLPYLTPI 100
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEI-LFDGEVCRFKDI-RDS-EALGIVIIHQELALIPYLSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 101 ENVTLGCEfsksRKQKAL---QQTTepkpslqKEAIRLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIAD 177
Cdd:NF040905 97 ENIFLGNE----RAKRGVidwNETN-------RRARELLAKVGLDESPDTL-VTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180
....*....|....*....|
gi 490726575 178 EPTSALDTANRESFIKLLFE 197
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLE 184
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-207 |
3.60e-10 |
|
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: 59.06 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFkwHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLsnTQRDVFRA 81
Cdd:COG5265 358 VRFENVSF--GYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV--TQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 enIGYIFQN---FNLlpylTPIENVTLGcefsksrKQKALQQTTEpkpslqkEAIRLltA------LGLSEPYHS----- 147
Cdd:COG5265 434 --IGIVPQDtvlFND----TIAYNIAYG-------RPDASEEEVE-------AAARA--AqihdfiESLPDGYDTrvger 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 148 --KdvasLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANrESFIKLLFEQAKRANSTLV 207
Cdd:COG5265 492 glK----LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT-ERAIQAALREVARGRTTLV 548
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-212 |
5.09e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTP----SSGNIRILNRDLNTLSNTQRDVFRAENIGYIFQNfnllPY--L 97
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE----PQscL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 98 TPIENVtlGCEFSKS-----RKQKALQQTTEPKpslqKEAIRLLTALGLSEPyhsKDVAS-----LSIGQQQRVAAARAF 167
Cdd:PRK15093 103 DPSERV--GRQLMQNipgwtYKGRWWQRFGWRK----RRAIELLHRVGIKDH---KDAMRsfpyeLTEGECQKVMIAIAL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490726575 168 IGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHD 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
8-184 |
7.81e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.19 E-value: 7.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 8 TFKWHKNDaKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLsntQRDVFRAEnigyi 87
Cdd:PRK10789 320 QFTYPQTD-HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSR----- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 88 FQNFNLLPYL---TPIENVTLGCEfsksrkqKALQQTTEpkpslqkEAIRLLTA----LGLSEPYHSkDVAS----LSIG 156
Cdd:PRK10789 391 LAVVSQTPFLfsdTVANNIALGRP-------DATQQEIE-------HVARLASVhddiLRLPQGYDT-EVGErgvmLSGG 455
|
170 180
....*....|....*....|....*...
gi 490726575 157 QQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVD 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-212 |
9.47e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 9.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 18 PTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIrILNRDLnTLSNTQRDVFRAENiGYIFQnfnllpYL 97
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDL-IVARLQQDPPRNVE-GTVYD------FV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 98 TpiENVTLGCEFSKSRKQKALQQTTEPKPSLQKEAIRL-------------------LTALGLSEpyhSKDVASLSIGQQ 158
Cdd:PRK11147 88 A--EGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLqeqldhhnlwqlenrinevLAQLGLDP---DAALSSLSGGWL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLfeqaKRANSTLVFVSHD 212
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHD 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
25-184 |
1.38e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.19 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfrAEN-IGY------IFQNfnllpyL 97
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKR----ARLgIGYlpqeasIFRK------L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 98 TPIENVTLgcefsksrkqkALQQTTEPKPSLQKEAIRLLTALGLSEPYHSKDVaSLSIGQQQRVAAARAFIGSPELIIAD 177
Cdd:COG1137 94 TVEDNILA-----------VLELRKLSKKEREERLEELLEEFGITHLRKSKAY-SLSGGERRRVEIARALATNPKFILLD 161
|
....*..
gi 490726575 178 EPTSALD 184
Cdd:COG1137 162 EPFAGVD 168
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-212 |
1.46e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 4 LDNVTFKWhkndAKPTLNIP-TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTqrdVFrAE 82
Cdd:PRK10575 14 LRNVSFRV----PGRTLLHPlSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AF-AR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 83 NIGYIFQNFNLLPYLTPIENVTLG--------CEFSKSRKQKAlqqttepkpslqKEAIRLltaLGLsEPYHSKDVASLS 154
Cdd:PRK10575 86 KVAYLPQQLPAAEGMTVRELVAIGrypwhgalGRFGAADREKV------------EEAISL---VGL-KPLAHRLVDSLS 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-211 |
2.11e-09 |
|
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: 57.33 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTfKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsntqrdvfr 80
Cdd:TIGR01257 1937 ILRLNELT-KVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT---------- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 aeNIGYIFQNFNLLPYLTPIENVTLGCE----FSKSRKQkalqqttePKPSLQKEAIRLLTALGLSePYHSKDVASLSIG 156
Cdd:TIGR01257 2006 --NISDVHQNMGYCPQFDAIDDLLTGREhlylYARLRGV--------PAEEIEKVANWSIQSLGLS-LYADRLAGTYSGG 2074
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 157 QQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFeQAKRANSTLVFVSH 211
Cdd:TIGR01257 2075 NKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV-SIIREGRAVVLTSH 2128
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-225 |
2.21e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRIlnrdlntlsntqrdvfrA 81
Cdd:PRK15064 320 LEVENLTKGF---DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-----------------S 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 EN--IGYIFQN----FNllpyltpiENVTLGCEFSKSRKQKALQQttepkpslqkeAIR-LLTALGLSEPYHSKDVASLS 154
Cdd:PRK15064 380 ENanIGYYAQDhaydFE--------NDLTLFDWMSQWRQEGDDEQ-----------AVRgTLGRLLFSQDDIKKSVKVLS 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726575 155 IGQQQRVAAARAFIGSPELIIADEPTSALDTANRESfIKLLFEQAKranSTLVFVSHD-ETLKPLFNRAISL 225
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIES-LNMALEKYE---GTLIFVSHDrEFVSSLATRIIEI 508
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-212 |
2.36e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.17 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 11 WHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsnTQRDVFR-AENIGYIFQ 89
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY---SKRGLLAlRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 90 NFNLLPYLTPIENvtlGCEFSksrkqkaLQQTTEPKPSLQK---EAIRLLTALGlsepYHSKDVASLSIGQQQRVAAARA 166
Cdd:PRK13638 85 DPEQQIFYTDIDS---DIAFS-------LRNLGVPEAEITRrvdEALTLVDAQH----FRHQPIQCLSHGQKKRVAIAGA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490726575 167 FIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANStLVFVSHD 212
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHD 195
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-211 |
3.11e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLL-ALLAGINTPSSGNIRILNRdlntlsntqrdVFR 80
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRGT-----------VAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AENIGYIFQnfnllpyLTPIENVTLGCEFSKSRKQKALQQTtepkpSLQKEaIRLLTALGLSEpYHSKDVaSLSIGQQQR 160
Cdd:PLN03130 684 VPQVSWIFN-------ATVRDNILFGSPFDPERYERAIDVT-----ALQHD-LDLLPGGDLTE-IGERGV-NISGGQKQR 748
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDT-ANRESFIKLLFEQAKRANSTLV-----FVSH 211
Cdd:PLN03130 749 VSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVtnqlhFLSQ 805
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-212 |
6.89e-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: 54.68 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 8 TFKWHKndakptlnIPTLRIdkGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIrilnrDLNTLSNTQRDVFRaeniGYI 87
Cdd:cd03236 14 SFKLHR--------LPVPRE--GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF-----DDPPDWDEILDEFR----GSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 88 FQNfnllpYLTPIENVTLGC--------EFSKSRKQKALQQTTEPKPSLQKEaiRLLTALGLsEPYHSKDVASLSIGQQQ 159
Cdd:cd03236 75 LQN-----YFTKLLEGDVKVivkpqyvdLIPKAVKGKVGELLKKKDERGKLD--ELVDQLEL-RHVLDRNIDQLSGGELQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490726575 160 RVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVfVSHD 212
Cdd:cd03236 147 RVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLV-VEHD 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
35-211 |
6.96e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 35 LHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfrAEN-IGYIFQNFNLLPYLTPIENVTLGcefsksR 113
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA----LENgISMVHQELNLVLQRSVMDNMWLG------R 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 114 KQKALQQTTEPKpsLQKEAIRLLTALGLSEPYHSKdVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIK 193
Cdd:PRK10982 99 YPTKGMFVDQDK--MYRDTKAIFDELDIDIDPRAK-VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT 175
|
170
....*....|....*...
gi 490726575 194 LLfEQAKRANSTLVFVSH 211
Cdd:PRK10982 176 II-RKLKERGCGIVYISH 192
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-215 |
1.06e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.75 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDAK-PTLNIptlRIDKGEHIFLHGPSGVGKSTLLALLAGInTPSSGNIRILNRDlntlsntqrdvf 79
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLiESLSF---EVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTKPAK------------ 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 80 raENIGYIFQNfnllPYLTpieNVTL--------GCE--FSKSRKQKALQQTTEpkpSLQKEAIrLLTALGLSEPYHSKD 149
Cdd:TIGR00954 515 --GKLFYVPQR----PYMT---LGTLrdqiiypdSSEdmKRRGLSDKDLEQILD---NVQLTHI-LEREGGWSAVQDWMD 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490726575 150 VasLSIGQQQRVAAARAFIGSPELIIADEPTSALdTANRESFIkllFEQAKRANSTLVFVSHDETL 215
Cdd:TIGR00954 582 V--LSGGEKQRIAMARLFYHKPQFAILDECTSAV-SVDVEGYM---YRLCREFGITLFSVSHRKSL 641
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-214 |
1.83e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 34 FLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQrdvfraenIGYIFQNFNLLPYLTPIENVTLGCEFSKSr 113
Cdd:PRK13541 30 YIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--------CTYIGHNLGLKLEMTVFENLKFWSEIYNS- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 114 kqkalqqtTEPKPSlqkeAIRLLTALGLSepyhSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIK 193
Cdd:PRK13541 101 --------AETLYA----AIHYFKLHDLL----DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN 164
|
170 180
....*....|....*....|...
gi 490726575 194 LLfeqAKRANS--TLVFVSHDET 214
Cdd:PRK13541 165 LI---VMKANSggIVLLSSHLES 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-214 |
2.56e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 29 KGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNrdlntlsntqrdvfraenigyifqnfnllpyltpienvtlgce 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 109 fsksrkqkalqqttepkpslqKEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANR 188
Cdd:smart00382 38 ---------------------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
|
170 180 190
....*....|....*....|....*....|.
gi 490726575 189 -----ESFIKLLFEQAKRANSTLVFVSHDET 214
Cdd:smart00382 97 allllLEELRLLLLLKSEKNLTVILTTNDEK 127
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-215 |
3.46e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 27 IDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNirilnrdlntlsntqrdVFRAENIGY-IFQNFNLLpyltpienvtl 105
Cdd:PLN03073 532 IDLDSRIAMVGPNGIGKSTILKLISGELQPSSGT-----------------VFRSAKVRMaVFSQHHVD----------- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 106 GCEFSKSrkqkALQQTTEPKPSLQKEAIRL-LTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:PLN03073 584 GLDLSSN----PLLYMMRCFPGVPEQKLRAhLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180 190
....*....|....*....|....*....|...
gi 490726575 185 TANRESFIK--LLFEQAkranstLVFVSHDETL 215
Cdd:PLN03073 660 LDAVEALIQglVLFQGG------VLMVSHDEHL 686
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-185 |
3.73e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.34 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 17 KPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAG-INTPS-SGNIRILNRDLntlsnTQRDVFRaenIGYIFQNFNLL 94
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANNRKP-----TKQILKR---TGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 95 PYLTPIENVTLgceFSKSRKQKALqqTTEPKPSLQKEAIrllTALGLSEPYHS----KDVASLSIGQQQRVAAARAFIGS 170
Cdd:PLN03211 153 PHLTVRETLVF---CSLLRLPKSL--TKQEKILVAESVI---SELGLTKCENTiignSFIRGISGGERKRVSIAHEMLIN 224
|
170
....*....|....*
gi 490726575 171 PELIIADEPTSALDT 185
Cdd:PLN03211 225 PSLLILDEPTSGLDA 239
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-212 |
5.25e-08 |
|
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: 52.03 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 19 TLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDlntlsntqrdvfraenIGYIFQnfnllpYLT 98
Cdd:cd03237 14 TLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT----------------VSYKPQ------YIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 99 PIENVTLGcEFSKSRKQKALQQttepkPSLQKEairLLTALGLsEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADE 178
Cdd:cd03237 72 ADYEGTVR-DLLSSITKDFYTH-----PYFKTE---IAKPLQI-EQILDREVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190
....*....|....*....|....*....|....
gi 490726575 179 PTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHD 175
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
37-212 |
5.34e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.85 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 37 GPSGVGKSTLLALLAGINTPSSGNIRILNR-----DLNTLSNTQ-RDVFRAEnIGYIFQN--FNLLPYLTPIENV----- 103
Cdd:PRK11701 39 GESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAErRRLLRTE-WGFVHQHprDGLRMQVSAGGNIgerlm 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 104 TLGCEFSKSRKQKALQ--QTTEPKPSlqkeaiRLltalglsepyhsKDV-ASLSIGQQQRVAAARAFIGSPELIIADEPT 180
Cdd:PRK11701 118 AVGARHYGDIRATAGDwlERVEIDAA------RI------------DDLpTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
170 180 190
....*....|....*....|....*....|..
gi 490726575 181 SALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK11701 180 GGLDVSVQARLLDLLRGLVRELGLAVVIVTHD 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-211 |
6.32e-08 |
|
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: 51.26 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntQRDVFRA 81
Cdd:cd03369 7 IEVENLSVRY-APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP--LEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 enIGYIFQNfnllPYLtpienvtlgceFSKSrkqkaLQQTTEPKPSLQKEAIRllTALGLSEpyhskDVASLSIGQQQRV 161
Cdd:cd03369 84 --LTIIPQD----PTL-----------FSGT-----IRSNLDPFDEYSDEEIY--GALRVSE-----GGLNLSQGQRQLL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 162 AAARAFIGSPELIIADEPTSALDTAN--------RESFikllfeqakrANSTLVFVSH 211
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATdaliqktiREEF----------TNSTILTIAH 182
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-207 |
6.33e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.81 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWHknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNtlsntqrDVFRA 81
Cdd:PRK15056 7 IVVNDVTVTWR--NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-------QALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 82 ENIGYIFQNFNL---LPYLtpIENVTLGCEFSKsrkqkaLQQTTEPKPSLQKEAIRLLTALGLSEpYHSKDVASLSIGQQ 158
Cdd:PRK15056 78 NLVAYVPQSEEVdwsFPVL--VEDVVMMGRYGH------MGWLRRAKKRDRQIVTAALARVDMVE-FRHRQIGELSGGQK 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490726575 159 QRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLV 207
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLV 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-212 |
7.58e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 3 ELDNVTFKWhknDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRIlnrdlntlsNTQRDV---- 78
Cdd:PRK11147 321 EMENVNYQI---DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC---------GTKLEVayfd 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 -FRAEnigyifqnfnLLPYLTPIENVTLGcefsKS------RKQKALQQTTE----PKpslqkeaiRLLTAlglsepyhs 147
Cdd:PRK11147 389 qHRAE----------LDPEKTVMDNLAEG----KQevmvngRPRHVLGYLQDflfhPK--------RAMTP--------- 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 148 kdVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANREsfikLLFEQAKRANSTLVFVSHD 212
Cdd:PRK11147 438 --VKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE----LLEELLDSYQGTVLLVSHD 496
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
148-216 |
8.00e-08 |
|
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: 51.07 E-value: 8.00e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 148 KDVASLSIgqqqRVAAARAFIGSPELIIADEPTSALDTANRE-SFIKLLFEQAKRANSTLVFVSHDETLK 216
Cdd:cd03240 121 KVLASLII----RLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFQLIVITHDEELV 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-211 |
8.08e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 8.08e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490726575 152 SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTaNRESFI-KLLFEQAKRANSTLVFVSH 211
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIeKTIVDIKDKADKTIITIAH 1417
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-210 |
8.89e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 27 IDKGEHIFLHGPSGVGKSTLLALLAGiNT-----PSSGNIRILNRDLNTLSNTqrdvFRAENIgYIFQNFNLLPYLTPIE 101
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAS-NTdgfhiGVEGVITYDGITPEEIKKH----YRGDVV-YNAETDVHFPHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 102 nvTLgcEFSksrkqkALQQTTEPKPSL-------QKEAIRLLTALGLSepyHSKD-------VASLSIGQQQRVAAARAF 167
Cdd:TIGR00956 158 --TL--DFA------ARCKTPQNRPDGvsreeyaKHIADVYMATYGLS---HTRNtkvgndfVRGVSGGERKRVSIAEAS 224
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490726575 168 IGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTlVFVS 210
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTT-PLVA 266
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-215 |
8.90e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 15 DAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPS--------SGNIRILNRDLNTLSNTQRDVFRAenigy 86
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRA----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 87 ifqnfnLLPY-------LTPIENVTLGCeFSKSRKQKALQQTTepkpslqKEAIRLLTALGLSEPYHSKDVASLSIGQQQ 159
Cdd:PRK13547 87 ------VLPQaaqpafaFSAREIVLLGR-YPHARRAGALTHRD-------GEIAWQALALAGATALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 160 RVAAARAF---------IGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHDETL 215
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNL 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
40-210 |
1.13e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 40 GVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfRAENIGY---------IFQNFNLLpyltpiENVTLGCeFS 110
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA---IRAGIAYvpedrkgegLVLDLSIR------ENITLAS-LD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 111 KSRKQKALQQTTEpkpslQKEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRES 190
Cdd:COG1129 358 RLSRGGLLDRRRE-----RALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAE 432
|
170 180
....*....|....*....|
gi 490726575 191 FIKLLFEQAKRaNSTLVFVS 210
Cdd:COG1129 433 IYRLIRELAAE-GKAVIVIS 451
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-212 |
6.16e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 37 GPSGVGKSTLLALLAGINTPSSGnirilnrdlntlsntqrDVFRAE--NIGYIFQNFNLLPYLTPIENVTLGCefsksRK 114
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVDKEFEG-----------------EARPAPgiKVGYLPQEPQLDPEKTVRENVEEGV-----AE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 115 QKALQQT--------TEPKPSLQK---------EAI-------------RLLTALGLSEPyhSKDVASLSIGQQQRVAAA 164
Cdd:PRK11819 98 VKAALDRfneiyaayAEPDADFDAlaaeqgelqEIIdaadawdldsqleIAMDALRCPPW--DAKVTKLSGGERRRVALC 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490726575 165 RAFIGSPELIIADEPTSALDTanrESFIKLlfEQA-KRANSTLVFVSHD 212
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDA---ESVAWL--EQFlHDYPGTVVAVTHD 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-212 |
6.93e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRidKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTlsNTQRDVFrAENIGYIFQNFN---LLPYLTPI 100
Cdd:PRK10762 274 TLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT--RSPQDGL-ANGIVYISEDRKrdgLVLGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 101 ENVTLGC--EFSK---SRKQKALQQTTEpkpslqkEAIRLLTalgLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELII 175
Cdd:PRK10762 349 ENMSLTAlrYFSRaggSLKHADEQQAVS-------DFIRLFN---IKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190
....*....|....*....|....*....|....*...
gi 490726575 176 ADEPTSALDT-ANREsfIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK10762 419 LDEPTRGVDVgAKKE--IYQLINQFKAEGLSIILVSSE 454
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-212 |
7.57e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 27 IDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGnirilnrdlntlsntqrDVFRAENIGYIFQnfnllpYLTPIENVTLg 106
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG-----------------EVDPELKISYKPQ------YIKPDYDGTV- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 107 cefsksrkQKALQQTTEPKPS--LQKEAIRlltALGLsEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:PRK13409 418 --------EDLLRSITDDLGSsyYKSEIIK---PLQL-ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
170 180
....*....|....*....|....*...
gi 490726575 185 TANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
5-216 |
9.30e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 48.31 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 5 DNVTFKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRdlntlsntqrdvfraenI 84
Cdd:cd03291 38 NNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------I 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 85 GYIFQNFNLLPYlTPIENVTLGCEFSKSRkQKALQQTTEPKPSLQKEAIRLLTALGlsepyhsKDVASLSIGQQQRVAAA 164
Cdd:cd03291 101 SFSSQFSWIMPG-TIKENIIFGVSYDEYR-YKSVVKACQLEEDITKFPEKDNTVLG-------EGGITLSGGQRARISLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490726575 165 RAFIGSPELIIADEPTSALDTANRESfiklLFEQAK---RANSTLVFV-SHDETLK 216
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDVFTEKE----IFESCVcklMANKTRILVtSKMEHLK 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-211 |
2.27e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 2 IELDNVTFKWhknDAKPTLNI---PTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIrILNrDLNTLSNTQRDV 78
Cdd:PTZ00265 383 IQFKNVRFHY---DTRKDVEIykdLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IIN-DSHNLKDINLKW 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 79 FRAE-----------------NIGYIFQNFNLLPYLTP-----------------------------IENVTLGCEFSKS 112
Cdd:PTZ00265 458 WRSKigvvsqdpllfsnsiknNIKYSLYSLKDLEALSNyynedgndsqenknkrnscrakcagdlndMSNTTDSNELIEM 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 113 RKQKALQQTTEPKPSLQKEAIRLLTAlGLSEPYHS---KDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRE 189
Cdd:PTZ00265 538 RKNYQTIKDSEVVDVSKKVLIHDFVS-ALPDKYETlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260
....*....|....*....|..
gi 490726575 190 SFIKLLFEQAKRANSTLVFVSH 211
Cdd:PTZ00265 617 LVQKTINNLKGNENRITIIIAH 638
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-201 |
3.87e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKwhkndAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNtlsntQRDVFR 80
Cdd:PRK10982 250 ILEVRNLTSL-----RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKIN-----NHNANE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AENIGY-----------IFQN----FNLLpyltpIENVtlgcefsKSRKQK-ALQQTTEPKPSLQkeaiRLLTALGLSEP 144
Cdd:PRK10982 320 AINHGFalvteerrstgIYAYldigFNSL-----ISNI-------RNYKNKvGLLDNSRMKSDTQ----WVIDSMRVKTP 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 145 YHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKR 201
Cdd:PRK10982 384 GHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK 440
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-212 |
5.30e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRdvfRAENIGYI---FQNFNLlpYL-TP 99
Cdd:PRK15439 283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQR---LARGLVYLpedRQSSGL--YLdAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 100 IE-NVtlgCEFSKSRKQKALQQTTEpkpslqkEAI--RLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIA 176
Cdd:PRK15439 358 LAwNV---CALTHNRRGFWIKPARE-------NAVleRYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190
....*....|....*....|....*....|....*.
gi 490726575 177 DEPTSALDTANRESFIKLLFEQAKRaNSTLVFVSHD 212
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSD 462
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-212 |
6.09e-06 |
|
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: 46.32 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 27 IDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNirilnrdlntlsntqrdVFRAENIGYIFQnfnllpYLTPIENVTLg 106
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE-----------------VDEDLKISYKPQ------YISPDYDGTV- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 107 cefsksrkQKALQQT-TEPKPS--LQKEAIRlltALGLsEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSAL 183
Cdd:COG1245 419 --------EEFLRSAnTDDFGSsyYKTEIIK---PLGL-EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190
....*....|....*....|....*....|..
gi 490726575 184 DTANRES---FIKLLFEQAKRanSTLVfVSHD 212
Cdd:COG1245 487 DVEQRLAvakAIRRFAENRGK--TAMV-VDHD 515
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
35-212 |
7.26e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 35 LHGPSGVGKSTLLALLAGINTPSSGNIRI-LNRDLNTLSNTQrdvfraenigYIFQNFNLlpyltpIENVTLG-CEFSKS 112
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQ----------FAFEEFTV------LDTVIMGhTELWEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 113 RKQK----ALQQTTEPK----PSLQKE------------AIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPE 172
Cdd:PRK15064 96 KQERdriyALPEMSEEDgmkvADLEVKfaemdgytaearAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490726575 173 LIIADEPTSALDTANresfIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK15064 176 ILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHD 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-195 |
9.16e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 35 LHGPSGVGKSTLLALLAGINTPS--SGNIRILN---RDlntlSNTQRdvfraeNIGYIFQNFNLLPYLTPIENVtlgcEF 109
Cdd:TIGR00956 794 LMGASGAGKTTLLNVLAERVTTGviTGGDRLVNgrpLD----SSFQR------SIGYVQQQDLHLPTSTVRESL----RF 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 110 SKSRKQKAlQQTTEPKPSLQKEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELII-ADEPTSALDTANR 188
Cdd:TIGR00956 860 SAYLRQPK-SVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
....*..
gi 490726575 189 ESFIKLL 195
Cdd:TIGR00956 939 WSICKLM 945
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-210 |
1.18e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.55 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 3 ELDNVTFKwhknDAKPTLNIpTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSntQRDVFRaE 82
Cdd:PRK09700 267 EVRNVTSR----DRKKVRDI-SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS--PLDAVK-K 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 83 NIGYI---------FQNFNLLpyltpiENVTLGCEFSKSRKQKALQQTTEPKPSLQKEAIRLLTALGLSEPyhSKDVASL 153
Cdd:PRK09700 339 GMAYItesrrdngfFPNFSIA------QNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSV--NQNITEL 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490726575 154 SIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVS 210
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSS 467
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
12-212 |
1.87e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 12 HKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRilnrdlntlsntqrdvfRAENIGYIFQNF 91
Cdd:PRK13546 32 HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAISA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 92 NLLPYLTPIENVTLGCeFSKSRKQKALQQTTePKpslqkeaIRLLTALGlsePYHSKDVASLSIGQQQRVAAARAFIGSP 171
Cdd:PRK13546 95 GLSGQLTGIENIEFKM-LCMGFKRKEIKAMT-PK-------IIEFSELG---EFIYQPVKKYSSGMRAKLGFSINITVNP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490726575 172 ELIIADEPTSALDTANRESFIKLLFEqAKRANSTLVFVSHD 212
Cdd:PRK13546 163 DILVIDEALSVGDQTFAQKCLDKIYE-FKEQNKTIFFVSHN 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-209 |
2.38e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTFKWHKNDakpTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRDLNTLSNTQRDVFR 80
Cdd:PRK10938 3 SLQISQGTFRLSDTK---TLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 81 AEnigyIFQNFNLlPYLTPIENvtlgcEFSKSRKQKALQQTTEPKPSLQKEAIRLLTALgLSEPYhskdvASLSIGQQQR 160
Cdd:PRK10938 80 SD----EWQRNNT-DMLSPGED-----DTGRTTAEIIQDEVKDPARCEQLAQQFGITAL-LDRRF-----KYLSTGETRK 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490726575 161 VAAARAFIGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFV 209
Cdd:PRK10938 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL-ASLHQSGITLVLV 191
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-212 |
2.68e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.92 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKS-TLLALL----AGINTpSSGNIRILNRDLNTLSntqrdvFRAENIGYIFQN----FNllp 95
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQ-TAGRVLLDGKPVAPCA------LRGRKIATIMQNprsaFN--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 96 yltPIENVTlgcefskSRKQKALQQTTepKPSLQKEAIRLLTALGLSEPyhsKDVASL-----SIGQQQRVAAARAFIGS 170
Cdd:PRK10418 94 ---PLHTMH-------THARETCLALG--KPADDATLTAALEAVGLENA---ARVLKLypfemSGGMLQRMMIALALLCE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490726575 171 PELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVSHD 212
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHD 200
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-208 |
3.12e-05 |
|
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: 43.41 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 9 FKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGIntpSSGNIRIlNRDL--NTLSNTQ-RDVFRAENIg 85
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSV-EGDIhyNGIPYKEfAEKYPGEII- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 86 YIFQNFNLLPYLTpienvtlgcefsksrkqkaLQQTTEPKPSLQKEAIrlltalglsepyhskdVASLSIGQQQRVAAAR 165
Cdd:cd03233 87 YVSEEDVHFPTLT-------------------VRETLDFALRCKGNEF----------------VRGISGGERKRVSIAE 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490726575 166 AFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVF 208
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFV 174
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
35-195 |
6.33e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 42.23 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 35 LHGPSGVGKSTLLALLAGINTPS--SGNIrilnrdlnTLSNTQRDVFRAENIGYIFQNFNLLPYLTPIENVtlgcEFSKs 112
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGRKTAGviTGEI--------LINGRPLDKNFQRSTGYVEQQDVHSPNLTVREAL----RFSA- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 113 rkqkalqqttepkpslqkeAIRlltalglsepyhskdvaSLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFI 192
Cdd:cd03232 105 -------------------LLR-----------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
...
gi 490726575 193 KLL 195
Cdd:cd03232 149 RFL 151
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-191 |
6.57e-05 |
|
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: 43.75 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 18 PTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILNRdlntlsntqrdvfraenIGYIFQNFNLLPYl 97
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWIMPG- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 98 TPIENVTLGCEFSKSRKQ---KALQQTTEPKPSLQKEAIRLLTAlGLsepyhskdvaSLSIGQQQRVAAARAFIGSPELI 174
Cdd:TIGR01271 502 TIKDNIIFGLSYDEYRYTsviKACQLEEDIALFPEKDKTVLGEG-GI----------TLSGGQRARISLARAVYKDADLY 570
|
170
....*....|....*...
gi 490726575 175 IADEPTSALD-TANRESF 191
Cdd:TIGR01271 571 LLDSPFTHLDvVTEKEIF 588
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-76 |
8.58e-05 |
|
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: 42.13 E-value: 8.58e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGIN--TPSSGNIRILNRDLNTLSNTQR 76
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEER 74
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-210 |
1.11e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.61 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 1 MIELDNVTfKWHK-NDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGInTP--SSGNIRILNRDLNTlsNTQRD 77
Cdd:PRK13549 259 ILEVRNLT-AWDPvNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGA-YPgrWEGEIFIDGKPVKI--RNPQQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 78 VFRAeNIGYIFQN---FNLLPYLTPIENVTLGC--EFSK-SRKQKALQQTTepkpsLQKEAIRLltALGLSEPYHSkdVA 151
Cdd:PRK13549 335 AIAQ-GIAMVPEDrkrDGIVPVMGVGKNITLAAldRFTGgSRIDDAAELKT-----ILESIQRL--KVKTASPELA--IA 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490726575 152 SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANStLVFVS 210
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVA-IIVIS 462
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
148-222 |
1.11e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726575 148 KDVASLSIgqqqRVAAARAFIGSPELIIADEPTSALDTANRES----FIKLLFEQAKRANSTLVFVSHDETLKPLFNRA 222
Cdd:TIGR00606 1205 KVLASLII----RLALAETFCLNCGIIALDEPTTNLDRENIESlahaLVEIIKSRSQQRNFQLLVITHDEDFVELLGRS 1279
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-225 |
1.35e-04 |
|
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: 41.19 E-value: 1.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 153 LSIGQQQRVAAA-----RAFIGSPeLIIADEPTSALDTANRESFIKLLFEQAKRaNSTLVFVSHDETLKPLFNRAISL 225
Cdd:cd03227 78 LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAELADKLIHI 153
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
150-210 |
1.74e-04 |
|
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: 42.12 E-value: 1.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490726575 150 VASLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFEQAKRANSTLVFVS 210
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSS 461
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
130-213 |
2.71e-04 |
|
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: 40.70 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 130 KEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAfIGSP---ELIIADEPTSALDTANRESFIKLLFEQAKRANsTL 206
Cdd:cd03270 115 RERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQ-IGSGltgVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TV 192
|
....*..
gi 490726575 207 VFVSHDE 213
Cdd:cd03270 193 LVVEHDE 199
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
118-225 |
4.20e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 118 LQQTTEPKPSLQ------KEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGspELI----IADEPTSAL---D 184
Cdd:PRK00635 436 LSQLPSKSLSIEevlqglKSRLSILIDLGLPYLTPERALATLSGGEQERTALAKHLGA--ELIgityILDEPSIGLhpqD 513
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490726575 185 TANRESFIKLLFEQAkranSTLVFVSHDETLKPLFNRAISL 225
Cdd:PRK00635 514 THKLINVIKKLRDQG----NTVLLVEHDEQMISLADRIIDI 550
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-63 |
5.76e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 5.76e-04
10 20
....*....|....*....|....*..
gi 490726575 37 GPSGVGKSTLLALLAGINTPSSGNIRI 63
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
24-65 |
7.02e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 38.67 E-value: 7.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490726575 24 TLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRILN 65
Cdd:cd00009 13 ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLN 54
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-63 |
1.26e-03 |
|
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: 39.53 E-value: 1.26e-03
10 20
....*....|....*....|....*..
gi 490726575 37 GPSGVGKSTLLALLAGINTPSSGNIRI 63
Cdd:TIGR03719 355 GPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
17-184 |
1.33e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 17 KPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGIN--TPSSGNIRILNRDLNTLSNTQRdvfRAENIGYIFQnfnll 94
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDR---AGEGIFMAFQ----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 95 pYLTPIENV-------TLGCEFSKSRKQKAL-----QQTTEPKPSLQKEAIRLLTalglsepyHSKDVAsLSIGQQQRVA 162
Cdd:PRK09580 86 -YPVEIPGVsnqfflqTALNAVRSYRGQEPLdrfdfQDLMEEKIALLKMPEDLLT--------RSVNVG-FSGGEKKRND 155
|
170 180
....*....|....*....|..
gi 490726575 163 AARAFIGSPELIIADEPTSALD 184
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLD 177
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
153-229 |
1.63e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 153 LSIGQqqRVAAARAF--------IGSPELIIADEPTSALDTANRESFIKLLfEQAKRANSTLVFVSHDETLKPLFNRAIS 224
Cdd:PRK03918 789 LSGGE--RIALGLAFrlalslylAGNIPLLILDEPTPFLDEERRRKLVDIM-ERYLRKIPQVIIVSHDEELKDAADYVIR 865
|
....*
gi 490726575 225 lVSLQ 229
Cdd:PRK03918 866 -VSLE 869
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-184 |
2.71e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 2.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490726575 127 SLQKEAIRLLTALGLSEPYHSKDVASLSIGQQQRVAAARAFIGSPELIIADEPTSALD 184
Cdd:PLN03073 319 TAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
152-212 |
3.29e-03 |
|
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: 37.17 E-value: 3.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490726575 152 SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANR---ESFIKLLFEQAKRansTLVFVSHD 212
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaARAIRRLSEEGKK---TALVVEHD 131
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-63 |
4.26e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 37.95 E-value: 4.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490726575 3 ELDNVTFKWHKNDAKPTLNIPTLRIDKGEHIFLHGPSGVGKSTLLALLAGINTPSSGNIRI 63
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
25-184 |
4.43e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 37.31 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 25 LRIDKGEHIFLHGPSGVGKSTLLALLAGinTPS----SGNIRILNRDLNTLSNTQRD---VFRAenigyiFQNFNLLPYL 97
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAhlgIFLA------FQYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 98 TPIENVTLGCefskSRKQKAlQQTTEPKPSLQKEAIR-LLTALGLSEPYHSKDV-ASLSIGQQQRVAAARAFIGSPELII 175
Cdd:CHL00131 100 SNADFLRLAY----NSKRKF-QGLPELDPLEFLEIINeKLKLVGMDPSFLSRNVnEGFSGGEKKRNEILQMALLDSELAI 174
|
....*....
gi 490726575 176 ADEPTSALD 184
Cdd:CHL00131 175 LDETDSGLD 183
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
152-211 |
8.60e-03 |
|
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: 36.43 E-value: 8.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726575 152 SLSIGQQQRVAAARAFIGSPELIIADEPTSALDTANRESFIKLLFeqAKRANSTLVFVSH 211
Cdd:cd03288 156 NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM--TAFADRTVVTIAH 213
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
32-81 |
9.81e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 35.01 E-value: 9.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 490726575 32 HIFLHGPSGVGKSTLL-ALLAGINTPSSGNIRILNRDLNTLSNTQRDVFRA 81
Cdd:pfam13401 7 ILVLTGESGTGKTTLLrRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRA 57
|
|
| |
